Nucleic acids that encode enhanced transaminase proteins

Abstract

The present invention relates to proteins having enhanced omega-transaminase (β-TA) activity, to nucleic acid molecules encoding respective proteins having enhanced β-TA activity, and to methods for the stereoselective synthesis of amino acids and chiral amines or for increasing isomers of chiral amines in mixtures of enantiomers.

Description

PROTEIN-ENCODING NUCLEIC ACIDS ENHANCED TRANSAMINASES The present invention relates to proteins having enhanced omegatransaminase (ω-ΤΑ) activity, to nucleic acid molecules encoding respective proteins having enhanced ω-ΤΑ activity, and to methods for the stereoselective synthesis of amino acids and chiral amines or for the increase of isomers of chiral amines in mixtures of enantiomers. Biocatalysis can be based on naturally available enzymes. More often, the desire to produce a specific product creates a demand for a specific enzyme, which is tailored to economically viable production of the desired product on a large scale. Enzyme engineering is an option to optimize enzymes toward the economical production of a given product. Amines and amino acids are ubiquitous in nature not only as parts of proteins and nucleic acids, but are also of great importance as neurotransmitters (e.g. adrenaline and histamine), as coenzyme precursors (e.g. coenzyme A cysteamine) or from complex lipids (eg, phosphatidylethanolamine ethanolamine). Especially the higher substituted amines pharmaceutically classified as alkaloids display an enormous variety of structures as well as biological effects found in various forms of life. The biological activities of amines, such as antibiotic, analgesic or neurotoxic activity, increase their potential as pharmaceuticals and, therefore, make them very promising candidates in the search for new drugs. The absolute configuration of the stereocenters of chiral amines is crucial for the interaction with biomolecules and therefore for the type of effect on biological systems. For the production of a desired target molecule, generating the correct chirality is often challenging. (Schaetzle, 2011, Opening Lecture, Ernst-Moritz-Arndt-University of Greifswald, Germany, “Identification, characterization and application of novel (R)selective amino transaminases”). Many of the active compounds in the pharmaceutical companies' portfolio are chiral. Optically active amines belong to important classes of compounds for the synthesis of many active agricultural and pharmaceutical products. L-phenylalanine, for example, is an important additive in animal feed. No commercially viable process for the chemical synthesis of enantiomerically pure amino acids is available. However, the chemical synthesis of racemic amino acids remains important, since the resolution of racemic mixtures into pure isomers is possible in some cases by means of biocatalytic processes. (Breuer et al., 2004, Angewandte Chemie International Issue 43, 788-824). Amino transaminases or ω-transaminases (ω-TAs) are biocatalysts of great importance for the production of chiral primary amines. ω-TAs catalyze the transfer of an amino group from an amino donor onto a carbonyl residue, using pyridoxal-5'-phosphate (PLP) as a cofactor. Therefore, the reaction mixture consists of two amines (an amino donor and a product) and two carbonyl compounds (a ketone substrate and a byproduct). Both SJ-selective and β-selective transaminases have so far been discovered and well described. The enzymes are highly stereoselective and thus have great potential for direct asymmetric amination, where chiral amines are generated with high enantiomeric excesses directly from an achiral ketone using inexpensive amino donors (Fesko et al., 2013, Rev. de Catálisis Molecular B, Enzimática 96, 103-110). Transaminases have gained attention in the biocatalytic synthesis of a wide variety of amino acids and chiral amines. Transaminases can be applied either in the kinetic resolution of racemic amino acids (removing one isomer from a mixture) or in asymmetric synthesis starting from the corresponding prochiral ketosubstrate. The transaminase-catalyzed reaction can be considered a redox reaction with oxidative deamination of the donor in conjunction with reductive amination of the acceptor. (Rudat et al., 2012, AMB Express 2:11). Cann et al. (2012, Investigación y Desarrollo de Procesos Orgánicos 16, 1953-1966) report the successful use of ω-transaminases for the stereoselective production of an α-aminoester, a precursor for the production of a migraine pharmaceutical. The advantages and disadvantages of chemical versus enzymatic synthesis are discussed. US 4,950,606 describes processes for the production of optically active amines. In this process, ω-transaminases from Bacillus megaterium and Pseudomonas putida convert prochiral ketones or ketoacids to amines via enantioselective transfer of an amino group from an amino donor. The (R)- and (S)- configuration of amines can be obtained. Park et al. (2013, Organic and Biomolecular Chemistry 11, 6929-6933) report the behavior of different transaminases in the enantioselective synthesis of unnatural amino acids from ketoacids using isopropylamine and various other compounds as amine donors. Park et al. (2013, QuímCatQuím 5, 1734-1738) demonstrate the feasibility of using (R)- or (S>selective ω-transaminases for the thermodynamically favorable asymmetric amination of prochiral alkyl ketones by using racemic arylalkylamines as an amino donor. in a one-pot reaction The reaction does not require the addition of excessive amounts of the amino donor or the removal of co-products. The use of racemic 2-propylamine, 1-propylamine, and 2-butylamine as reactions catalyzed by ω-transaminase amino donors has been shown to lead to up to three-fold higher conversions compared to reactions using alanine as the amino donor. Not me. The amino acids β-alanine and asparagine were deficient amino acid donors. For some methyl ketones containing an aromatic residue, optically pure amines were obtained in high yields when excess 2-butylamine or 1-phenylethylamine was used as the amino donor. No further steps were required to change the balance. (Fesko et al., 2013, Rev. of Molecular Catalysis B, Enzymatics 96,103-110) Shin & Kim (2001, Bioci. Biotecno. Biochem. 65(8), 1782-1788) disclose the isolation of ω-transaminases using arylamines including (S)-α-methylbenzylamine ((S)-a-MBA), 1-methyl -3-phenylpropyl-amine, 1-aminotetralin or 1-aminoindane as amine donor. Good amino acceptors were found to be the ketoacids pyruvate and glyoxylate or the aldehydes propionaldehyde and butaraldehyde. US 6,133,018 discloses the production of ('S>1-methoxy-2-aminopropane by contacting methoxyacetone and the achiral amino donor 2-aminopropane with ω-transaminase. A four-enzyme system for the production of D-amino acids via the conversion of a keto acid to the respective D-amino acid catalyzed by a D-amino acid aminotransferase (transaminase) using D-alanine as an amino donor is described in Galkin et al. (1997, Rev. of Fermentation and Bioengineering 83(3), 299-300). In order to drive the equilibrium of the reaction in the direction of D-amino acids, additional reactions were coupled to D-amino acid aminotransferase. Pyruvate and ammonia are converted to L-alanine via alanine dehydrogenase, simultaneously reducing NADH to NAD. Alanine racemase converts L-alanine to D-alanine. The recycling of NADH from NAD is established by the formation of carbon dioxide from formic acid catalyzed by formate dehydrogenase. Pyruvate is recycled from alanine via the D-amino acid aminotransferase reaction. The D-enantiomers of glutamate, leucine, norleucine, and methionine could be produced in high yield, while D-phenylalanine and D-tyrosine were synthesized in low yields, D-Norvaline could only be produced in 30% access, and aminobutyrate was only produced. as a racemic mixture. WO 2010 / 089171 A2 discloses methods for ammonizing at least one keto group to at least one keto group comprising a multicyclic ring system within an amino group in reactions catalyzed by enzymes having transaminase activity. WO 2015 / 195707 A1 (US2015361468 A1) discloses the production of blocks of QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ Construction of 5-carbon polymers by transgenic bacteria. Bacterial biosynthetic pathways are manipulated through the introduction of multiple enzymes including ω-transaminases. ω-Transaminases were shown to catalyze reactions from glutarate semi-aldehyde to 5-aminopentanoate and the reverse reaction, 5-aminopentanol to 5-oxopentanol, cadaverine to 5-aminopentanal, N5-acetyl-1,5-diaminopentane to N5-acetyl-5-aminopentanal . L-glutamate / 2-oxoglutaramate or L-alanine / pyruvate were used as amino donor / acceptor, respectively. KR 20030072067 discloses the isolation of a thermophilic T30 strain of Bacillus sp. comprising an L-selective aromatic amino acid transferase (transaminase) and the use of this strain as a biocatalyst for the production of aromatic L-amino acids at high reaction temperatures, thereby increasing the solubility of the keto acid substrate. Koszelewski et al. (2010, QuímCat Quím 2(1), 73-77, including Supporting Information) disclose the use of whole cell catalysts for the synthesis of enantiomerically pure amines from the corresponding prochiral amines and the resolution of racemic amines. Different ω-transaminases from Bacillus megaterium SC6394, Alcaligenes denitrificans Y2k-2, Chromobacterium violaceum DSM30191, the Vibrio fluvialis ω-transaminase mutant W57G and a mutant named CNB05-01, originating from an Arthrobacter species, were expressed in Escherichia coli cells. Lyophilized Escherichia coli cells were used for the stereoselective amination and kinetic resolution reactions. The range of products accessible through the use of transaminases is limited by the characteristics of most naturally occurring ω-transaminases in not accepting bulkier substrates than an ethyl group in a position adjacent to the ketone (Savile et al., 2010, Science 329, 305-309, including Supporting Information). Parketal. (2014, Sínt. y Catál. Avanz. 356, 212-220) discovered an fSJ-selective ω-transaminase from Paracoccus denitrificans that accepts substrates with substituents up to an n-butyl group (i.e., n-hexyl 2-oxohexanoate ), but did not accept branched-chain α-ketoacids. A variant (V153A) of the fSJ-selective ω-transaminase from Paracoccus denitrificans showed enhanced activity towards the linear keto acid (S)-1-phenylbutylamine but did not accept branched ketoacids. Variants of a mesophilic Arthrobacter citreus ω-transaminase comprising seventeen amino acid substitutions compared to the amino acid sequence of the respective wild-type sequence show improved thermostability and significantly improved specific activity in reactions producing fSJ-substituted aminotetralin from substituted tetralone in the presence of isopropylamine as amine donor. (Martin et al., 2007, Journal of Biochemical Engineering 37, 246-255). QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ Savile et al. (2010, Science 329, 305-309, including Supporting Information) disclose the manufacture of the complex antidiabetic pharmaceutical sitagliptin by a biocatalytic process involving an ω-transaminase. Several variants of an Arthrobacter sp. ωtransaminase (RJ-selective (ATA-117)) were produced. The enzymes show a wide range of substrates, increased tolerance to isopropylamine and organic solvents. These enzymes could produce various amines and substituted phenylamines Trifluoromethyl An optimized variant of an ω-transaminase (Fij-selective from Arthrobacter sp. (ATA-117) containing 27 amino acid substitutions compared to the wild-type enzyme was used to produce sitagliptin via amination of prositagliptin ketone in the presence of isopropylamine as an amine donor. WO 2006 / 06339 (US 7,247,460) discloses variants of ω-transaminases from Arthrobacter citerus which are heat stable, have a higher reaction rate and tolerance to high concentrations of amine donors, in each case compared to the respective enzyme from wild type. Although several improvements of transaminases have been achieved so far, limitations that arise during asymmetric amine synthesis or resolution of racemic amines, such as unfavorable equilibrium, substrate and product inhibition, poor thermostability, insufficient substrate specificity, and sometimes low enantioselectivity of transaminase, have yet to be overcome for efficient production of a wide range of amines on an industrial scale. Accordingly, there is a need for further improvement of ωtransaminases. In particular, with regard to the production of desired aminated, enantiomerically enriched or pure products, preferably under specific and / or economically viable production processes, additional improved ω-transaminases are needed. The present invention provides variants of ω-transaminases (ω-ΤΑ) comprising modifications in their amino acid sequence or additional modified ω-ΤΑ variants comprising additional modifications in their amino acid sequence, these variants and further modified variants comprising amino acid modifications additional ones that possess improved reaction kinetics, improved substrate acceptance and improved specific activity compared to the respective wild-type ω-TAs. The variants and variants comprising additional amino acid modifications of the invention therefore allow the development of economically efficient production processes for aminated products in methods of producing new aminated products or respective product precursors that cannot be achieved by means of the use of the respective wild-type ω-TAs. QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ Additional variants or modified variants of the ω-TAs described herein have advantages over known wild-type ω-TAs and others already known. In particular, the modified or variant ω-TAs described herein have the advantage that they can produce nearly pure or enantiomerically enantiomerically enriched or pure compounds, such as branched-chain or aromatic amino acids that cannot be produced with the respective ω-TAs. -wild-type transaminases. Further modified variants of the ω-ΤΑ described herein have the advantage that they can produce enantiomerically enriched, pure or nearly pure phosphoamino acid compounds. Positions 1 to 477 in SEQ ID NO 3 represent the amino acid sequence of a wild-type ω-transaminase (ω-ΤΑ) from Bacillus megaterium that is derived from GenPept (PDB) under Accession No 5G09_A. Positions 1 to 479 in SEQ ID NO 6 represent the amino acid sequence of a wild type ω-ΤΑ from Arthrobacter sp. which is derived from GenPept (PDB) under the 5G2P Access No. A. Positions 1 to 476 in SEQ ID NO 9 represent the amino acid sequence of a wild type ω-ΤΑ from Bacillus sp. (soil 76801D1 which is derived from GenPept (PDB) under Accession No. KRF52528.1. Positions 1 to 476 in SEQ ID NO 12 represent the amino acid sequence of a variant of ω-ΤΑ from Arthrobacter sp. which are derived from SEQ ID NO 16 in WO 2006 / 06336 A2. Positions 1 to 476 in SEQ ID NO 15 represent the amino acid sequence of a wild type ω-ΤΑ from Arthrobacter sp. which are derived from SEQ ID NO 2 in WO 2006 / 06336 A2. Proteins having ω-ΤΑ activity are described herein, wherein the amino acid sequences of these proteins represent variants of proteins known to have ω-ΤΑ activity. In particular, the amino acid sequence of proteins possessing the activity of an ω-ΤΑ described herein represents variants of the amino acid sequences represented by amino acids from positions 1 to 477 in SEQ ID NO 3 and / or represented by the amino acids from positions 1 to 479 in SEQ ID NO 6 and / or represented by amino acids from positions 1 to 476 in SEQ ID NO 9 and / or represented by amino acids from positions 1 to 476 in SEQ ID NO 12 and / or represented by the amino acids from positions 1 to 476 in SEQ ID NO 15, where in each of the amino acid sequences shown under SEQ ID NO 3, SEQ ID NO 6, SEQ ID NO 9, SEQ ID NO 12 and SEQ ID NO 15 at least the amino acids in positions 25, 64, 88, 157, 165, 169, 174, 187, 197, 239, 327, 328, 384, 389, 391,396, 410 QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ and 414 are different from those amino acids given at the respective amino acid position in each of the sequences shown under SEQ ID NO 3, SEQ ID NO 6, SEQ ID NO 9, SEQ ID NO 12 and SEQ ID NO 15, respectively. The abbreviation ω-ΤΑ is used and herein means ω-transaminase. The term "variant" as used herein means a subject matter that is different from the subject matter known in the art. With respect to proteins and nucleic acid molecules, variants are understood to encompass a nucleic acid sequence or an amino acid sequence, respectively, which deviates from known sequences accordingly but which encodes a protein having the same function. or that catalyzes the same reaction, for example, the function of encoding a protein that has the activity of an ω-ΤΑ. Deviation of the sequences of nucleic acid molecules and amino acid sequences from known nucleic acid sequences and protein sequences means that the sequences comprise nucleotide or amino acid substitutions (replacements) and / or deletions and / or insertions , respectively, by comparison with correspondingly known amino acid sequences or nucleic acid sequences. A first embodiment of the invention concerns proteins having the activity of an ω-ΤΑ, wherein the proteins are selected from the group consisting of a) proteins comprising the amino acid sequence from positions 1 to 477 as shown under SEQ ID NO 3 in addition to the fact that the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; b) proteins comprising the amino acid sequence from positions 1 to 479 as shown under SEQ ID NO 6 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from T and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; c) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 9 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; d) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 12 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from T, the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; e) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 15 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; f) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, even more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with any of the amino acid sequences shown under a), b), c), d), e) or f), given that in each case the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the corresponding amino acid at position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid corresponding to the position 197 is different from T or M and the amino acid corresponding to position 239 is different from S and the amino acid corresponding to position 327 is different from S and the amino acid corresponding to position 328 is different from V and the amino acid corresponding to the position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P. The meaning of the amino acid abbreviations A, C, D, E, F, G, Η, I, K, L, Μ, N, P, Q, R, S, T V, W, Y is derived in the present below from Table 4 under the paragraph subtitled Description of the Sequences. An amino acid corresponding to position x in a first amino acid sequence (for example, positions 64 in SEQ ID NO 3) means herein that an amino acid of a second amino acid sequence when compared to a first amino acid sequence appears at position x of the first amino acid sequence in a pairwise sequence alignment of the first amino acid sequence with the second amino acid sequence in case the amino acid numbering of the second amino acid sequence differs from the amino acid numbering of the first amino acid sequence. QL7 Lnn / L7í17 / E / Yli In the context of the present invention, the term identity with respect to sequence identity or sequences that are identical is to be understood as the number of identical amino acids or nucleotides shared over the entire length of the sequence by a first amino acid or acid sequence. nucleic acid with another (second) amino acid sequence or nucleic acid, respectively, expressed as a percentage. Sequence identity can be determined by aligning two amino acid sequences or two nucleotide sequences using global or local alignment algorithms contained, for example, in software known as GAP or BESTFIT or the Emboss Needle program. These softwares use the Needleman and Wunsch global alignment algorithm to align two sequences, over their entire length, maximizing the number of matches and minimizing the number of gaps. In general, the default or default parameters are used, with a gap creation penalty = 10 and a gap extension penalty = 0.5 (for both nucleotide and protein alignments). For nucleotides, the default scoring matrix used is DNAFULL and for proteins, the default scoring matrix is ​​Blosum62 (Henikoff & Henikoff, 1992, PNAS 89, 10915-10919). Sequence alignments and scores for percent sequence identity can be determined, for example, using software, such as EMBOSS, accessible from the EBI global website (ebi.ac.uk / Tools / emboss / ). Alternatively, sequence similarity or identity can be determined by searching databases (eg, EMBL, GenBank) using commonly known algorithms and output formats such as FASTA, BLAST, etc., but preferably, hits should be retrieved and aligned in pairs to finally determine sequence identity. Preferably, the identity with respect to a protein having the activity of an ω-ΤΑ is determined by means of comparisons with the amino acid sequence given under SEQ ID NO 18 and the identity with respect to a nucleic acid molecule encoding a protein having the activity of a ω-ΤΑ is determined by comparisons of the nucleic acid sequence given under SEQ ID NOs 16 or 17 with other proteins or nucleic acid molecules, respectively, with the aid of computer programs. If the sequences to be compared with each other are of different length, the identity will be determined by determining the identity in percent of the number of amino acids or nucleotides, respectively, that the shorter sequence shares with the longer sequence. Preferably, the identity is determined using the known and publicly available computer program ClustalW (Thompson et al., Nucleic Acid Research 22 (1994), 46734680). ClustalW is made publicly available by Julie Thompson (Thompson@EMBLHeidelberg.DE) and Toby Gibson (Gibson@EMBL-Heidelberg.DE), European Laboratory for QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ Molecular Biology, Meyerhofstrasse 1, D 69117 Heidelberg, Germany. ClustalW can also be downloaded from various Internet pages, including the IGBMC (Institute of Genetics and Molecular and Cellular Biology, B.P.163, 67404 lllkirch Cedex, France; ftp: / / ftp-igbmc.ustrasbg.fr / pub / ) and the EBI (ftp: / / ftp.ebi.ac.uk / pub / software / ) and all the Internet mirror pages of the EBI (European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom United). Preferably, use is made of the ClustalW version 1.8 software to determine the identity between the proteins described in the context of the present invention and other proteins. Here, the parameters should be set as follows: KTUPLE=1, TOPDIAG=5, WIND0W=5, PAIRGAP=3, GAPOPEN=10, GAPEXTEND=0.05, GAPDIST=8, MAXDIV=40, MATRIX=GONNET, ENDGAPS(OFF ), NOPGAP, NOHGAP. Preferably, use is made of the ClustalW version 1.8 software to determine the identity, for example, between the nucleotide sequence of the nucleic acid molecules described in the context of the present invention and the nucleotide sequence of other nucleic acid molecules. nucleic. Here, the parameters should be set as follows: KTUPLE=2, TOPDIAGS=4, PAIRGAP=5, DNAMATRIXJUB, GAPOPEN=10, GAPEXT=5, MAXDIV=40, TRANSITIONS: unweighted. Identity further means that there is a functional and / or structural equivalence between the nucleic acid molecules in question or the proteins encoded by them. Functional equivalence means that the sequences of nucleic acid molecules or that the amino acid sequences encode a protein that has the activity of an ω-ΤΑ. Nucleic acid molecules that are homologous to the molecules described above and that represent derivatives of these molecules are in general variants of these molecules that represent modifications that have the same biological function or that catalyze the same reaction, that is, that encode a protein. which has the activity of an ω-ΤΑ. They may be either naturally occurring variants, eg, sequences from other species, or mutations, where these mutations may have occurred naturally or were introduced by site-directed mutagenesis. In addition, the variants can be synthetically produced sequences. Allelic variants can be either naturally occurring variants or synthetically produced variants or variants generated by recombinant DNA techniques. However, with respect to the present invention, it is decisive that those variants encode proteins that have ω-ΤΑ activity and that they comprise the amino acid substitutions (replacements), deletions or insertions described herein that concern the proteins according to the invention. A special class of derivatives are, for example, nucleic acid molecules that QLZLnn / Lznz / E / Yi differ from the nucleic acid molecules described in the context of the present invention as a result of the degeneracy of the genetic code. According to the NC-IUBMB (Nomenclature Committee of the International Union of Biochemistry and Molecular Biology) transaminases (TAs) belong to the class of transferases (EC 2). Transferases are enzymes that transfer a group, for example, a methyl group or a glycosyl group, from one compound (generally considered a donor) to another compound (generally considered an acceptor). The group of transferases comprises enzymes that transfer nitrogenous groups (EC 2.6). The TAs-catalyzed reaction can formally be considered a redox reaction with the oxidative deamination of an (amine) donor in conjunction with the reductive amination of a carbonyl acceptor through the transfer of a -NH2 and -H group to a compound that contains a carbonyl group in exchange for the =0 of that group according to general equation (I) R1-CH(-NH2)-R2+ R3-CO-R4R1-CO-R2+ R3-CH(-NH2)-R4. The reverse reaction that is also catalyzed by TAs can be formally described according to the general equation (la) R1-CO-R2+ R3-CH(-NH2)-R4R1-CH(-NH2)-R2+ R3-CO-R4. TAs are pyridoxal 5'-phosphate (PLP) dependent enzymes. The only distinctive feature of TA-catalyzed reactions is the transfer of an amino group (via a well-established mechanism involving covalent substrate-coenzyme intermediates), justifying the assignment of these enzymes among transferases within a special subclass , designated transaminases or amino transferases (EC 2.6.1). TAs are furthermore commonly classified in the art as α-TAs and ω-TAs. This nomenclature is based on the relative position of the amino group of amino acids that is transferred by the respective TAs. With respect to amine carboxylic acids, α-TAs catalyze the transamination of amino groups from one to carbon only, where ω-TAs also act on ηο-α-amines and transfer the amino group distal from the respective substrate. (Shin et al., 2003, Applied Microbiology and Biotechnology 61,463-471). However, it is known in the art that some ω-TAs are capable of catalyzing the transamination of (primary) amine compounds that do not carry a carboxyl group (Rudat et al., 2012, AMB Express 2(11); Shin et al. ., 2003, Microbiol and Biotecnol Apile 61,463-471). If a protein has the activity of a TA, in particular an ω-ΤΑ can be detected with methods known and described in the art. An assay to detect ωΤΑ activity of proteins based on α-amino acid blue staining with CuSOVMeOH was developed by Hwang & Kim (2004, Microbial and Enzymatic Technology 34(5), 429-436). Truppo et al. (2009, Chem. Org. and Biomol. 7, 395-398) describe an assay for high throughput screening for ω-TAs based on a multi-enzyme cascade pH indicator assay and further QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ discloses a conventional HPLC analysis assay. It is not decisive which method is used to detect whether a protein according to the invention has the activity of a ω-ΤΑ. Preferably, in connection with the present invention, the method described under General Methods, point 4, is used to detect whether a protein according to the invention has the activity of an ω-ΤΑ, in particular, this method is used to detect whether a variant of ω-ΤΑ according to the invention has the activity of a ωΤΑ. With regard to ω-ΤΑ variants comprising additional amino acid modifications, preferably the method described under General Methods”, point 7, is used to detect whether a protein according to the invention has the activity of a ω-ΤΑ . In a preferred embodiment of the invention, the protein according to the invention is an fSJ-selective ω-ΤΑ. The term "SJ-selective" means in connection with the present invention that reductive amination of the (amine) acceptor according to general equation (I) produces the (S)-enantiomer in enantiomeric excess over the (TJJ-enantiomer). The reaction catalyzed by fSJ-selective ω-TAs can be formally described according to the general equation (II) R1-CH(-NH2)-R2+ R3-CO-R4R1-CO-R2+ R3-CH(( / SJ-NH2)-R\ The ω-ΤΑ variant proteins according to the invention may have additional amino acid modifications (amino acid substitutions, deletions or insertions) compared to the amino acid sequences described herein above with respect to the amino acid sequences shown under SEQ ID Nos. 3, 6, 9, 12 or 15. In addition to the ω-ΤΑ variants described herein above under a) or c), the amino acid sequence shown from position 1 to 477 under SEQ ID NO 3 or the amino acid sequence shown from position 1 to 477 under SEQ ID NO 9, respectively, may have additional amino acid substitutions at positions 2 and / or 48 and / or 164 and / or 242 and / or 245 and / or 311 and / or 353 and / or 424 and / or the amino acid sequence shown under SEQ ID NO 3 may have additional amino acid substitutions at positions 202 and / or 205 and / or 359 and / or 475 and / or 476 and / or a deletion of the amino acid at position 477 and / or the amino acid sequence shown under SEQ ID. NO 9 may have additional amino acid substitutions at positions 69 and / or 90 and / or 268 and / or 318 and / or 322 and / or 452. In addition to the ω-ΤΑ variants described above under points b) and d), each of the amino acid sequences shown from positions 1 to 479 under SEQ ID NO 6 or the amino acid sequences shown from positions 1 to 476 QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ under SEQ ID NO 12, respectively, may have additional amino acid substitutions at positions 46 and / or 60 and / or 185 and / or 186 and / or 195 and / or 205 and / or 252 and / or 268 and / or 409 and / or 436 and / or in the amino acid sequence shown under SEQ ID NO 6, the amino acids at positions 477 and / or 478 and / or 479 can be deleted. In addition to the ω-ΤΑ variants described above under e), the amino acid sequence shown from positions 1 to 476 under SEQ ID NO 15 may have additional amino acid substitutions at positions 48 and / or 164 and / or 242 and / or 245 and / or 255 and / or 424. A further embodiment of the invention therefore concerns proteins according to the invention comprising additional amino acid modifications, preferably those embodiments consist of proteins having the activity of an ω-ΤΑ, wherein the proteins are selected from the group integrated to a) proteins comprising the amino acid sequence from positions 1 to 477 as shown under SEQ ID NO 3 in addition to the fact that the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P and the amino acid at position 2 is different from S and the amino acid at position 48 is different from D and the amino acid at position 164 is different from Y and the amino acid at position 202 is different from D and the amino acid at position 205 is different from L and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 311 is different from L and the amino acid at position 353 is different from F and the amino acid at position 359 is different from D and the amino acid at position 424 is different from K and the amino acid at position 475 is different from A and the amino acid at position 476 is different from L and the amino acid at position 477 is deleted; b) proteins comprising the amino acid sequence from positions 1 to 479 as shown under SEQ ID NO 6 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and the amino acid at position 157 is different from T and the QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and amino acid at position 187 is different from S and the amino acid at position 197 is different from T and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P and the amino acid at position 46 is different from T and the amino acid at position 60 is different from C and the amino acid at position 185 is different from C and the amino acid at position 186 is different from S and the amino acid at position 195 is different from S and the amino acid at position 205 is different from Y and the amino acid at position 252 is different from V and the amino acid at position 268 is different from S and the amino acid at position 409 is different from R and amino acid at position 436 is different from A and amino acids at positions 477 and 478 and 479 are deleted; c) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 9 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P and the amino acid at position 2 is different from S and the amino acid at position 48 is different from D and the amino acid at position 69 is different from P and the amino acid at position 90 is different from S and the amino acid at position 164 is different from Y and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 268 is different from T and the amino acid at position 311 is different from L and the amino acid at position 318 is different from E and the amino acid at position 322 is different from R and the amino acid at position 353 is different from S and the amino acid at position 424 is different from K and the amino acid at position 452 is different from E; d) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 12 in addition to the amino acid at position 25 QLZLnn / Lznz / B / Yi is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and the amino acid at position 157 is different from T and the amino acid at position 165 is different from R and the amino acid at position 169 is different from V and the amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from T, the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P and the amino acid at position 46 is different from T and amino acid at position 60 is different from C and amino acid at position 185 is different from O and amino acid at position 186 is different from C and amino acid at position 195 is different from S and the amino acid at position 205 is different from Y and the amino acid at position 252 is different from V and the amino acid at position 268 is different from S and the amino acid at position 409 is different from R and the amino acid at position 436 it is different from A; e) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 15 plus the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and amino acid at position 157 is different from T and amino acid at position 165 is different from R and amino acid at position 169 is different from V and amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different of K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P and the amino acid at position 48 is different from D and the amino acid at position 164 is different from Y and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 255 is different from F and the amino acid at position 424 is different from K; f) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, even more preferably 96%, with particular preference 97%, with utmost preference 98% or with special preference 99% identical to any of the QLZLnn / Lznz / E / Yi amino acid sequences that are defined under a) (amino acid sequence from positions 1 to 477 as shown under SEQ ID NO 3) since the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid at position 197 is different from M and the amino acid corresponding to position 239 is different from S and the corresponding amino acid at position 327 is different from S and the corresponding amino acid at position 328 is different from V and the corresponding amino acid at position 384 is different from Y and the corresponding amino acid at position 389 is different of I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P and the amino acid corresponding to position 2 is different from S and the amino acid corresponding to position 48 is different from D and the amino acid corresponding to position 164 is different from Y and the amino acid corresponding to position 202 is different from D and the amino acid corresponding to position 205 is different from L and the amino acid corresponding to position 242 is different from A and the amino acid corresponding to position 245 is different from A and the amino acid corresponding to position 311 is different from L and the corresponding amino acid at position 353 is different from F and the amino acid corresponding to position 359 is different from D and the amino acid corresponding to position 424 is different from K and the amino acid corresponding to position 475 is different from A and the amino acid corresponding to the position 476 is different from L and the amino acid corresponding to position 477 is deleted; g) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, even more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with any of the amino acid sequences as defined under b) (positions 1 to 476 as shown under SEQ ID NO 6) given that the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the corresponding amino acid QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ at position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid at position 197 is different from T and the amino acid corresponding to position 239 is different from S and the amino acid corresponding to position 327 is different from S and the amino acid corresponding to position 328 is different from V and the amino acid corresponding to position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P and the amino acid at position 46 is different from T and the amino acid corresponding to position 60 is different from C and the amino acid corresponding to position 85 is different from C and the amino acid corresponding to position 186 is different from S and the amino acid corresponding to the position 195 is different from S and the amino acid corresponding to position 205 is different from Y and the amino acid corresponding to position 252 is different from V and the amino acid corresponding to position 268 is different from S and the amino acid corresponding to position 409 is different from R and the amino acid corresponding to position 436 is different from A and the amino acids corresponding to positions 477 and 478 and 479 are deleted; h) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, even more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with any of the amino acid sequences as defined under c) (positions 1 to 479 as shown under SEQ ID NO 9) given that the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid at position 197 is different of M and the amino acid corresponding to position 239 is different from S and the amino acid corresponding to position 327 is different from S and the amino acid corresponding to position 328 is different from V and the amino acid corresponding to position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P and the amino acid corresponding to position 2 is different QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ of S and the corresponding amino acid at position 48 is different from D and the corresponding amino acid at position 69 is different from P and the corresponding amino acid at position 90 is different from S and the corresponding amino acid at position 164 is different from Y and the amino acid corresponding to position 242 is different from A and the amino acid corresponding to position 245 is different from A and the amino acid corresponding to position 268 is different from T and the amino acid corresponding to the position 311 is different from L and the amino acid corresponding to position 318 is different from E and the amino acid corresponding to position 322 is different from R and the amino acid corresponding to position 353 is different from S and the amino acid corresponding to position 424 is different from K and the amino acid corresponding to position 452 is different from E; i) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with any of the amino acid sequences as defined under d) (positions 1 to 476 as shown under SEQ ID NO 12 given that the corresponding amino acid at position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid at position 197 is different from T and the amino acid corresponding to position 239 is different from S and the amino acid corresponding to position 327 is different from S and the amino acid corresponding to position 328 is different from V and the amino acid corresponding to position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P and the amino acid corresponding to position 46 is different from T and the amino acid corresponding to position 60 is different from C and the amino acid corresponding to position 185 is different from C and the amino acid corresponding to position 186 is different from C and the amino acid corresponding to position 195 is different from S and the amino acid corresponding to position 205 is different from Y and the amino acid corresponding to position 252 is different from V and the amino acid corresponding to position 268 is different from S and the amino acid corresponding to position 409 is different from R and the amino acid corresponding to position 436 is different from A; j) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with any of the amino acid sequences as defined under e) (positions 1 to 476 as shown under SEQ ID NO 15) given that the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the corresponding amino acid at position 239 is different from S and the corresponding amino acid at position 327 is different from S and the corresponding amino acid at position 328 is different from V and the corresponding amino acid at position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding to position 414 is different from P and the amino acid at position 48 is different from D and the amino acid at position 164 is different from Y and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 255 is different from F and the amino acid at position 424 is different from K. Positions 1 to 476 in SEQ ID NO 18 represent the amino acid sequence of a variant ω-ΤΑ protein comprising all of the amino acid modifications described herein above compared to each of the amino acid sequences as shown under SEQ ID NO 3 (from positions 1 to 477), SEQ ID NO 6 (from positions 1 to 479), SEQ ID NO 9 (from positions 1 to 476), SEQ ID NO 12 (from positions 1 to 476) and SEQ ID NO 15 (from positions 1 to 476). Table 1 synthesizes the modifications present in the amino acid sequence of a variant protein of ω-ΤΑ according to the invention (positions 1 to 476 under SEQ ID NO 18) in comparison with each of the amino acid sequences of ω- Wild-type TAs (positions 1 to 477 under SEQ ID NO 3 or positions 1 to 479 under SEQ ID NO 6 or positions 1 to 476 under SEQ ID NO 9 or positions 1 to 476 under SEQ ID NO 15) as well as well as in comparison with a modified ω-ΤΑ from Arthrobacter sp. (positions 1 to 476 under SEQ ID NO 12). QL7 Lnn / L7í17 / E / Yli Amino acid position Amino acid present at the respective amino acid position in SEQ ID NO 3 SEQ ID NO 6 SEQ ID NO 9 SEQ ID NO12 SEQ ID NO 15 SEQ ID NO 18 2 S G S G G G 25 F F F F F R 46 M T M T M M 48 D G D G D G 60 Y C Y C Y Y 64 L L L L L I 69 Q Q P Q Q Q 88 T T T T T A 90 A S A A A A A 157 T T T T T A 164 Y F Y F Y F 165 R R R R Q 169 V V V V A 174 E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E E EAS I I I I F I 268 N s T s N N 311 L V L V V V 318 A A E A A A 322 K K R K K K 327 S s S s S T 328 V V V V V G 353 F L F L L L 359 D N N N N N 384 Y Y Y Y Y C 389 I I I I I L 391 D D D D D E 396 K K K K K E 409 T R T R T T 410 H H H H H R 414 P P P P P L 424 K E K E K E 436 V A V A V V 452 G G E G G G 475 A Q Q Q Q Q 476 L S S S S S 477 E A Extreme Extreme Extreme Extreme QL7Lnn / L7n7 / E / Yli 478 L End 479 E 480 End Table 1 "End" in Table 1 indicates the position after the last amino acid present in the amino acid sequence of the respectively known (wild-type) sequence. A preferred embodiment of the invention therefore concerns a protein according to the invention having the activity of a ω-ΤΑ selected from the group consisting of a) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18; b) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, even more preferably 96%, with particular preference 97%, most preferably 98% or with special preference 99% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID N018 given that each of the amino acids corresponding to positions 25, 64, 88, 157, 165, 169,174, 187,197 239, 327, 328, 384, 389,391,396,410 and 414 in SEQ ID N018 represent those amino acids shown at the respective positions in the amino acid sequence shown under SEQ ID NO 18; c) proteins having an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%, most preferably 98% or with special preference 99% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID N018 given that each of the amino acids corresponding to positions 2, 25, 46, 48, 60, 64, 69, 88, 90, 157, 164, 165, 169, 174, 185, 186, 187, 195, 197, 202, 205, 239, 242, 245, 252, 255, 268, 311,318, 322, 327, 328, 353, 359, 384, 389, 391,396, 409, 410, 414, 424, 436, 452, 475 and 476 represent those amino acids shown in the respective positions in the amino acid sequence shown under SEQ ID NO 18. In the highly preferred embodiment the protein according to the invention encoding a ω-ΤΑ is a protein comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18. The proteins hitherto described herein above are commonly referred to herein as ω-ΤΑ variants or variant proteins according to the invention. It was found that the introduction of additional amino acid modifications within protein variants according to the invention further improves the activity of the ω-ΤΑ variants, in particular with regard to their substrate specificity, which means that these ω-ΤΑ variants Further modified ω-ΤΑ are better adapted to produce nearly pure or enantiomerically enriched products as compared to the ω-ΤΑ variants described herein above. The ω-TAs comprising further modifications are further modified compared to the ω-ΤΑ variants described herein above as the proteins according to the invention. Variants of ω-ΤΑ comprising additional modifications are in particular suitable for producing enantiomerically enriched or nearly enantiomerically pure phosphoamino acids and are designated herein as ω-ΤΑ vanants comprising additional amino acid modifications or proteins according to the invention comprising additional amino acid modifications. With regard to ω-ΤΑ variants having additional amino acid modifications, preferred methods for demonstrating that a protein has the activity of an ω-ΤΑ, for example, are described in WO 2017 / 151573, a particularly preferred method for Demonstrating ω-ΤΑ variants having additional amino acid modifications is described herein under "General Methods", item 7. "Enantiomerically enriched" means herein that one of two enantiomers is present in a composition in higher amounts than the other enantiomer, preferably at least 60% of one enantiomer is present in the composition, more preferably at least 65%. % of an enantiomer is present in the composition, even more preferably at least 70% of an enantiomer is present in the composition, still more preferably at least 75% of an enantiomer is present in the composition, still with More preferably at least 80% of an enantiomer is present in the composition, particularly preferably at least 85% of an enantiomer is present in the composition, most preferably at least 90% of an enantiomer is present in the composition or with particular preference, at least 94% of an enantiomer is present in the composition. "Enantiomerically nearly pure" means herein that one of two enantiomers is present in a composition in amounts of at least 95.0%, preferably one of two enantiomers is present in a composition in amounts of at least 95.5% %, more preferably, one of two enantiomers is present in a composition in amounts of at least 96.0%, even more preferably, one of two enantiomers is present in a composition in amounts of at least 96.5% still more preferably one of two enantiomers is present in a composition in amounts of at least 97.0%, still more preferably one of two QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ enantiomers is present in a composition in amounts of at least 98.0%, with particular preference, one of two enantiomers is present in a composition in amounts of at least 98.5%, with Most preferably, one of the two enantiomers is present in a composition in amounts of at least 99.0%, or more preferably, one of the two enantiomers is present in a composition in amounts of at least 99.5%. Another embodiment according to the invention therefore concerns protein variants according to the invention having the activity of a ω-ΤΑ variant, wherein the amino acid sequences according to the invention comprise additional amino acid modifications compared to with the proteins according to the invention. Preferably, another embodiment of the invention with respect to amino acid sequences of proteins having the activity of an ω-ΤΑ according to the invention (variants of ω-ΤΑ) comprising additional amino acid modifications is therefore a protein of according to the invention that has the activity of a ω-ΤΑ selected from the group consisting of a) proteins according to the invention since the amino acid at position 166 is G and the amino acid at position 327 is Q; b) proteins according to the invention since the amino acid at position 327 is Q and the amino acid at position 384 is S; c) proteins according to the invention since the amino acid at position 326 is Q and the amino acid at position 327 is Q; d) proteins according to the invention since the amino acid at position 327 is Q; e) proteins according to the invention since the amino acid at position 326 is F and the amino acid at position 327 is Q; f) proteins according to the invention since the amino acid at position 327 is C; g) proteins according to the invention since the amino acid at position 327 is I; h) proteins according to the invention since the amino acid at position 327 is M; i) proteins according to the invention since the amino acid at position 164 is Y; j) proteins according to the invention since the amino acid at position 164 is S; k) proteins according to the invention since the amino acid at position 327 is V; I) proteins according to the invention since the amino acid at position 409 is R; m) proteins according to the invention since the amino acid at position 327 is S; n) proteins according to the invention since the amino acid at position 271 is I; o) proteins according to the invention since the amino acid at 329 is G; p) proteins according to the invention since the amino acid at position 409 is P; q) proteins according to the invention since the amino acid at position 414 is M; r) proteins according to the invention since the amino acid at position 165 is K; s) proteins according to the invention since the amino acid at position 414 is R; t) proteins according to the invention since the amino acid at position 414 is H; u) proteins according to the invention since the amino acid at position 165 is C; v) proteins according to the invention since the amino acid at position 327 is V; w) proteins according to the invention since the amino acid at position 164 is O; x) proteins according to the invention since the amino acid at position 409 is K. A more preferred embodiment of the invention with respect to amino acid sequences of proteins having the activity of an ω-ΤΑ comprising additional amino acid modifications concerns proteins having the activity of an ω-ΤΑ selected from the group consisting of a) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid S at position 166 in SEQ ID NO 18 is replaced by G and the amino acid T at position 327 in SEQ ID NO 18 is replaced by Q; b) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the Q 17 Lnn / Lznz / Ε / ΥΙΛΙ amino acid T at position 327 in SEQ ID NO 18 is replaced by Q and amino acid C at position 384 in SEQ ID NO 18 is replaced by S; c) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid E at position 326 in SEQ ID NO 18 is replaced by Q and the amino acid T at position 327 in SEQ ID NO 18 is replaced by Q; d) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 327 in SEQ ID NO 18 is replaced by Q ; e) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid E at position 326 in SEQ ID NO 18 is replaced by F and the amino acid T at position 327 in SEQ ID NO 18 is replaced by Q; f) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 327 in SEQ ID NO 18 is replaced by O ; g) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 327 in SEQ ID NO 18 is replaced by I ; h) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 327 in SEQ ID NO 18 is replaced by M ; i) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid F at position 164 in SEQ ID NO 18 is replaced by Y ; j) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid F at position 164 in SEQ ID NO 18 is replaced by S ; k) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 327 in SEQ ID NO 18 is replaced by V ; I) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 409 in SEQ ID NO 18 is replaced by R ; m) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ amino acid T at position 327 in SEQ ID NO 18 is replaced by S; n) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid V at position 271 in SEQ ID NO 18 is replaced by I ; o) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid S at position 329 in SEQ ID NO 18 is replaced by G ; p) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 409 in SEQ ID NO 18 is replaced by P ; q) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid L at position 414 in SEQ ID NO 18 is replaced by M ; r) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid Q at position 165 in SEQ ID NO 18 is replaced by K ; s) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid L at position 414 in SEQ ID NO 18 is replaced by R ; t) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid L at position 414 in SEQ ID NO 18 is replaced by H ; u) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid Q at position 165 in SEQ ID NO 18 is replaced by C ; v) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which amino acid T at position 327 in SEQ ID NO 18 is replaced by V ; w) proteins that have the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid F at position 164 in SEQ ID NO 18 is replaced by C ; x) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to which the amino acid T at position 409 in SEQ ID NO 18 is replaced by K y) proteins that possess an amino acid sequence that is at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still with QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ most preferred 95%, even more preferred 96%, particularly preferred 97%, most preferred 98%, or most preferred 99% identity to any of the amino acid sequences as defined under a), b), c), d), e), f), g), h), i), j), k), I), m), n), o), p), q ), r), s), t), u), v), w) or x) provided that each amino acid position as defined under a), b), c), d), e), f), g ), h), i), j), k), I), m), n), o), p), q), r), s), t), u), v), w) or x ), respectively, is also present at the corresponding amino acid position in the amino acid sequences of the protein sequence having at least 60, preferably 70%, more preferably 80%, still more preferably 90%, still with most preferably 95%, even more preferably 96%, particularly preferably 97%, most preferably 98%, or most preferably 99% identity to any of the amino acid sequences as defined under each of a), b ), c), d), e), f), g), h), i), j), k), I), m), n), o), p), q), r), s), t), u), v), w) or x). As an embodiment of the invention, preferred proteins having the activity of a ω-ΤΑ variant comprising additional amino acid modifications are those proteins defined under a), b), c), d), e), f ), g), h), i), j), k), I), m), n), o) and p) defined just above, more preferred are those proteins defined under a), b), c), d), e), f), g) and h) defined just above and even more preferred are those proteins defined under points a), b) and c) defined just above. Table 2 summarizes the additional amino acid modifications present in the amino acid sequence of ω-TAs comprising additional amino acid modifications compared to the amino acid sequence shown under SEQ ID NO 18 (from positions 1 to 476). QLZLnn / Lznz / B / Yi ωΤΑ variant comprising additional amino acid modifications Amino acid position in SEQ ID NO 18 Amino acid in additionally modified variant SEQ ID NO 18 Amino acid position in SEQ ID NO18 Amino acid in additionally modified variant SEQ ID NO 18 T327Q , S166G 327 Q T 166 G S T327Q, C384S 327 Q T 384 S C T327Q, E326Q 327 Q T 326 Q E T327Q 327 Q T T327Q, E326F 327 Q T 326 F E T327C 327 C T T327I 327 I T T327M 327 M T F164Y 164 Y F F164S 164 S F T327V 327 V T T409R 409 R T T327S 327 S T V271I 271 I V S329G 329 G s T409P 409 P T L414M 414 M L Q165K 165 K Q L414R 414 R L L414H 414 H L Q165C 165 C Q T327V 327 V T F164C 164 C F T409K 409KT Table 2 QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ A further embodiment of the invention concerns nucleic acid molecules encoding a protein according to the invention. Nucleic acid molecules according to the invention can be any type of nucleic acid, as long as the nucleic acid encodes a protein according to the invention. The nucleic acids can be ribonucleic nucleic acid (eg, RNA, mRNA) molecules or deoxyribonucleic nucleic acid (DNA) molecules, including genomic DNA which may or may not comprise introns and coding DNA. Of particular interest to the invention are nucleic acid molecules encoding a protein having the activity of an ω-ΤΑ comprising the amino acid sequence as shown from positions 1 to 476 under SEQ ID NO 18. Therefore, the invention also concerns nucleic acid molecules encoding a protein having the activity of an ω-ΤΑ selected from the group consisting of a) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence shown under SEQ ID NO 17; b) nucleic acid molecules that encode a protein comprising the amino acid sequence from position 1 to 476 in the amino acid sequence shown under SEQ ID NO 18; c) nucleic acid molecules having at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, particularly preferably 97 %, most preferably 98% or most preferably 99% identity to the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 17 since the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO 17 has the sequence of nucleotides ath and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the sequence of nucleotides gene and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the sequence of nucleotides gene and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID N017 has the sequence of gene nucleotides and the codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID N017 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 979 to 981 in SEQ ID N017 has the nucleotide sequence acn and the codon at nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gary and the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1228 to 1230 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn\ d) nucleic acid molecules having at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, particularly preferably 97 %, most preferably 98% or most preferably 99% identity with the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 17, given that the codon corresponding to the nucleotide positions 4 to 6 in SEQ ID NO 17 have the nucleotide sequence ggn and the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 have the nucleotide sequence mgn and the codon corresponding to the nucleotide positions 136 to 138 in SEQ ID NO 17 have the atg nucleotide sequence and the codon corresponding to the nucleotide positions QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ 142 144 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 178 to 180 in SEQ ID NO 17 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID N017 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 205 to 207 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 268 to 270 in SEQ ID N017 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 490 to 492 in SEQ ID N017 has the nucleotide sequence tty and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 553 to 555 in SEQ ID NO 17 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 556 to 558 in SEQ ID N017 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 583 to 585 in SEQ ID NO 17 has the ccn nucleotide sequence and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID NO 17 have the gen nucleotide sequence and the codon corresponding to nucleotide positions 604 to 606 in SEQ ID NO 17 have the nucleotide sequence aa and y the codon corresponding to nucleotide positions 613 to 615 in SEQ ID NO 17 has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO 17 has the sequence of ccn nucleotides and the codon corresponding to nucleotide positions 724 to 726 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 733 to 735 in SEQ ID NO 17 has the sequence of acn nucleotides and the codon corresponding to nucleotide positions 754 to 756 in SEQ ID NO 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 763 to 765 in SEQ ID N017 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 802 to 804 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 931 to 933 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 952 to 954 in SEQ ID NO 17 has the gene nucleotide sequence and the corresponding codon QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ at nucleotide positions 964 to 966 in SEQ ID NO 17 has the nucleotide sequence aand the codon corresponding to nucleotide positions 979 to 981 in SEQ ID N017 has the sequence of nucleotides acn and the codon corresponding to nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1057 to 1059 in SEQ ID NO 17 has the sequence of ytn nucleotides and the codon corresponding to nucleotide positions 1075 to 1077 in SEQ ID NO 17 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 have the nucleotide sequence gar and the codon corresponding to nucleotide positions 1225 to 1227 in SEQ ID NO 17 have the nucleotide sequence acn and the codon corresponding to nucleotide positions 1228 to 1230 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1270 to 1272 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1306 to 1308 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 1354 to 1356 in SEQ ID NO 17 has the nucleotide sequence ggn·, e) nucleic acid molecules that hybridize with the complementary strand of the nucleic acid molecules defined under a), b), c) or d), given that the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the gene nucleotide sequence and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the gene nucleotide sequence and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence mgny e\ codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the gene nucleotide sequence and codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO QLZLnn / Lznz / E / Yi has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon at nucleotide positions 982 to 984 in SEQ ID NO 17 it has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 it has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID N017 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID N017 has the nucleotide sequence gary and the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 has the nucleotide sequence gary and the codon corresponding to nucleotide positions 1228 to 1230 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn\ f) nucleic acid molecules that hybridize with the complementary strand of the nucleic acid molecules defined under a), b), c) or d) given that the codon corresponding to nucleotide positions 4 to 6 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 136 to 138 in SEQ ID NO 17 has the nucleotide sequence atg and the codon corresponding to nucleotide positions 142 to 144 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 178 to 180 in SEQ ID NO 17 has the tay nucleotide sequence and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO 17 has the ath nucleotide sequence and the codon corresponding to nucleotide positions 205 to 207 in SEQ ID N017 has the nucleotide sequence cary the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 268 to 270 in SEQ ID NO 17 has the sequence of nucleotides gene and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the sequence of nucleotides gene and the codon corresponding to nucleotide positions 490 to 492 in SEQ ID NO 17 has the sequence of tty nucleotides and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence cary and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 553 to 555 in SEQ ID NO 17 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 556 to 558 in SEQ ID NO 17 has the sequence of QLZLnn / Lznz / E / Yi nucleotides a to and and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID N017 has the nucleotide sequence a to and and the codon corresponding to nucleotide positions 583 to 585 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 604 to 606 in SEQ ID NO 17 has the nucleotide sequence aa and and the codon corresponding to nucleotide positions 613 to 615 in SEQ ID NO 17 has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID N017 has the sequence of nucleotides ccn and the codon corresponding to nucleotide positions 724 to 726 in SEQ ID NO 17 has the sequence of nucleotides gtn and the codon corresponding to nucleotide positions 733 to 735 in SEQ ID NO 17 has the sequence of nucleotides acn and the codon corresponding to nucleotide positions 754 to 756 in SEQ ID NO 17 has the sequence of nucleotides ath and the codon corresponding to nucleotide positions 763 to 765 in SEQ ID NO 17 has the sequence of nucleotides ath and the codon corresponding to nucleotide positions 802 to 804 in SEQ ID NO 17 has the nucleotide sequence aa and the codon corresponding to nucleotide positions 931 to 933 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 952 to 954 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 964 to 966 in SEQ ID NO 17 has the nucleotide sequence aary the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1057 to 1059 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1075 to 1077 in SEQ ID NO 17 has the nucleotide sequence aa and y the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1225 to 1227 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 1228 to 1230 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ corresponding to nucleotide positions 1270 to 1272 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1306 to 1308 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 1354 to 1356 in SEQ ID NO 17 have the nucleotide sequence ggrr, g) nucleic acid molecules that deviate from the nucleic acid molecules defined under a), b), c), d), e) or f) due to a degeneracy of the genetic code; h) nucleic acid molecules encoding a protein having at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID N018 since the amino acids corresponding to positions 25, 64, 88, 157, 165, 169, 174, 187, 239, 327, 328, 384, 389, 391,396, 410 and 414 in SEQ ID NO 18 represent those amino acids shown at the respective positions in the amino acid sequence that are sample under SEQ ID NO 18; i) nucleic acid molecules encoding a protein having at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%, most preferably 98% or most preferably 99% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18 since the amino acids corresponding to positions 2, 25 , 46, 48, 60, 64, 69, 88, 90, 157, 164, 165, 169, 174, 185, 186, 187, 195, 197, 202, 205, 239, 242, 245, 252, 255, 268 , 311,318, 322, 327, 328, 353, 359, 384, 389, 391,396, 409, 410, 414, 424, 436, 452, 475 and 476 in SEQ ID NO 18 represent those amino acids shown at the respective positions in the amino acid sequence shown under SEQ ID NO 18; j) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16. SEQ ID NO 16 shows a nucleotide sequence obtained by reverse translation of a protein that has the amino acid sequence as shown under SEQ ID NO 18, where the degeneracy of the genetic code is reflected. SEQ ID NO 17 is a synthetic nucleic acid molecule obtained by replacing, due to the degeneracy of the genetic code, flexible nucleotides in SEQ ID NO 16 with specific nucleotides. Both, SEQ ID NO 16 and SEQ ID NO 17 encode a protein that has the activity of a ω-ΤΑ that has the amino acid sequence as described QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ sample under SEQ ID NO 18. In the context of the present invention, the term "hybridizing with" means hybridization under standard hybridization conditions, preferably under stringent conditions, as described, for example, in Sambrooket al. (Molecular Cloning, A Laboratory Manual, 3rd Edition (2001) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. ISBN: 0879695773) or Ausubel et al. (Short Protocols in Molecular Biology, John Wiley & Sons; 5th edition (2002), ISBN: 0471250929). With particular preference, hybridization means hybridization under the following conditions: hybridization buffer: 2xSSC; 10X Denhardt's solution (Fikoll 400+PEG+BSA; ratio 1:1:1); 0.1% SDS; 5mM EDTA; 50 mM Na2HPO4; 250 pg / ml herring sperm DNA; 50 pg / ml tRNA; either M sodium phosphate buffer pH 7.2; 1mM EDTA; 7% SDS hybridization temperature: T = 65 to 68°C wash buffer: 0.1xSSC; 0.1% SDS washing temperature: T = 65 to 68°C. Nucleic acid molecules that hybridize to nucleic acid molecules that encode a protein having the activity of an ω-ΤΑ can come from any organism; consequently, they can originate from bacteria, fungi, animals, humans, plants, or viruses. Nucleic acid molecules that hybridize to nucleic acid molecules encoding a protein having the activity of an ω-ΤΑ preferably originate from microorganisms, more preferably from fungi or bacteria, most preferably from of bacteria. Nucleic acid molecules that hybridize to the aforementioned molecules can be isolated, for example, from genomic or cDNA libraries. Said nucleic acid molecules can be identified and isolated using the nucleic acid molecules described herein or they can be identified and isolated using parts of these molecules or the reverse complements of these molecules, for example, by means of hybridization according to methods standard (see, for example, Sambrook et al., Molecular Cloning, A Laboratory Manual, 3rd Edition (2001) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. ISBN: 0879695773; Ausubel et al., Short Protocols in Biology Molecular, John Wiley & Sons; 5th edition (2002), ISBN: 0471250929) or by amplification using PCR. As a hybridization sample for isolating a nucleic acid sequence encoding a protein having the activity of an ω-ΤΑ, it is possible to use, for example, nucleic acid molecules having exactly or essentially the nucleic acid sequences QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ from positions 1 to 1431 described under SEQ ID NO 2 or essentially the nucleic acid sequences from positions 1 to 1437 described under SEQ ID NO 5 or essentially the nucleic acid sequences described under SEQ ID NO 8 or essentially the nucleic acid sequences described under SEQ ID NO 11 or essentially the nucleic acid sequences described under SEQ ID NO 14 or essentially the nucleic acid sequences described under SEQ ID NO 17 or fragments of these sequences nucleic acids. The fragments used as hybridization samples can also be oligonucleotides or synthetic fragments prepared using usual synthetic techniques, the sequence of which is essentially identical to the nucleic acid molecule described in the context of the present invention. Once the genes that hybridize to the nucleic acid sequences described in the context of the present invention are identified and isolated, the sequence should be determined and the properties of the proteins encoded by this sequence should be analyzed to determine if they are proteins that have the activity of a ω-ΤΑ. Methods for determining whether a protein has the activity of a protein that has the activity of an ω-ΤΑ are known to the person skilled in the art and have been mentioned herein above. The molecules that hybridize with the nucleic acid molecules described in the context of the present invention comprise in particular fragments, derivatives and allelic variants of the mentioned nucleic acid molecules. In the context of the present invention, the term "derivative" means that the sequences of these molecules differ at one or more positions from the sequences of the nucleic acid molecules described above and are highly identical to these sequences. Differences from the nucleic acid molecules described above may, for example, be due to deletion, addition, substitution, insertion, or recombination. Another embodiment of the invention with respect to nucleic acid molecules encoding proteins having the activity of an ω-ΤΑ comprising additional amino acid modifications concerns nucleic acid molecules according to the invention encoding proteins having the activity of one ω-ΤΑ selected from the group consisting of a) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 496 to 498 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence ggn and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car , b) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car and the codon at nucleotide positions 1150 to 1152 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence wsn; c) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 976 to 978 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car, and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car, d) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car, e) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 976 to 978 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence tty and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car , f) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence car, g) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence ath\ h) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence atg\ i) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under the QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ SEQ ID NO 16 or SEQ ID NO 17, in addition to the fact that the codon at nucleotide positions 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence tay; j) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence wsn; k) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence gtn; I) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence mgn; m) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence wsn; n) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 811 to 813 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence ath; o) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 985 to 987 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence ggn; p) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence ccn; q) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence atg; r) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under the QL7 Lnn / LZnZ / E / Yli SEQ ID NO 16 or SEQ ID NO 17, in addition to the fact that the codon at nucleotide positions 493 to 495 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence aar; s) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence mgn; t) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence cay; u) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 493 to 495 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence tgy; v) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at positions of the nucleotides 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence gtn; w) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at the positions of the nucleotides 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 have the nucleotide sequence tgy; x) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at positions of the nucleotides 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 have the aar nucleotide sequence; y) nucleic acid molecules having a nucleic acid sequence having at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, even more preferably 95%, even more preferably 96%, particularly preferably 97%, most preferably 98% or most preferably 99% identity with any of the nucleic acid sequences defined under a), b), c), d), e), f), g). h)>¡λ j)>k)> D>m)>n), o), p), q), r), s), t), u), v), w) or x) given that each nucleotide sequence of the codon as defined in each of a), b), c), d), e), f), g), h), i), j), k), I), m) , n), o), p), q), r), s), t), u), v), w) or x), respectively, is also present at the corresponding nucleotide position of the codon in the sequence of nucleic acids having at least 60% preferably 70%, more preferably 80%, even more preferably QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ 90%, still more preferably 95%, still more preferably 96%, particularly preferably 97%, most preferably 98%, or most preferably 99% identity with any of the nucleic acid sequences defined under each of a), b), c), d), e), f), g), h), i), j), k), I), m), n), o), p), q) , r), s), t), u), v), w) or x). Preferred nucleic acid molecules according to the invention are those nucleic acid molecules defined just above under a), b), c), d), e), f), g), h), i) , j), k), I), m), n), o) and p), more preferred are those nucleic acid molecules defined just above under a) to k), even more preferred are those nucleic acid molecules defined just above under points a), b), c), d), e), f), g) and h) and highly preferred are those nucleic acid molecules defined just above under points a), b) ye). The meaning of the nucleotide abbreviations a, c, g, t, and those of the degenerate nucleotide abbreviations r, y, s, w, k, m, b, d, h, v, n are derived in the present after Table 3 under the paragraph subtitled "Description of the Sequences". Which amino acids are encoded by codons comprising degenerate nucleotides are herein derived following Table 5 under the paragraph subtitled "Description of Sequences". Furthermore, the invention relates to recombinant nucleic acid molecules comprising a nucleic acid molecule according to the invention. In conjunction with the present invention, the term "recombinant nucleic acid molecule" is to be understood as meaning a nucleic acid molecule, which contains additional sequences in addition to nucleic acid molecules according to the invention, which do not occur naturally in the combination in which which they occur in recombinant nucleic acids according to the invention. Here, the aforementioned additional sequences may consist of any sequence, preferably they are functional or regulatory sequences (promoters, termination signals, enhancers, ribosome binding sites (rbs), leader sequences that enhance transcription, translation or RNA stability, subcellular targeting sequences, etc.), with particular preference, they are functional or regulatory sequences that are active in microorganisms, and especially with particular preference, they are regulatory sequences that are active in fungi, in particular, in yeasts or in bacteria. Methods for creating recombinant nucleic acid molecules according to the invention are known to those skilled in the art, and include genetic methods such as joining nucleic acid molecules by ligation, genetic recombination, or new synthesis of nucleic acid molecules. Those methods are described, for example, in Sambrok et al. (Molecular Cloning, A Laboratory Manual, 3rd Edition (2001) Cold Spring Harbor QL7 Lnn / L7í17 / E / Yli Laboratory Press, Cold Spring Harbor, NY. ISBN: 0879695773) or Ausubel et al. (Short Protocols in Molecular Biology, John Wiley & Sons; 5th edition (2002), ISBN: 0471250929). In a further embodiment, the recombinant nucleic acid molecules according to the invention comprise a nucleic acid molecule according to the invention which is linked to regulatory sequences, which initiate transcription in prokaryotic or eukaryotic cells. Regulatory sequences, which initiate "transcription" in a cell are also known as promoters. Information regarding regulatory sequences and plasmids is well known to one skilled in the art and is described, for example, by the International Foundation for Genetic Engineering Machines (¡GEM)-supported Registry of Standard Biological Parts. ) (One Kendall Square, Suite B6104, Cambridge, MA 02139, United States) on the World Wide Web (http: / / parts.igem.org / Catalog). Regulatory sequences that initiate transcription in prokaryotic organisms, eg E. coli, and in eukaryotic organisms are sufficiently described in the literature, in particular, they are described as such for expression in yeast, eg Saccharomyces cerevisiae. An overview of various systems for protein expression in various host organisms can be found, for example, in Methods in Enzymology 153 (1987), 383-516 and in Bitter et al. (Methods in Enzymology 153 (1987), 516-544) or in Gomes et al. (2016, Advances in Animal and Veterinary Sciences, 4(4), 346) and Baghban et al. (2018, Current Pharmaceutical Biotechnology, 19(6)). Common yeast promoters are pAOX1, pHIS4, pGAL, pScADH2 (Baghban et al., 2018, see above). Common bacterial promoters are T5, T7, rhamnose-inducible, arabinose-inducible, PhoA, artificial trc (trp-lac) promoter as described by Marschall et al. (2017, Microbiol y Biotecnol Aplic 101, 501-512) and Tegel et al. (2011, Journal FEBS 278, 729-739). A further embodiment of recombinant nucleic acid molecules of the present invention are vectors or plasmids, which comprise the nucleic acid molecules according to the invention. Vectors are commonly understood in the field of molecular biology and herein to represent a nucleic acid sequence or a vehicle comprising a nucleic acid sequence used to transfer genetic material (DNA or RNA) into a target cell. Vectors can be plasmids, for example, T-DNA or binary vectors for generating transgenic plants, expression vectors for expression of nucleic acid sequences in a host cell, shuttle vectors that are eligible for propagation in different hosts, or the vectors they can be virus particles or bacteriophages that have been modified to deliver foreign genetic material into a host. QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ In the field of molecular biology and at present it is commonly understood that plasmids represent an often circular DNA molecule, autonomously self-replicating and, when present, present in a host cell separate from chromosomal DNA. The nucleic acid molecules according to the invention, the recombinant nucleic acid molecules according to the invention, the vectors or plasmids according to the invention can be used for the production of proteins according to the invention, for example by the expression of the nucleic acid molecules according to the invention in host cells. Another embodiment of the invention concerns hosts or host cells comprising or expressing a nucleic acid molecule according to the invention or comprising proteins according to the invention or comprising a recombinant nucleic acid molecule according to the invention or comprising a vector according to the invention or comprising a plasmid according to the invention. Nucleic acid molecules according to the invention encoding a protein having the activity of an ω-ΤΑ can be expressed in host cells for eg their multiplication or for the production of proteins according to the invention. For expression in host cells, the nucleic acid molecules according to the invention may be comprised in vectors or plasmids or they may be stably integrated into the genome of a respective host cell. Nucleic acid molecules according to the invention may also be composed of vectors that support their introduction into host cells. A further embodiment of the present invention concerns a host or a host cell according to the invention comprising a nucleic acid molecule according to the invention or comprising a recombinant nucleic acid molecule according to the invention or comprising a vector according to the invention or comprising a plasmid according to the invention and, in each case, comprising a protein according to the invention. Another embodiment of the present invention concerns a host or a host cell according to the invention comprising a nucleic acid molecule according to the invention or comprising a recombinant nucleic acid molecule according to the invention or comprising a vector according to the invention or comprising a plasmid according to the invention and, in each case, expressing a protein according to the invention. Another embodiment of the present invention concerns a host or a host cell according to the invention comprising a nucleic acid molecule of QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ according to the invention or comprising a recombinant nucleic acid molecule according to the invention or comprising a vector according to the invention or comprising a plasmid according to the invention and, in each case, expressing a protein, wherein the protein has the activity of an ω-transaminase. Expressing a nucleic acid molecule is to be understood herein to mean that in case the nucleic acid molecule is RNA or mRNA, the nucleic acid molecule is translated into a protein, preferably, it is translated into a protein having the activity of an ω-ΤΑ or in the case that the nucleic acid molecule is DNA or cDNA, it is transcribed (and in the case of genomic DNA containing introns, processed) into mRNA, preferably into an mRNA which encodes a protein having the activity of an ω-ΤΑ and is subsequently translated into a protein, preferably, is translated into a protein having the activity of an ω-ΤΑ. Transcription of a given nucleic acid molecule in a host can be demonstrated by means of methods known to a person skilled in the art, for example by detection of specific transcripts (mRNA) of foreign nucleic acid molecules through blot analysis. Northern or RT-PCR. Whether the hosts or host cells comprise a given protein or comprise a protein that is derived from the expression of a nucleic acid molecule can be determined by methods known to a person skilled in the art, for example by immunological methods, such as Western blot analysis, ELISA. (Enzyme Linked Immunosorbent Assay) or RIA (Radioimmune Assay). The person skilled in the art is familiar with methods for preparing antibodies that specifically react with a certain protein, that is, that specifically bind to a certain protein (see, for example, Lottspeich and Zorbas (eds.), 1998, Bioanalytik, Spektrum akad, Verlag, Heidelberg, Berlin, ISBN 3-8274-0041-4). Some companies (Thermo Fisher Scientific, 168 Third Avenue, Waltham, MA USA 0245; GenScript, 60 Centennial Ave., Piscataway, NY 08854, USA) offer preparation of such antibodies as an order service. In addition, a person skilled in the art can assess whether a host or a host cell comprises a protein according to the invention by (additional) detecting the activity of proteins having the activity of an ω-ΤΑ in a respective host cell. Preferably, the activity of proteins having additional activity of an ω-ΤΑ in a respective host cell is detected by comparing the activities of the ω-TAs of a host cell according to the invention with the respective activity of the host cell that it does not comprise a protein according to the invention. The test of whether a protein has the activity of an ω-ΤΑ can be performed as QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ described herein above. A person skilled in the art can produce a host or host cells according to the invention by means of known methods for genetically modifying or transforming organisms. Therefore, a further subject of the present invention consists of a host or a host cell according to the invention, in particular a prokaryotic or eukaryotic host or host cell, which is genetically modified (or transformed) with a nucleic acid molecule according to the invention or with a recombinant nucleic acid molecule according to the invention or with a vector according to the invention or with a plasmid according to the invention. Preferably, the genetically modified (transformed) host or host cell according to the invention expresses a protein having the activity of an ω-transaminase, more preferably, the modified host or host cell ( genetically transformed according to the invention expresses a protein according to the invention. Genetically modified with a nucleic acid molecule or transformed with a nucleic acid molecule is hereby understood to mean that a nucleic acid molecule is or was introduced into a host or a host cell via technical and / or non-natural means, preferably by means of technical methods in the field of molecular biology, biotechnology or genetic modification. The descendants, progeny or progeny of the hosts or host cells according to the invention also constitute an embodiment of the invention, preferably these descendants, progeny or progeny comprise a nucleic acid molecule according to the invention or comprise a molecule of recombinant nucleic acid according to the invention or comprise a vector according to the invention or comprise a plasmid according to the invention or comprise a protein according to the invention, more preferably, these progeny, offspring or progeny comprise a molecule of nucleic acid according to the invention or comprise a recombinant nucleic acid molecule according to the invention or comprise a vector according to the invention or comprise a plasmid according to the invention and, in each case, express a protein, wherein the protein has the activity of an ω-ΤΑ, still more preferably, these progeny, offspring or progeny comprise a nucleic acid molecule according to the invention or comprise a recombinant nucleic acid molecule according to the invention or comprise a vector according to the invention or comprise a plasmid according to the invention and, in each case, express a protein, wherein the protein has the activity of an ω-ΤΑ according to the invention. The host or host cell according to the invention may be a host or host cell of any prokaryotic or eukaryotic organism. The hosts or host cells can be bacteria or bacterial cells (for example, E. coli, bacteria of the genus Bacillus, in particular Bacillus subtilis, Agrobacterium, in particular Agrobacterium tumefaciens or Agrobacterium rhizogenes, Pseudomonas, in particular Pseudomonas fluorescens, Streptomyces spp, Rhodococcus spp, in particular Rhodococcus rhodochrous, Vibrio natrigens, Corynebacterium, in particular Corynebacterium glutamicum) or fungi or fungal cells (for example Agaricus, in particular Agaricus bisporus, Aspergillus, Trichoderma or yeasts, in particular S. cerevisiae, Pichia ssp., such as P. pastoris), as well as plants or plant cells or they can be animals or animal cells. Preferred host cells according to the invention are microorganism cells. Within the framework of the present patent application, this is understood to include all bacteria and all protists (for example, fungi, in particular yeast and algae), as defined in Schlegel's General Microbiology (Georg Thieme Publishing House (1985 ), 1- 2), for example. With regard to microorganisms, the hosts or host cells according to the invention are preferably bacteria / bacterial cells or yeast / yeast cells, most preferably they are bacteria / bacterial cells. As far as bacteria / bacterial cells are concerned, the hosts or host cells according to the invention are preferably Bacillus species / cells of Bacillus species or Escherichia co / / 7 cells of Escherichia coli cells, most preferably, Escherichia co / / 7 cells of Escherichia coli. Alternatively, hosts or host cells according to the invention may be Pseudomonas, in particular Pseudomonas fluorescens, Streptomyces spp, Rhodococcus spp, in particular Rhodococcus rhodochrous, Vibrio spp, in particular Vibrio natrigens, Corynebacterium, in particular Corynebacterium glutamicum or others. A preferred embodiment of the invention concerns hosts or host cells according to the invention comprising a nucleic acid molecule according to the invention, wherein the nucleic acid molecule according to the invention is characterized in that the codons of said molecule nucleic acid sequences are changed such that they match the codon usage frequency of the host or a host cell, respectively. The host cells according to the invention can be used for the production of proteins according to the invention. The proteins according to the invention can be used in methods for the production of enantiomerically enriched or nearly enantiomerically pure amines from a carbonyl (acceptor) in the presence of an amine (donor). QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ The reaction catalyzed in the methods for the production of enantiomerically enriched or nearly enantiomerically pure amines by means of a protein according to the invention can be formally described herein above by the general equation (I). Accordingly, another embodiment of the invention concerns a method for the production of an amine comprising the steps of a) providing an amine acceptor molecule; b) providing an amine donor molecule; c) contacting the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) with a protein according to the invention; d) optionally, obtain the amine. A preferred embodiment of the method according to the invention for the production of an amine consists in a method for the production of an aliphatic amine (including, but not limited to, linear, branched or cyclic alkane amines, alkene amines, alkyne amines ) or consists of a method for the production of an aryl amine or consists of a method for the production of an amino acid, more preferably, a method for the production of an amino acid, even more preferably, a method for the production of an α-branched amino acid, an α-aromatic amino acid or an α-aromatic amino acid comprising substituted phenyl groups, most preferably a method for the production of norvaline, leucine, phenylalanine or tyrosine amino acids. With regard to ω-ΤΑ variants according to the invention comprising additional amino acid modifications, the method according to the invention for the production of an amine is preferably a method for the production of an aliphatic amine comprising phosphorus ( including, but not limited to, a linear, branched or cyclic alkane amine, alkene amine, alkyne amine, comprising phosphorus) or consisting of a method for the production of a phosphorus-comprising aryl amine or consisting of a method for the production of a phosphorus-comprising amino acid, more preferably, in a method for the production of a phosphorus-comprising α-amino acid, still more preferably, in a method for the production of a phosphorus-comprising branched α-amino acid, an α - phosphorus-comprising aromatic amino acid or a phosphorus-comprising aromatic α-amino acid comprising substituted phenyl groups, still more preferably, in a method for the production of a phosphorus-comprising α-amino acid, even more preferably, in a method for the production of an α-amino acid comprising a methyl-substituted phosphorus, most preferably, in a method for the production of glufosinate. QLZLnn / Lznz / B / Yi The amine acceptor molecule in step a) of the method according to the invention for the production of an amine is a molecule comprising a carbonyl group that accepts an amino group from an amine donor molecule, whereby, the carbonyl group of acceptor molecule is converted to amine. Preferably, the amine acceptor molecule in step a) of the method according to the invention for the production of an amine is an aliphatic ketone (including, but not limited to, alkanones, alkenones, linear, branched or cyclic alquinones). ) is either an there ketone or is a keto acid, more preferably this is a keto acid, even more preferably this is an α-keto acid, most preferably the amine acceptor molecule is selected from the group consisting of 2-acid oxovaleric, 4-methyl-2-oxovaleic acid, phenylpyruvic acid or 4-hydroxyphenylpyruvic acid. With regard to ω-ΤΑ protein variants according to the invention comprising additional amino acid modifications, the amine acceptor molecule in step a) of the method according to the invention for the production of an amine is preferably a ketone. phosphorus-containing aliphatic acid (including, but not limited to, linear, branched, or cyclic alkanones, alkenones, alquinones) or a phosphorus-containing aryl ketone or phosphorus-containing keto acid, more preferably, the amine acceptor molecule is a phosphorus-comprising ketoacid, even more preferably, the amine acceptor molecule is a phosphorus-comprising acetoacid, still more preferably, a methyl-substituted phosphorus-comprising α-ketoacid, most preferably, the amine acceptor molecule is step a) is 4-[hydroxy¡(methyl)phosphoryl]-2-oxobutano¡co acid. Preferably, the amine acceptor molecule in step a) of the method according to the invention for the production of an amine is provided in an amount of between 30 g / l (gram per liter) and 300 g / l, with greater preferably, between 30 g / l to 250 g / l, still more preferably, between 40 g / l to 250 g / l, even more preferably, between 50 g / l to 250 g / l. The amine donor molecule in step b) of the method according to the invention for the production of an amine is a molecule comprising an amine group that donates an amine group to the amine acceptor molecule, whereby an amine group of the amine donor molecule is converted to a carbonyl group. The amine donor molecule in step b) of the method according to the invention for the production of an amine can be a chiral, prochiral or non-chiral amine, preferably the amine donor molecule is an alkyl or aryl or aryl-alkyl amine chiral, prochiral or non-chiral, respectively, more preferably, the amine donor molecule is an amino acid or an alkyl amine. With regard to alkyl or aryl amines, the preferred amino donor molecule to be used in step b) of the method for the production of an amine according to the invention QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ are β-alanine, 1-propylamine, (racemic-) 2-butylamine, 6-aminohexanoic acid, isopropylamine, benzylamine, methylbenzylamine, 1-aminoindane, 1-methyl-3-phen¡ lprop¡na. In case the amino donor is a non-chiral amino acid, glycine is a preferred amino donor molecule to be provided in step b) of the method for the production of an amine according to the invention. In case the amino donor in step b) of the method for the production of an amine according to the invention is a chiral amino acid, the amino acid is preferably represented by its (SJ-enantiomer. The donor molecules Preferred amino acids having the (S) configuration to be provided in step b) of the method for the production of an amine according to the invention are (S)methylbenzylamine, (S / 1-aminoindane, (SJ-aspartic acid from ( S>1-methyl-3-phenylpropylamine, (S)asparagine, (SJ-alanine, (S / glutamine, (S / glutamic acid, (S / ornithine, (S / phosphoserine, (S) phenylalanine, (S>leucine, fS>tyrosine, (SJ-norvaline. The most preferred amino donor molecule to be provided in step b) of the method for the production of an amine according to the invention is isopropylamine. Isopropylamine, when used as an amino donor molecule in the methods according to the invention, is converted by the action of an ω-ΤΑ to acetone. Acetone is a volatile compound which leads to the advantage that it evaporates at relatively low temperatures. This allows the acetone produced by the ω-ΤΑ to be removed from the reaction mixture while the reaction is taking place, which leads to the advantageous effect that the reaction equilibrium is shifted towards the amine produced by the acetone production method. an amine according to the invention. This allows to obtain the desired amine in large amounts since the reverse reaction catalyzed by ω-ΤΑ is reduced due to the lack of a reaction partner. Preferably, the amine donor molecule in step b) of the method according to the invention for the production of an amine is provided in an amount of between 10 g / l (gram per liter) to 250 g / l, with greater preferably, between 15 g / l to 200 g / l, even more preferably, between 17 g / l to 180 g / l. In step c) of the method for the production of an amine according to the invention, the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) are brought into contact with a protein of according to the invention, preferably in solution. The solution can be an aqueous solution comprising only water, but it can also be a solution comprising water and organic solvents. In the case of contacting the protein according to the invention in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule provided in step a) and an amine donor molecule amine provided in step b) in an aqueous solution comprising an organic solvent, the organic solvent QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ is preferably selected from DMSO (dimethyl sulfoxide), DMAc (dimethylacetamide), DMF (dimethylformamide), acetonitrile, toluene, erc-butylmethylether, hexane, heptane. Most preferred are DMSO, DMAc and toluene. Preferably, the aqueous solutions comprising an organic solvent comprise the organic solvent in an amount of up to 10%, more preferably up to 20%, even more preferably up to 30%, still more preferably up to 40 %, most preferably, up to 50%. The use of aqueous solutions comprising an organic solvent has the advantage that, in case the amine acceptor molecule provided in step a) and / or the amine donor molecule provided in step b) of the method for the production of an amine according to the invention, has low solubility, their respective solubility can be improved, which leads to larger amounts of available substrates for ω-ΤΑ. This leads to a higher reaction rate, which means producing the desired amine in higher amounts in smaller volumes and in a shorter time, thus improving space-time yield. In case the protein according to the invention is contacted in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule provided in step a) and a donor molecule of amine provided in step b) in an aqueous solution, the solution preferably comprises a buffer system to adjust the pH. Preferred buffer systems are those comprising TRIS-HCI, MOPS, HEPES, TRIS, Bicine. Preferably, the pH of the aqueous solution in which the protein according to the invention is contacted in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule provided in the step a) and an amine donor molecule provided in step b) is adjusted to a value of between pH 4 to pH 11, more preferably, to a value of between pH 5 to pH 10, even more preferably, to a value between pH 6 to pH 10, even more preferably, up to a value between pH 7 to pH 10, even more preferably, up to a value between pH 8 to pH 10, most preferably, up to a value of between pH 8.5 to pH 9.5. Preferably, contacting the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) with a protein according to the invention in step c) of the method according to invention for the production of an amine takes place at a temperature between 10eC and 602C, more preferably between 20eC and 60eC, still more preferably between 25eC and 55eC, still more preferably between 30eC and 50eC, even with more preferably, between 30°C and 45°C, most preferably, between 342°C and 422°C. QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ The amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) are contacted with a protein according to the invention in step c) of the method for the production of an amine according to with the invention for a sufficient time to produce an amine. Preferably, the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) are brought into contact with a protein according to the invention in step c) of the method according to the invention for the production of an amine for 5 hours to 48 hours, more preferably 5 hours to 36 hours, even more preferably 5 hours to 30 hours, still more preferably 5 hours to 24 hours, even with more preferably, for 5 hours to 18 hours, most preferably, for 5 hours to 14 hours, and particularly preferably, for 5 hours to 13 hours. To contact the protein according to the invention in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule provided in step a) and the amine donor molecule provided in step step b), the protein can be contacted with an amine acceptor molecule and an amine donor molecule in different ways, preferably, the protein is contacted with an amine acceptor molecule and an amine donor molecule partially purified form or the protein is contacted with an amine acceptor molecule and an amine donor molecule in purified form or the protein is present in a crude cell extract when it is contacted with an amine acceptor molecule and an amine donor molecule amine or protein is contacted with an amine acceptor molecule and an amine donor molecule when present as a component of a living or non-living host cell. If the protein is contacted in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule and an amine donor molecule as a component of a host cell, the host cells can be those comprising the culture medium that was used to cultivate the host cells or the host cells may be free of the culture medium in which the host cells were cultured, or the host cells may have been (additionally) processed, preferably, the host cells are nearly free of the culture medium in which the host cells were grown, more preferably the host cells have been (additionally) processed, still more preferably the host cells are nearly free of the culture medium in which in which the host cells were cultured and in which the host cells have been (further) processed. Crude cell extract shall herein denote an extract obtained by means of the QLZLnn / Lznz / E / Yi QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ destruction of a living cell comprising all or substantially all inorganic or organic matter (including additional proteins and / or nucleic acid molecules) present in the cell. Partially purified shall herein mean a composition containing a protein that comprises (only) parts of the total organic or inorganic matter (including additional proteins and / or nucleic acid molecules) present in a living cell expressing the protein. A partially purified extract can be obtained, for example, by fractionating organic or inorganic matter from a crude cell extract by commonly known means such as centrifugation, filtration, any type of chromatographic separation, dialysis, etc. Fractionation of a crude cell extract can be carried out repeatedly using the same or different fractionation methods and can include precipitation steps. Purified shall herein denote a protein whose specific activity (the activity of the protein present in the dry weight fraction divided by the total amount of the material, in particular, other proteins in the dry weight fraction) cannot be increased by means of additional fractionation or purification steps. It is apparent from the commonly accepted definition given above for the term "purified" that "purified" can mean, but in most cases does not mean, that a protein is totally free of other inorganic and / or organic compounds. Preferably, purified shall mean herein that the protein according to the invention represents at least 95%, more preferably at least 96%, still more preferably at least 97%, still more preferably, at less than 98%, still more preferably at least 99%, most preferably at least 99.5% of the total amount of material by dry weight comprising the protein. The term "living cell" shall herein denote a cell that is capable of growing and / or reproducing. The term "non-living cell" shall herein mean a cell that is not capable of growing and / or reproducing. The non-living cells, even though they are not capable of reproducing and / or growing further, however, still show enzymatic activity, with respect to the present application, in particular, activity of a protein according to the invention having the activity of a ω-ΤΑ. The term culture medium free, as used herein, means that the culture medium used to grow a cell (host) has been removed, for example, by means of centrifugation and / or filtration. It is evident from the commonly accepted understanding given above for the term free from the culture medium that it can mean, but in most cases does not necessarily mean, that a cell is totally free of other inorganic and / or organic compounds that were present in the culture medium. Preferably, purified shall mean herein that the cell according to the invention represents at least 95%, more preferably at least 96%, still more preferably at least 97%, still more preferably at least 98%, still still more preferably at least 99%, most preferably at least 99.5% of the total amount of material in dry weight comprising the cell that is free from the culture medium. The term host cells have been (additionally) processed shall herein mean that host cells comprising a protein according to the invention have been treated by physical and / or chemical means prior to contacting in step c) of the method for the production of an amine according to the invention with an amine acceptor molecule and an amine donor molecule, preferably they have been treated with physical means, more preferably they have been dried, even more preferably they have have been freeze-dried or spray-dried, most preferably they have been spray-dried. Drying processes, in particular freeze-drying and spray-drying processes of the cells, are known to the person skilled in the art. Preferably, the host cells comprising a protein according to the invention have been freeze-dried or spray-dried, most preferably they have been spray-dried before contacting in step c) of the method for the production of an amine according to the invention by means of the method described herein under General Methods, item 9. It is known to a person skilled in the art that proteins having the activity of an ω-ΤΑ are pyridoxal phosphate (PLP) dependent enzymes. In a preferred embodiment, the protein is contacted in step c) of the method for producing an amine according to the invention with the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b ) in the presence of PLP, more preferably, the PLP is present in an amount between 0.05 g / l to 2.0 g / l, even more preferably, in an amount between 0.05 g / l to 1, 5 g / l, still more preferably, in an amount of between 0.05 g / l to 1.0 g / l, even more preferably, in an amount of between 0.075 g / l to 0.75 g / l, most preferably, in an amount of between 0.1 g / l to 0.5 g / l. Obtaining the amine in the obligatory step d) in the method for the production of an amine may mean that the amine is present in the composition of step d) without any further purification of the amine produced or it may mean that the amine produced is further purifies. The purification of the amine can be carried out by methods QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ known to a person skilled in the art. Such methods for purification of the amine include, but are not limited to, methods involving precipitation, methods including chromatography, distillation, extraction, adsorption, or filtration. A preferred embodiment of the method for the production of an amine according to the invention consists of a method for the production of a composition comprising an (S / amine in enantiomeric excess over its ff / amine (respective) comprising the steps of a) providing an amine acceptor molecule; b) providing an amine donor molecule; c) contacting the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) with a protein according to the invention; d) optionally, obtaining a composition comprising a ¿SJ-amine in enantiomeric excess over its (ñj-amine (respectively). The term "enantiomer" as used herein has the meaning commonly understood in the art of chemistry to be a molecule that is one of two stereoisomers that are structural mirror images of each other that are non-superimposable. The term Enantiomer is also commonly known as optical isomer. The term enantiomeric excess (commonly abbreviated to ee) is commonly understood in the technical field of chemistry and is used herein to specify the excess of one enantiomer in a composition over the respective other defined as the absolute difference between the mole fractions of each enantiomer. Often, enantiomeric excess is expressed in the art as percent enantiomeric excess. As an example, a composition comprising 70% of an fS / enantiomer and 30% of a (TTJ-enantiomer has, relative to the (SJ-enantiomer, an ee = 40% (40% ('SJ-enantiomer pure + 60% racemic (= 30% (S) + 30% (R)).In conclusion, the mixtures of racemic enantiomers have an ee = 0%, the pure (S)- or (F?>enantiomers have a ee = 100%. A preferred embodiment of the method according to the invention for the production of a composition comprising an / Si-amine in enantiomeric excess consists in a method for the production of an aliphatic fSJ-amine (including, but not limited to, alkane linear, branched or cyclic amines, alkene amines, alkyne amines) in enantiomeric excess or consists of a method for the production of an aryl (S>amine in enantiomeric excess or consists of a method for the production of an SJ-amino acid in excess enantiomeric, more preferably, in a method for the production of an enantiomeric excess (S)-α-amino acid, even more preferably, in a method for the production of a (S)-α-branched amino acid, an (S)- aromatic α-amino acid or a (S)-a QLZLnn / Lznz / E / Yi aromatic amino acid comprising enantiomeric excess substituted phenyl groups, most preferably, in a method for the production of the amino acids (S>norvalin, (S)leucine, (Sj-phenylalanine or (S) >t¡ros¡na in enantiomeric excess. With regard to ω-ΤΑ variants according to the invention comprising additional amino acid modifications, the method according to the invention for the production of a composition comprising an (SJ-amine in enantiomeric excess is preferably a method for the production of an aliphatic (S>amine comprising phosphorus (including, but not limited to, an alkane (S>amine, alkene (SJ-amine, alkyne (S>linear amine, branched or cyclic comprising phosphorus) in enantiomeric excess or is a method for the production of an aryl (S / amine comprising phosphorus in enantiomeric excess or is a method for the production of an (S>amino acid comprising phosphorus in enantiomeric excess, more preferably, a method for the production of a (S)-α-amino acid comprising phosphorus in enantiomeric excess, even more preferably, a method for the production of a (S)-α-branched amino acid comprising phosphorus, a (S)-α-phosphorus-comprising aromatic amino acid or a phosphorus-comprising (S)-α-aromatic amino acid comprising substituted phenyl groups in enantiomeric excess, still more preferably, a method for the production of a (S)-α -amino acid comprising phosphorus in enantiomeric excess, even more preferably, a method for the production of an (S)-a amino acid comprising methyl-substituted phosphorus in enantiomeric excess, most preferably, a method for the production of (SJ -glufosinate in enantiomeric excess. Another preferred embodiment of the method according to the invention for the production of a composition comprising an (SJ-amine in enantiomeric excess, consists of a method for the production of a composition comprising an (S>amine in an enantiomeric excess (ee ) of at least 20%, more preferably, at least 40%, even more preferably, at least 60%, even more preferably, at least 80%, even more preferably, at least 90% , with particular preference, at least 94%, most preferably, at least 96% or with particular preference, at least 98%. What has been defined herein above with respect to the preferred embodiments of amine acceptor molecules to be provided and the preferred embodiments of the amounts to be provided in step a) and the preferred embodiments of the amine donor molecule to be provided and Preferred embodiments of the amounts to be provided in step b) of the method according to the invention for the production of an amine is applicable accordingly to the amine acceptor molecule in step a) and to the amine donor molecule in step b ), respectively, in the method for the production of a composition comprising an (SJ-amine in enantiomeric excess over its (respective) (RJ-amine). However, it is evident that in the case that the amine donor molecules a provided in step b) in the method for the production of a composition comprising an (SJ-amine in enantiomeric excess over its (respective) (phy / amine) is a chiral molecule, at least one mixture of enantiomers is provided comprising a (S)stereoisomer of the amine donor, preferably a racemic mixture of an amine donor is provided If available and cost-effective, the chiral amine donor can preferably be provided in a mixture where the ( S)stereoisomer is in enantiomeric excess, more preferably, the amine donor can be provided as a composition comprising the (SJ-stereoisomer in high enantiomeric excess, in which case high enantiomeric excess means an enantiomeric excess of at least 30%, more preferably, at least 40%, even more preferably, at least 60%, even more preferably, at least 80%, even more preferably, at least 90%, particularly preferably, at least 94%, with great preference, at least 96% or with special preference, at least 98%. What has been defined herein above with respect to preferred embodiments of solutions, aqueous solutions, aqueous solutions comprising organic solvents, buffer systems, pH values ​​and / or temperature, the form of the protein (crude cell extract, protein partially purified, purified protein, protein present as a component of a living or non-living host cell, host cell processed (additionally), spray-dried host cell), the amount of protein and the presence and amount of PLP relative to step c) of the method according to the invention for the production of an amine is applicable according to step c) of the method for the production of a composition comprising an (SJ-amine in enantiomeric excess over its (fl / amine (respective). What has been defined herein above with respect to the preferred embodiments of step d) of the method according to the invention for the production of an amine is applicable according to step d) of the method for the production of a composition containing comprises an (SJ-amine in enantiomeric excess over its (fíj-amine (respectively). In addition to what has been defined for step d) of the method according to the invention for the production of an amine, preferably, a composition is obtained comprising an (S / amine in an enantiomeric excess of at least 40%, more preferably, at least 70%, even more preferably, at least 80%, even more preferably, at least 90%, even more preferably, at least 95%, particularly preferably, at least of 97%, most preferably, of at least 98% or with particular preference, of at least 99% in step d) of the method for the production of a composition comprising an (S / amine in enantiomeric excess over its (fixed -amine (respective). The proteins according to the invention can also be used in methods for QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ decrease or eliminate a stereoisomer from compositions comprising (R)- and (S)-amine stereoisomers. The protein-catalyzed reaction according to the invention, when decreasing or eliminating a stereoisomer from compositions comprising (R)- and (S)-amine isomers follows the general equation (la). Compared to the reaction for the synthesis of amines (see equation (I)), it can be seen that the amino donor and amino acceptors are exchanged with each other in reactions that decrease or eliminate a stereoisomer from compositions comprising ( R)- and (S)-amines (see equation (la)) The reaction according to equation (la) has the advantage that specific stereoisomers can be enriched in compositions comprising different stereoisomers or, in other words, specific stereoisomers can be removed from a composition, sometimes also referred to in the art as resolving a mixture of enantiomers. These methods are of particular importance in cases where a compound is produced by chemical synthesis, which commonly leads to a racemic mixture. The chemical synthesis of said compound may be the desired production process in terms of economics of the process or for other reasons. However, the separation of chemically produced enantiomers can be difficult, expensive, or even not possible. The proteins according to the invention can be used to selectively eliminate a stereoisomer from said chemically produced racemic mixtures. A further embodiment of the invention, therefore, pertains to a method for decreasing the amount of an amine enantiomer in a composition comprising (R)amines and (SJ-amines), comprising the steps of a) providing a composition comprising enantiomers of (fij-amine and (S)amine b) providing an amine acceptor molecule; c) contacting the composition provided in step a) and the amine accept provided in step b) with a protein according to the invention; d) optionally, obtaining a composition in which the amount of an amine enantiomer decreases compared to the amount present in the composition provided in step a). In the method of decreasing the amount of an amine enantiomer in a composition comprising (?j-amines and (Sj-amines, the amount of structurally different (?j-amine and ?SJ-amine molecules that are present in the composition provided in step a) of each of these methods, provided that at least one molecule of ¿SJ-amine and (Ή / amine. The composition comprising (R)- and (S)-amines provided in step a) of the method for decreasing the amount of an amine enantiomer in a composition containing QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ comprises (R)- and (S)-amines comprises at least one (f?>amine and at least one (SJ-amine, wherein the at least one (fij-amine and the at least one (S / amine may be stereoisomers of the same molecule or the at least one (fj-amine and the at least one (SJ-amine may be stereoisomers of structurally different molecules. A preferred embodiment of a method for decreasing the amount of an amine enantiomer in a composition comprising (phy>amines and (SJ-amines) consists of a method for decreasing the amount of an aliphatic amine enantiomer (including, but not limited to linear, branched, or cyclic alkane amines, alkene amines, alkyne amines) or is a method of decreasing the amount of an enantiomer of an aryl amine or is a method of decreasing the amount of an enantiomer of an amino acid, with greater preferably, a method of decreasing the amount of an enantiomer of an α-amino acid, even more preferably, a method of decreasing the amount of enantiomer of a branched α-amino acid, an enantiomer of an aromatic α-amino acid, or an enantiomer of a aromatic α-amino acid comprising substituted phenyl groups, most preferably a method of decreasing the amount of an enantiomer of the amino acids selected from norvaline, leucine, phenylalanine or tyrosine. With respect to ω-ΤΑ variants comprising additional amino acid modifications according to the invention, the method according to the invention for decreasing the amount of an amine enantiomer in a composition comprising (R)- and (Si- amines is preferably a method of decreasing the amount of an enantiomer of a phosphorus-containing aliphatic amine (including, but not limited to, a phosphorus-containing linear, branched or cyclic alkane amine, alkene amine, alkyne amine) o is a method of decreasing the amount of an enantiomer of a phosphorus-containing aryl amine o is a method of decreasing the amount of an enantiomer of a phosphorous-containing amino acid, more preferably, a method of decreasing the amount of an enantiomer of a phosphorus-comprising α-amino acid, even more preferably, a method of decreasing the amount of an enantiomer of a phosphorus-comprising branched α-amino acid, an enantiomer of a phosphorus-comprising aromatic α-amino acid or an enantiomer of an aromatic phosphorus-comprising α-amino acid phosphorus comprising substituted phenyl groups, still more preferably, a method of decreasing the amount of an enantiomer of an a-amino acid comprising substituted phosphorus, even more preferably, a method of decreasing the amount of an enantiomer of an α-amino acid that comprises a methyl substituted phosphorus, most preferably a method of decreasing the amount of a glufosinate enantiomer. What has been defined herein above with respect to preferred embodiments of solutions, aqueous solutions, aqueous solutions comprising solvents QL7 Lnn / L7í17 / E / Yli organic, buffer systems, pH values ​​and / or temperature, the form of the protein (crude cell extract, partially purified protein, purified protein, protein present as a component of a living host cell or not live, host cell processed (additionally), spray dried host cell), the amount of protein and the presence and amount of PLP in connection with step c) of the method according to the invention for the production of an amine is applicable according to step c) of the method for decreasing the amount of amine enantiomer in a composition comprising (RJ-amines and (S>amines. What has been defined herein above with respect to the preferred embodiments of step d) of the method according to the invention for the production of an amine is applicable according to step d) of the method for decreasing the amount of enantiomer of amine in a composition comprising (RJ-amines and (SJ-amines. The proteins according to the invention can be used in particular in methods to decrease the amount of or to substantially or nearly totally eliminate (S)enantiomers from compositions comprising (RJ-amine and (S)amine) stereoisomers, producing by Consequently compositions in which a (RJ-amine is present in enantiomeric excess. The respective reaction catalyzed in the methods for the production of enantiomerically enriched or nearly enantiomerically pure amines by means of formally selective ωTAs (Sj-can be described by the general equation ( II) R1-CH((S,RJ-NH2)-R2+ R3-CO-R4R1-CO-R2+ R3-CH((R)-NH2)-R4 Many compounds that have biological activity, such as medicines, active compounds used in agronomy, complementary food additives, feed additives, etc. They exist as enantiomers. In the vast majority of cases, only one of the enantiomers has the desired biological activity and the other is inactive or often even has unwanted side effects. Today, numerous compounds that have biological activity and that are used as medicines, in agronomy, as supplementary food or feed additives (for example, amino acids) can only be produced or can be produced only under economically viable conditions by means of chemical synthesis with the disadvantage that these compounds are only available as racemic mixtures. The proteins according to the invention provide the advantage that the amount of (Sj-amines can be partially, significantly or almost totally removed from said racemic mixtures, with the effect that compositions comprising the biologically active enantiomer or a precursor for used in a production process of biological active enantiomers in access or comprising the biological active enantiomer or a precursor thereof in a composition that is almost free of the inactive enantiomer This reduces side effects in medicines, in products used in agronomy or in products comprising complementary foods or feed additives. QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ In a preferred embodiment, the method for decreasing the amount of an amine enantiomer in a composition comprising fR>amine and fS>amine enantiomers consists of a method for decreasing the amount of an fSJ-amine enantiomer in a composition comprising fR / amines and fS>amines comprising the steps of a) providing a composition comprising (RJ-amines and fS / amines; b) providing an amine acceptor molecule; c) contacting the composition provided in step a) and the amine acceptor molecule provided in step b) with a protein according to the invention; d) optionally, obtaining a composition in which the amount of an fS>amine enantiomer is decreased compared to the amount present in the composition provided in step a). A preferred embodiment of the method for decreasing the amount of an / S / amine enantiomer in a composition comprising (R)- and (S / amine) enantiomers consists of a method for decreasing the amount of an fS>aliphatic amine (including , but not limited to, alkane (S]-amines, alkene (S / amines, linear, branched, or cyclic alkyne / S / amines) or is a method of decreasing the amount of an aryl fSJ-amine or of decreasing the amount of a (SZ-amino acid, more preferably, a method of decreasing the amount of a (S)-a-amino acid, still more preferably, a method of decreasing the amount of a (S)-a branched-chain amino acid, a (S)- α-aromatic amino acid or an (S)- α-aromatic amino acid comprising substituted phenyl groups, most preferably, a method of decreasing the amount of the selected amino acids of fSf-norvaline, / Sj-leucine, (SJ-phenylalanine or ( S)tyrosine. With respect to ω-ΤΑ vanants comprising additional amino acid modifications according to the invention, the method according to the invention for decreasing the amount of a ¿S / amine enantiomer in a composition comprising (R)- and (S)amines is preferably a method of decreasing the amount of a phosphorus-comprising aliphatic (SJ-amine (including, but not limited to, an alkane / Sj-amine, alkene fS>amine, alkyne / Sj -linear, branched or cyclic amine comprising phosphorus) or is a method of decreasing the amount of an aryl fS>amine comprising phosphorus or is a method of decreasing the amount of a (Sj-amino acid comprising phosphorus, with higher preferably, a method of decreasing the amount of a (S)-α-amino acid comprising phosphorus, even more preferably, a method of decreasing the amount of a (S)-α-branched amino acid comprising phosphorus, an (S) - phosphorus-comprising aromatic α-amino acid or a phosphorus-comprising (S)-α-aromatic amino acid comprising substituted phenyl groups, still more preferably, a method of decreasing the amount of a phosphorus-comprising (S)-α-amino acid, even more preferably, a method of decreasing the QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ amount of a (S)-α-amino acid comprising a methyl-substituted phosphorus, most preferably a method of decreasing the amount of (S1-glufosinate. Preferably, the composition comprising (R)- and (S1-amines provided in step a) of each of the methods for decreasing the amount of amine enantiomer in a composition comprising (RJ-amines and (S1 -amines or the method for decreasing the amount of an enantiomer of (S1-amine in a composition comprising (R1-amines and (S1-amines) comprising (R)- and / or (S1-amines selected from the group of compounds selected from (R)- and (S1-aliphatic amines (including, but not limited to, alkane (R)- and (Si-amines, alkene (R)- and (S / amines, linear, branched or cyclic alkyne (R)- and (S1-amines) or aryl (R)- and (S1-amines or (R)- and (S1-amino acids, more preferably, (R)- and (S)-a amino acids, even more preferably, (R)- and (S)- α-branched amino acids, (R)- and (S)- a aromatic amino acids or (R)- and (S) - aromatic α-amino acids comprising substituted phenyl groups, most preferably the amino acids (R)- and (S1-norvaline, (R)- and (S1-leucine, (R)- and (S1-phenylalanine or (R)- and (S1-tyrosine. With respect to the ω-ΤΑ variants according to the invention that comprise additional amino acid modifications, preferably, the composition comprising (R)- and (S1-amines provided in step a) of each of the methods for decreasing the amount of an amine enantiomer in a composition comprising (R1-amines and (S)amines or the method for decreasing the amount of an (S1-amine enantiomer in a composition comprising (R1-amines and (S1-amines) comprises (R)- and / or (S1-amines from the group of compounds selected from (R)- and (S1-amines) aliphatic phosphorus-comprising (including, but not limited to a, alkane (R)- and (Si-amines, alkene (R)- and (S1-amines, alkyne (R) and (linear, branched or cyclic S1-amines containing phosphorus) or aryl (R )- and (Si-phosphorus-comprising amines or (R)-y (Si-phosphorus-comprising amino acids, more preferably, (R)- and (S)- α-phosphorus-comprising amino acids, even more preferably (R ) and (S)- α-phosphorus-containing branched amino acids, (R)- and (S)- phosphorus-containing α-aromatic amino acids or (R)- and (S)- phosphorus-containing α-aromatic amino acids comprising groups substituted phenyl, still more preferably, R)- and (S)-a-amino acids comprising substituted phosphorus, still even more preferably, (R)- and (S)-a-amino acids comprising a methyl substituted phosphorus, with sum preferably, (R)- and (S)glufosinate. More preferably, the composition comprising (R)- and (S1-amines provided in step a) of each of the methods for decreasing the amount of an amine enantiomer in a composition comprising (R)- and (S1-amines or the method for decreasing the amount of an enantiomer of (S1-amine in a composition comprising (R) and (S1-amines) comprises (R)- and (S1-amines of the same molecule, more preferably, it comprises (R)- and (S>amines each representing an enantiomer of a single compound selected from the group of compounds consisting of (R)- and (SJ-aliphatic amines ( including, but not limited to, alkane (R)- and (SJ-amines, alkene (R)- and (SJ-amines, linear, branched or cyclic alkyne (R)- and (S)amines) or aryl ( R)- and (Sj-amines or (R)- and (S>amino acids, more preferably, (R)- and (S)- «-amino acids, even more preferably, (R)- and (S)- a-branched amino acids, (R)- and (S)- a-aromatic amino acids or (R)- and (S)- a-aromatic amino acids comprising substituted phenyl groups, most preferably the amino acids (R)- and (S> norvaline, (R)- and (SJ-leucine, (R)- and (S>phenylalanine or (R)- and (SJ-tyrosine. With respect to the ω-ΤΑ variants according to the invention that comprise additional amino acid modifications, preferably, the composition comprising (R)- and (S>amines provided in step a) of each of the methods for decreasing the amount of amine enantiomer in a composition comprising (R)- and (SJ-amines or the method of decreasing the amount of an (SJ-amine enantiomer in a composition comprising (R)- and (SJ-amines , comprises (R)- and (SJ-amines of the same molecule, more preferably, it comprises (R)- and (SJ-amines each representing an enantiomer of a single compound selected from the group of compounds consisting of (R )- and (S>phosphorus-comprising aliphatic amines (including, but not limited to, alkane (R)- and (SJ-amines, alkene (R)- and (S)-amines, alkyne (R)- and (S>linear, branched or cyclic amines comprising phosphorus) or aryl (R)- and (SJ-amines comprising phosphorus or (R)- and (SJ-amino acids comprising phosphorus, more preferably, (R)- and (S)-α-amino acids comprising phosphorus, even more preferably, (R)- and (S)-«-branched amino acids comprising phosphorus, (R)- and (S)-«-aromatic amino acids comprising phosphorus or (R)- and (S)-a phosphorus-comprising aromatic amino acids comprising substituted phenyl groups, still more preferably, (R)- and (S)-«-substituted phosphorus-comprising amino acids, still more preferably, (R )- and (S)- α-amino acids comprising methyl-substituted phosphorus, most preferably (R)- and (SJ-glufosinate. Preferably, the amine acceptor molecule provided in step b) of each of the methods for decreasing the amount of an amine enantiomer in a composition comprising (phy>amines and (S^-amines) or the method for decrease the amount of an enantiomer of (SJ-amine in a composition comprising (fj-amines and (SJ-amines is a molecule whose structure corresponds to the structure described as an amine donor molecule herein above to be provided in step b ) of the method for the production of an amine as an amine donor in addition to the amine group of those molecules described as amine donor molecule herein above to be provided in step b) of the method for the production of an amine is replaced by a carbonyl group.As an example, the replacement of the amine group of the isopropylamine described QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ as an amine donor molecule to be provided in step b) of the method for the production of an amine by means of a carbonyl group, leads to the corresponding acetone amine acceptor molecule to be used in step b) each of the methods for decreasing the amount of an amine enantiomer in a composition comprising (R)amines and ('Sj-amines) or the method for decreasing the amount of an fSJ-amine enantiomer in a composition comprising it comprises ffíj-amines and fSj-amines. The most preferred amine acceptor molecule provided in step b) of each of the methods for decreasing the amount of an amine enantiomer in a composition comprising (T^-amines and fS / amines or the method for decreasing the amount of an enantiomer of (S / amine in a composition comprising (Ή / amines and (Sj-amines is acetone. What has been defined herein above with respect to preferred embodiments of solutions, aqueous solutions, aqueous solutions comprising organic solvents, buffer systems, pH values ​​and / or temperature, the form of the protein (crude cell extract, protein partially purified, purified protein, protein present as a component of a living or non-living host cell, host cell processed (additionally), spray-dried host cell), the amount of protein and the presence and amount of PLP relative to step c) of the method according to the invention for the production of an amine is applicable according to step c) of the method for decreasing the amount of an enantiomer of ¿SJ-amine in a composition comprising (Ή / amines and SJ-amines. What has been defined herein above with respect to the preferred embodiments of step d) of the method according to the invention for the production of an amine is applicable according to step d) of the method for decreasing the amount of an enantiomer of / SJ-amine in a composition comprising (Ή / amines and ('SJ-amines. A further embodiment of the invention consists in the use of proteins according to the invention for the production of an amine, preferably for the production of an (S)amine. The use of proteins according to the invention to decrease the amount of an amine, preferably the amount of a / SJ-amine in an enantiomeric mixture is also an embodiment of the invention. The use of nucleic acid molecules according to the invention to express a protein according to the invention in a host cell according to the invention is also an embodiment of the invention. Another embodiment of the invention concerns the use of nucleic acid molecules according to the invention, recombinant nucleic acid molecules according to the invention, plasmids according to the invention, or vectors according to the invention, to transform or genetically modify a host cell according to the invention or for QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ the production of a protein according to the invention. The use of a host cell according to the invention for the production of an amine or to decrease the amount of an amine, preferably the amount of a (SJ-amine in an enantiomeric mixture, is also an embodiment of the invention. QLZLnn / Lznz / B / Yi Description of the Sequences Throughout the application, nucleotide and amino acid abbreviations are used according to the following IUPAC codes: IUPAC Nucleotide Code Base A Adenine C Cytosine G Guanine T(oU) Thymine (or Uracil) R Ao G Y CoT S GoC w Ao T K G oT M AoC B C or G or T D A or G or T H A or C or T V A or C or G N any base - space Table 3 For discrimination between amino acids and nucleotides, the upper case nucleotide code abbreviations provided in the Table above are written here in lower case. IUPAC Amino Acid Code Three Letter Code Amino Acid A Ala Alanine C Cys Cysteine ​​D Asp Aspartic Acid E Glu Glutamic Acid F Phe Phenylalanine G Gly Glycine H His Histidine I lie Isoleucine K Lys Lysine L Leu Leucine M Met Methionine N Asn Asparagine P Pro Proline Q Gln Glutamine R Arg Arginine S Ser Serine T Thr Threonine V Val Valine w Trp Tryptophan Y Tyr Tyrosine QLZLnn / Lznz / E / Yi Table 4 The codon usage herein follows the so-called general genetic code according to the following Table, where t is to be substituted for u in ribonucleic acid (RNA) sequences. "TLC" means Three Letter Code and "SLC" means Single Letter Amino Acid Code. Amino acid TLC SLC DNA codons Codons due to degenerate genetic code Alanine Ala A gca gene Alanine Ala A gcc gene Alanine Ala A gcg gene Alanine Ala A gct gene Arginine Arg R aga mgn Arginine Arg R agg mgn Arginine Arg R cga mgn Arginine Arg R cgc mgn Arginine Arg R cgg mgn Arginine Arg R cgt mgn Asparagine Asn N aac aay Asparagine Asn N aat aay Aspartic Acid Asp D gao gay Aspartic Acid Asp D gat gay Cysteine ​​Cys C tgc tgy Cysteine ​​Cys C tgt tgy Glutamic Acid Glu E gaa gar Glutamic Acid Glu E gag gar Glutamine Gln Q caa car Glutamine Gln Q cag car Glycine Gly G gga gg Glycine Gly G ggc gg Glycine Gly G ggg ggn Glycine Gly G ggt ggn Histidine His H cae cay Histidine His H cat cay Isoleucine lie I ata ath Isoleucine lie I ate ath Isoleucine lie I att ath Leucine Leu L cta ytn Leucine Leu L etc ytn Leucine Leu L ctg ytn Leucine Leu L ctt ytn Leucine Leu L tta ytn Leucine Leu L ttg ytn Lysine Lys K aaa aar Lysine Lys K aag aar Methionine Met M atg atg Phenylalanine Phe F ttc tty Phenylalanine Phe F ttt tty Proline Pro P cea ccn Proline Pro P ccc ccn Proline Pro P ceg ccn Proline Pro P cct ccn Serine Ser s age wsn Serine Ser s agt wsn Serine Ser s tea wsn Serine Ser s tcc wsn Serine Ser s teg wsn Serine Ser s tet wsn Threonine Thr T aca acn Threonine Thr T ace acn Threonine Thr T acg acn Threonine Thr T act acn Tryptophan Thr w tgg tgg Tyrosine Tyr Y tac tay Tyrosine Tyr Y tat tay Valine Val V gta gtn Valine Val V gtc gtn QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ Valine Val V gtg gtn Valine Val V gtt gtn Stop codons Termination Termination taa trr Stop codons Termination Termination tag trr Termination codons Termination Termination tga trr Table 5 QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ SEQ ID NO 1: Nucleic acid sequence encoding an omega-transaminase (ω-ΤΑ) from Bacillus megaterium obtained by back-translation of the amino acid sequence shown under SEQ ID NO 3, where the back-translation follows the principle of translation due to the degeneracy of the general genetic code. Nucleotides at positions 1432 to 1449 encoding six His amino acids were inserted into the sequence from Bacillus megaterium prior to the termination or stop codon located at positions 1450 to 1452. SEQ ID NO 2: Nucleic acid sequence encoding an ω-ΤΑ from Bacillus megaterium having the amino acid sequence as shown under SEQ ID NO 3. Nucleotides at positions 1432 to 1449 encoding six His amino acids were inserted within the sequence from Bacillus megaterium before the termination or stop codon located at positions 1450 to 1452. SEQ ID NO 3: Amino acid sequence of an ω-ΤΑ from Bacillus megaterium derived from GenPept (PDB) under Accession No. 5G09_A. The amino acid shown is encoded by the nucleic acid sequences as shown under SEQ ID NOs 1 and 2. The six His amino acids at positions 478 to 483 were inserted into the sequence from Bacillus megaterium by modification of sequence. SEQ ID NO 4: Nucleic acid sequence encoding an ω-ΤΑ from Arthrobacter sp. obtained by back-translation of the amino acid sequence shown under SEQ ID NO 6, wherein the back-translation follows the principle of translation due to the degeneracy of the general genetic code. SEQ ID NO 5: Nucleic acid sequence encoding an ω-ΤΑ from Arthrobacter sp. having the amino acid sequence as shown under SEQ ID NO 6. Nucleotides at positions 1438 to 1455 encoding six His amino acids were inserted into the sequence from Arthrobacter sp. before the termination or stop codon located at positions 1456 to 1458. SEQ ID NO 6: Amino acid sequence of an ω-ΤΑ from Arthrobacter sp. which is derived from GenPept (PDB) under Accession No. 5G2P A. The amino acid shown is encoded by nucleic acid sequences as shown under SEQ ID NOs 4 and 5. The six His amino acids at positions 480 to 485 were inserted into the sequence from Arthrobacter sp. by means of sequence modification. SEQ ID NO 7: Nucleic acid sequence encoding an ω-ΤΑ from Bacillus sp. (soil 76801D1 obtained by back-translating the amino acid sequence shown under SEQ ID NO 9, wherein the back-translation follows the translation principle due to the degeneracy of the general genetic code. SEQ ID NO 8: Nucleic acid sequence encoding an ω-ΤΑ from Bacillus sp. (soil 76801D1 derived from GenBank accession No. LMTA01000079.1. SEQ ID NO 9: Amino acid sequence of an ω-ΤΑ from Bacillus sp. (soil 76801D1 which is derived from GenPept (PDB) under Accession No. KRF52528.1. The amino shown is encoded by nucleic acid sequences as shown under SEQ ID NOs 7 and 8, described herein above. SEQ ID NO 10: Nucleic acid sequence encoding a mutated ω-ΤΑ from Arthrobacter sp. obtained by back-translation of the amino acid sequence shown under SEQ ID NO 12, wherein the back-translation follows the principle of translation due to the degeneracy of the general genetic code. SEQ ID NO 11: Nucleic acid sequence encoding a mutated ω-ΤΑ variant from Arthrobacter sp. having the amino acid sequence as shown under SEQ ID NO 12. The sequence is derived from SEQ ID NO 15 in WO 2006 / 063336 A2. SEQ ID NO 12: Amino acid sequence of a mutated ω-ΤΑ from Arthrobacter sp. which derives from SEQ ID NO 16 in WO 2006 / 06336 A2. The amino acid shown is encoded by nucleic acid sequences as shown under SEQ ID NOs 11 and 12, described herein above. SEQ ID NO 13: Nucleic acid sequence encoding a wild type ω-ΤΑ from Arthrobacter sp. obtained by back-translation of the amino acid sequence shown under SEQ ID NO 15, wherein the back-translation follows the principle of translation due to the degeneracy of the general genetic code. SEQ ID NO 14: Nucleic acid sequence encoding a wild-type ω-ΤΑ from Arthrobacter sp. having the amino acid sequence as shown under SEQ ID NO 15. The sequence is derived from SEQ ID NO 1 in WO 2006 / 063336 A2. SEQ ID NO 15: Amino acid sequence of a wild type ω-ΤΑ from Arthrobacter sp. which is derived from SEQ ID NO 2 in WO 2006 / 06336 A2. The amino acid shown is encoded by nucleic acid sequences as shown under SEQ ID NOs 13 and 14, described herein above. SEQ ID NO 16: Nucleic acid sequence encoding an improved ω-ΤΑ obtained by back-translation of the amino acid sequence shown below QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ SEQ ID NO 18, wherein the back translation follows the translation principle due to the degeneracy of the general genetic code. SEQ ID NO 17: Nucleic acid sequence encoding an improved ω-ΤΑ having the amino acid sequence as shown under SEQ ID NO 18. SEQ ID NO 18: Amino acid sequence of an improved ω-ΤΑ, where improvements are obtained by amino acid substitutions compared to the amino acid sequences from Bacillus megaterium shown under SEQ ID NOs 3 and 9 and compared to amino acid sequences from Arthrobacter sp. which are shown under SEQ ID NO 6, 12 and 15. SEQ ID NO 19: Sequence encoding nucleic acids of the D-amino acid oxidase (DAO1) gene from Rhodotorula toruloides (synonym: Rhodotorula gracilis). SEQ ID NO 20: Amino acid sequence of the protein that has D-amino acid oxidase (DAO1) activity obtained from the coding sequence shown under SEQ ID NO 19. SEQ ID NO 21: Sequence encoding nucleic acids for a variant of the D-amino acid oxidase (DAO1) gene from Rhodotorula toruloides comprising, compared to the nucleic acid sequence from Rhodotorula toruloides, substitutions (replacements) of nucleotides at codons identified by nucleotide positions 160-162 and codons identified by nucleotide positions 172174 and codons identified by nucleotide positions 637-639. SEQ ID NO 22: Amino acid sequence of the protein having D-amino acid oxidase activity obtained from the coding sequence shown under SEQ ID NO 21. The amino acid sequence comprises substitutions (replacements) of amino acids compared to the nucleic acid sequence from Rhodotorula toruloides at positions 54, 58 and 213, compared to the amino acid sequence shown under SEQ ID NO 21 and is therefore an amino acid sequence of a variant of DAAO (mutant). SEQ ID NO 23: Sequence encoding nucleic acids of a catalase gene from Listeria seeligeri. SEQ ID NO 24: Amino acid sequence of the protein that has catalase activity obtained from the coding sequence shown under SEQ ID NO 23. SEQ ID NO 25: Nucleic acid sequence encoding the protein having the amino acid sequence shown under SEQ ID NO 24 with the activity of a catalase. SEQ ID NO 26: Nucleic acid sequence of the designated genetic element QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ lac operator in Fig. 1. SEQ ID NO 27: Nucleic acid sequence of the genetic element designated Trc promoter in Fig. 1. SEQ ID NO 28: Nucleic acid sequence of the genetic element designated rrnB in Fig. 1. SEQ ID NO 29: Nucleic acid sequence of the genetic element designated cistron in Fig. 1. SEQ ID NO 30: Nucleic acid sequence of the genetic element designated rrnB terminator in Fig. 1. DESCRIPTION OF THE FIGURES Fig. 1: Map of plasmids showing the genetic elements used for the expression of proteins that have the activity of a DAAO, ω-ΤΑ and catalase from a single operon as tri-cistronic RNA. Explanations of the abbreviations of the regulatory genetic elements involved in the transcription and translation of tri-cistronic RNA: lac operator: Ullmann, 2001, Encyclopedia of Life Sciences, John Wiley & Sons, Ltd, ISBN: 9780470015902; Ullmann, 2009, Encyclopedia of Life Sciences (ELS), John Wiley & Sons, Ltd: Chichester. DOI: 10.1002 / 9780470015902.a0000849.pub2; consisting of the nucleic acid sequence shown under SEQ ID NO 26. Trc promoter: Synthesis promoter derived from E.coli trp and / acUV5 promoters (Brosius et al., 1985, Rev de Quím Biol 260, 3539-3541); consisting of the nucleic acid sequence shown under SEQ ID NO 27. rrnB: Rho! independent transcription termination signal (Pfeiffer & Hartmann, 1997, Rev de Quím Biol 265(4) 385-393; Orosz et al., 1991, Rev Eur de Bioquím. 201(3), 653-659); consisting of the nucleic acid sequence shown under SEQ ID NO 28. t7 enhancer: Transcription enhancer sequence from the t7 gene. (Sequence used: ttaacttta). RBS1: Ribosome binding site (Sequence: gaggt). cistron: transcription termination sequence; consisting of the nucleic acid sequence shown under SEQ ID NO 29. RBS2: Ribosome binding site (Sequence used: aaggag). boxA: transcription antitermination sequence (Sequence used: tgctctttaacaa). cistron: Synthetic cistron consisting of the nucleic acid sequence shown under SEQ ID NO 29. rrnB terminator: Transcription termination signal; which consists of the QL7 Líin / LZAZ / E / Yli nucleic acid sequence shown under SEQ ID NO 30. T2 terminator: Translation termination signal (Orosz et al., 1991, Rev Eur de Bioquím. 201(3), 653-659). Fig. 2: Presents the production of (S>norvallin via 2-oxovalenco amination catalyzed by wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 6 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 3 compared to ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18. Fig. 3: Presents the production of fSJ-leucine via wild-type ω-ΤΑ protein-catalyzed amination of 4-methyl-2-oxo-valeric acid from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 6 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 3 compared to ω-ΤΑ variants having the amino acid sequence which is shown under SEQ ID NO 18. Fig. 4: Presents the production of (SJ-phenylalanine via phenylpyruvic acid amination catalyzed by wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 6 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 3 as compared to ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18. Fig. 5: Presents the production of (SJ-tyrosine via amination of phydroxyphenylpyruvic acid catalyzed by wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 6 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 3 as compared to ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18. GENERAL METHODS 1. Production of ω-ΤΑ Variants and ω-ΤΑ Variants Having Additional Amino Acid Modifications Known nucleotide sequences described herein that encode proteins having the activity of an ω-ΤΑ described herein were synthesized by the service provider Eurofins Genomics GmbH (Eurofins Genomics GmbH, Anzinger Str. 7a, 85560 Ebersberg, Germany ). Nucleotide substitutions (replacements) were introduced within the nucleic acid sequences shown under SEQ ID Nos 2, 5, 8, 11, 14. The replacement can QLZLnn / Lznz / B / Yi be effected on the nucleic acid sequences encoding the reference polypeptide by any means that is appropriate to replace nucleotides in nucleic acid sequences. Those methods are widely described in the literature and are well known to the person skilled in the respective sequence. Various molecular biology methods can be used to achieve the respective nucleotide replacements. A useful method for preparing a mutated nucleic acid sequence according to the invention and the corresponding protein comprises carrying out site-directed mutagenesis at codons encoding one or more amino acids that are selected in advance, thereby changing the codons. selected so that they code for different amino acids. The methods for obtaining these site-directed mutations are well known to the skilled person and are widely described in the literature (in particular: Site-Directed Mutagenesis: A Practical Approach, 1991, Edited by M.J. McPHERSON, IRL PRESS), or are methods for which commercial kits (eg, QUIKCHANGE™ flash mutagenesis kit from Qiagen or Stratagene) may be used. After site-directed mutagenesis, the nucleic acids were transformed into Escherichia coli strain MG1655. Cells containing a mutated polypeptide with advantageous biotransformation yields were selected using an appropriate screening method. Appropriate screening methods are described herein under General Methods, items 4 and 7. The sequences of mutated nucleic acid sequences encoding improved polypeptides were verified. Methods for sequence verification are well known to the skilled artisan and are extensively described in the literature (eg, Sambrook and Russell (2012) Molecular Cloning: A Laboratory Manual (Coid Spring Harbor Laboratory Press, Cold Spring Harbor, NY). )). 2. Expression vectors / host cells for ω-ΤΑ variants Nucleic acid sequences encoding wild-type ω-TAs (SEQ ID Nos 2, 5, 8, 14) or known ω-ΤΑ comprising mutations (SEQ ID NO 11) or ω-ΤΑ variants as described described herein were cloned into the commercial vector pET22B (Merck KGaA, Frankfurter Str 250, 64293 Darmstadt, Germany) and expressed in cells of Escherichia coli strain BL21DE3. 3. Expression of variants of ω-ΤΑ A preculture of the Escherichia colique strain BL21DE3 comprising the vector pET22B into which the respective nucleic acid sequence encoding the ω-ΤΑ variants was introduced, was cultured in flasks containing 20 ml of LB medium supplemented with carbenicillin at 37° C on a rotary shaker at 180 rpm overnight. Expression of ωΤΑ proteins was carried out by transferring the preculture to flasks containing 250 ml of LB medium supplemented with carbenicillin. The expression of the ω-ΤΑ proteins was induced by QLZLnn / Lznz / E / Yi median from the addition of 0.5 mM IPTG (final concentration) after an OD (optical density) of between 0.6-0.8 was reached by growth at 37SC on a rotary shaker at 180 rpm. The induced cell culture was incubated at 20°C for 20 h at 180 rpm with shaking. Purification of the enzymes was performed using Qiagen's Ni-NTA Quick Start Kit (Qiagen GmbH, Qiagen Strasse 1,40724 Hilden) according to the manufacturer's protocol. 4. Activity test for ω-ΤΑ variants in the presence of amine acceptors and amine donors To 40 μΙ of triethanolamine buffer (200 mM solution in deionized water, pH=9.0), 10 μΙ of pyridoxal phosphate (10 mM solution in deionized water) and 10 μΙ of the amino donor ( 2 M solution in deionized water, adjusted to pH=9.0 by adding aqueous HCI). Subsequently, 20 μΙ of the amino acceptor (100 mM solution in deionized water) was added (if the amino acceptor is not soluble in water, add proportional DMSO). Finally, 20 μΙ of the transaminase enzyme (1.5 mg / ml) was added at room temperature and the mixture was incubated at 40°C on a rotary shaker at 800 rpm for 6-7 h. The transamination reaction was monitored by means of HPLC analysis of aliquots taken at various time intervals during the reaction. 5. Expression Vectors / Host Cells Used for ω-ΤΑ Variants Having Additional Amino Acid Modifications Activity testing for ω-ΤΑ variants having additional amino acid modifications was carried out using a method comprising two reaction steps. The first reaction step (step 1) produces an amine acceptor for ω-TAs. The step is catalyzed by a D-amino acid oxidase (DAAO or DAO, EC 1.4.3.3). DAAOs are flavin adenine dinucleotide (FAD)-containing flavoproteins that catalyze the oxidative deamination of D-amino acids with oxygen to generate the corresponding 2-oxoacids together with hydrogen peroxide and ammonia according to the following general equation (III): α-D-amino acid + H2O + O2-----> α-2-oxocarboxylic acid + NH3 + H2O2 The protein having the activity of a DAAO used for the production of α-2-οχο carboxylic acids in the first reaction step was a DAAO variant of the DAO1 protein from Rhodosporidium toruloides. The nucleic acid sequence encoding the wild-type DAO1 protein from Rhodosporidium toruloides is derived from GenBank No. acc. U6006.1 (shown under SEQ ID NO 19) and the corresponding amino acid sequence encoded by the nucleic acid sequence shown under SEQ ID NO 19 is derived from UniProt No. acc. P80324 (shown under SEQ ID NO 20). The DAAO variant used herein is disclosed in WO 2017 / 151573 as Muant Ac305 (page 36, Table 1). Compared to SEQ ID NO 20, the Ac305 mutant comprises substitutions QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ (replacements) of amino acids at positions 54 and 58 and 213. In Mutant Ac305 the amino acid N at position 54 in SEQ ID NO 20 is substituted (replaced) by C and the amino acid F in position 58 in SEQ ID NO 20 is substituted (replaced) by H and amino acid M at position 213 in SEQ ID NO 20 is substituted (replaced) by S. The amino acid sequence of Mutant Ac305 is shown under SEQ ID NO 22. A respective nucleic acid sequence encoding the protein having the amino acid sequence shown under SEQ ID NO 22 is shown under SEQ ID NO 21. The reaction of step 1 was catalyzed by means of a protein having the activity of a DAAO having the amino acid sequence shown under SEQ ID NO 22. In a second reaction step (step 2) the α-2-oxocarboxylic acid produced by a protein having the activity of a DAAO) in step 1 is converted in the presence of an amine donor by means of a protein having the activity of ω-ΤΑ into an amino acid according to the general equation (I). As is clear from the description of step 1 by means of the general equation (III), the conversion of D-amino acids to ketoacids catalyzed by proteins having the activity of a DAAO generates hydrogen peroxide (H2O2). Removal of H2O2 may be desired, but is not necessarily necessary in all circumstances. The removal of H2O2 was achieved in connection with the present invention by means of the addition of a protein having the activity of a catalase. Proteins having catalase activity (EC 1.11.1.6; hydrogen peroxide:hydrogen peroxide oxidoreductase) are known in the art and catalyze the conversion of hydrogen peroxide (H2O2) to water (H2O) and oxygen (O2 ) according to the following general equation (IV): 2H2O2----> O2+ 2H2O The amino acid sequence of a protein having the activity of a catalase from Listeria seiger used for H 2 O 2 removal is shown under SEQ ID NO 24 and is derived under GenePept Accession No. WP_012986600.1. SEQ ID NO 23 (which is derived under GenBank Accession No. NC_013891.1) shows the sequence encoding nucleic acids from Listeria seeliger for the catalase protein having the amino acid sequence as shown under SEQ ID NO 24 SEQ ID NO 25 is a nucleic acid sequence that also encodes the catalase protein having the amino acid sequence shown under SEQ ID NO 24. Compared with the nucleic acid sequence shown under SEQ ID NO 25 23, the codons of the nucleic acid sequence shown under SEQ ID NO 25 have been adapted to Escherichia coli codon usage. To produce proteins that have the activity of a DAAO, proteins that have the QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ activity of an ω-ΤΑ and proteins having the activity of a catalase, the nucleic acid sequences encoding the three respective proteins were cloned into an E. cali expression vector in such a manner that all three proteins were transcribed from a single operon as tricistronic RNA from the trc promoter (a hybrid promoter composed of sequences originating from the trp promoter and / acUV5). The order of the genes with respect to transcription from the promoter was DAAO (SEQ ID NO 21) -> nucleic acid molecules encoding ω-ΤΑ variants comprising additional amino acid modifications (as described herein above). -> catalase (SEQ ID NO 25). SEQ ID NO 21 was translationally fused at its 5' end with a nucleic acid sequence encoding the amino acid sequence M A R I R L. The expression vector used is based on pSE420 (description and sequences derived from: Addgene, 75 Sidney St, Suite 550A, Cambridge, MA 02139; https: / / www.addgene.org / vector-database / 4064 / or from Thermo Fisher Scientific (Invitrogen), Thermo Fisher Scientific Inc. 168 Third Avenue, Waltham, MA 02451 United States, https: / / www.thermofisher.com / search / results?query=pSE420&focusarea). Genetic elements were introduced into a modified pSE420 vector by commonly known methods. The relevant genetic elements present in the expression vector used are shown in Fig. 1. For the expression of the three enzymes, the expression vector was transferred into Escherichia cali strain MG1655 cells. 6. Expression of ω-ΤΑ Variants Involving Additional Amino Acid Modifications ω-ΤΑ variants comprising additional amino acid modifications were cloned into the tricistronic expression vector described above under "General Methods", item 5 and expressed in Escherichia coli strain MG1655 cells. To do this, a 20 ml preculture was grown overnight in LB Medium supplemented with kanamycin in a shake flask at 37°C on a rotary shaker at 180 rpm. Expression of ωΤΑ proteins was carried out by transferring the preculture to flasks containing 200 ml of LB medium supplemented with kanamycin. Expression of ωΤΑ proteins was induced after an OD between 0.6 and 0.8 was reached by the addition of 1 mM IPTG (final concentration). The induced cell culture was incubated at 20°C for 20 h at 180 rpm with shaking. For harvesting, the cell culture was centrifuged at 8000 g at 4°C for 15 minutes and the obtained cell pellet was stored at -80°C until lyophilized or spray-dried. 7. Testing for Activity of ω-ΤΑ Variants Having Additional Amino Acid Modifications 268 mL of a 50% aqueous solution in weight of (T?,S>racemic glufosinate ammonium (corresponds to 160.8 g of racemic glufosinate ammonium). Via pH controlled dosing unit, a 2 M aqueous solution of / so-propylamine was added under mechanical stirring (250 rpm) until pH= 9.0 is reached. The pH is kept constant throughout the reaction time by the controlled addition of the 2 M aqueous solution of / so-propylamine. The reactor is heated until 35SC internal temperature. In a beaker, 8 g of spray-dried Escherichia coli strain MG1655 cells containing the expression vector described in Fig. 1, expressing ω-ΤΑ variants and wild-type ω-ΤΑ proteins, were mixed. with additional amino acid modifications, 200 mg pyridoxal phosphate, 2 mL polypropylene glycol (P 2000), and 138 mL deionized water. This mixture was added to the glass reactor with stirring (250 rpm) at 35SC. Through the O 2 gas inlet tube, oxygen gas was bubbled through the reaction mixture at a flow rate of 0.1 L / min. The mixture was stirred for 24 h and the progress of the reaction was monitored by HPLC analysis of aliquots taken at various time intervals during the reaction. Subsequently, the oxygen gas feed was stopped as well as the / so-propylamine feed and the reaction mixture was denatured at 90°C for 30 min under stirring (250 rpm). The residual mixture was cooled to room temperature. 8. Detection of amines produced by ω-TAs A) Analysis of the transamination products fSJ-norvaline, SJ-leucine, (S)tyrosine, and (SJ-glufosinate ammonium The course of the transamination reaction was monitored by means of HPLC analysis. The HPLC methodology used in this work is based on the publication by Davankov et al. (1980, Chromatography 13(11), 677-685). Specifically, the following HPLC parameters were used: Column: Phenomenex Chirex 3126 (D) - penicillamine 150*4.6 mm (Cat.: 00F3126-E0) Flow Rate: 1ml / min Eluents: A) deionized water + 0.5 g / l of CuSO4 (v / v) B) methanol A:B = 90:10 (Socratic!) Detector: DAD 230nm Oven: 30°C Running time: 15 min B) Analysis of the transamination product L-phenylalanine: The course of the transamination reaction was monitored by means of HPLC analysis. QLZLnn / Lznz / E / Yi Specifically, the following HPLC parameters were used: Column: Phenomenex Prodigy 3 pm ODS-3 100A 100*4 mm (Cat.: 00D-4222-D0) Flow Rate: 2ml / min Eluents:A) acetonitrile B) deionized water Gradient from A:B = 5:95 to A:B = 95:5 within 7 min Detector: VWD1A, 210nm Oven: 40°C Running time: 9 min 9. Spray Drying of Cells The spray drying experiments have been carried out in a laboratory spray dryer (Laboratory Scale) with a maximum input temperature of 220°C. The dryer uses either compressed air or nitrogen with 200-800 l / h (litre / hour) below 5-8 bar. The maximum air flow can be achieved with 35 m3 / h (meter3 / hour). In order to dry the bacterial cell mass either from the flask culture or from the fermented material (i.e. 1 liter total volume), the broth has been concentrated ten times (10x) by means of centrifugation and has been resuspended to a final volume of 100 ml in the culture supernatant obtained after centrifugation. The obtained concentrate needs to be pumpable and should be constantly mixed with a magnetic stirrer. The liquid was applied to a 0.7 mm nozzle using an airflow of 500 L / h with the aspirator set to 100%. Typical product flow was 10 ml / min. and the applied temperatures averaged -145°C for the inlet and 85aC for the outlet. The subsequent dry biomass has been weighed and used on the g / l scale for the biotransformation experiments. EXAMPLES 1. Conversion of 2-oxovaleric acid to (SJ-norvaline Wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 6 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 3 or ωΤΑ variants having the amino acid sequence shown under SEQ ID N018 were expressed and purified as described under General Methods”, point 3. To 25 μΙ of triethanolamine buffer in deionized water (200 mM soln in deionized water, pH=9.0), 10 μΙ of pyridoxal phosphate (PLP) in deionized water (10 mM soln in deionized water) was added at room temperature ) and 10 μΙ of / so-propylamine in deionized water (2 M solution in deionized water, adjusted to pH=9.0 by adding aqueous HCI). Subsequently, 20 μΙ of 2-oxovaleric acid (100 mM solution in deionized water) was added. Finally, 35 μΙ of a solution comprising 1.5 mg / ml of the QL7 Lnn / L7í17 / E / Yli respective ω-ΤΑ protein was added at room temperature and the mixture was incubated at 40°C on a rotary shaker at 800 rpm for 6 h. The transamination reaction was monitored by means of HPLC analysis of the aliquots taken at different time intervals during the reaction as described under "General Methods", item 8. Table 6 presents the results obtained for a variant of ω-ΤΑ having the amino acid sequence shown under SEQ ID NO 18 in comparison with those of wild-type proteins from Arthrobacter sp. which has the amino acid sequence shown under SEQ ID NO 6 and Badilas megaterium which has the amino acid sequence shown under SEQ ID NO 3. The results are also shown in Fig. QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ Fig. 2. Amine area [mAU*s] of Arthrobacter amine area [mAU*s] Amine area time Bacillus megaterium (SEQ ID [mAU*s] of the ω-ΤΑ variant o[h ] NO 3) sp. (SEQ ID NO 6) (SEQ ID NO 18) 0 0 0 0 1 4691 1551 6096 2 5871 2486 8727 3 7508 3946 8868 5 8500 5333 9014 6 8463 Table 6 Description of Table 6: 5973 8573 "time" measured in hours (h) indicates the time elapsed since the reaction started. “mAU*s” is the abbreviation for milli (m) absorbance (A) units (U) multiplied (*) with seconds (s); a standard unit that describes the area under a peak on an HPLC chromatogram. The larger the area under a peak, the greater the amount of the respective product. It follows from Table 6 and Fig. 2, that in the reaction catalyzed by the ω-ΤΑ variant, the production of (S>norvalin from 2-oxovaleric acid proceeds faster than in the catalyzed reactions by wild-type proteins from Arthrobacter sp., and from Bacillus megaterium.In addition, the maximum amount of fS / norvaline produced during the reaction is reached significantly earlier in the reaction catalyzed by the ω-ΤΑ variant compared to the reactions catalyzed by the ω-ΤΑ variant. by wild-type proteins from Arthrobacter sp., and from Bacillus megaterium. 1. Conversion of 4-methyl-2-oxo-valeric acid to (SJ-leucine Wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6 or ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 they were expressed and purified as described under "General Methods", point 3. To 40 μΙ of triethanolamine buffer (200 mM solution in deionized water, pH=9.0), 10 μΙ of pyridoxal phosphate (10 mM solution in deionized water) and 10 μΙ of / so-propylamine were added at room temperature. (2 M solution in deionized water, adjusted to pH=9.0 by adding aqueous HCl). After that, 20 μΙ of 4-methyl-2-oxo-valeric acid (100 mM solution in deionized water) was added. Finally, 20 μΙ of a solution comprising 1.5 mg / ml of the respective ω-ΤΑ protein was added thereto at room temperature and the mixture was incubated at 40°C on a rotary shaker at 800 rpm for 6 h. The transamination reaction was monitored by means of HPLC analysis of the aliquots taken at different time intervals during the reaction as described under "General Methods", item 8. Table 7 presents the results obtained for a variant of ω-ΤΑ having the amino acid sequence shown under SEQ ID NO 18 in comparison with those of the wild-type proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 and from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6. The results are also shown in Fig. 3. Area of ​​amine [mAU*s] of Area of ​​amine Area of ​​amine [mAU*s] QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ time Bacillus megaterium (SEQ ID [mALJ*s] of ω-ΤΑ variant Arthrobacter o [h] NO 3) sp. (SEQ ID NO 6) (SEQ ID NO 18) 0 0 0 0 1 0 0 6971 2 0 0 7954 3 0 0 8052 4 0 0 7975 5 0 0 8267 6 0 0 8077 Table 7 Description of Table 7: See description of Table 6 It is derived from Table 7 and Fig. 3 that the wild-type enzymes from Arthrobacter sp. and from Bacillus megaterium do not produce ¿SJ-leucine via amination of 4-methyl-2-oxo-valeric acid, whereas the ω-ΤΑ variant does produce ¿SJ-leucine quite efficiently. 2. Conversion of phenylpyruvic acid to fSJ-phenylalanine Wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6 or ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 they were expressed and purified as described under "General Methods", point 3. To 40 μΙ of triethanolamine buffer (200 mM solution in deionized water, pH=9.0), 10 μΙ of pyridoxal phosphate (10 mM solution in deionized water) and 10 μΙ of / so-propylamine were added at room temperature. (2 M solution in deionized water, adjusted to pH=9.0 by adding aqueous HCl). Subsequently, 20 μΙ of phenylpyruvic acid in DMSO / deionized water was added in a 1:1 ratio (100 mM phenylpyruvic acid solution). Finally, 20 μΙ of a solution comprising 1.5 mg / ml of the respective ω-ΤΑ protein was added thereto at room temperature and the mixture was incubated at 40°C on a rotary shaker at 800 rpm for 6 h. The transamination reaction was monitored by means of HPLC analysis of the aliquots taken at different time intervals during the reaction as described under "General Methods", item 8. Table 8 presents the results obtained for a variant of ω-ΤΑ having the amino acid sequence shown under SEQ ID NO 18 in comparison with those of the wild-type proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 and from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6. The results are also shown in Fig. 4. Amine area [mAU*s] of Amine area [mAU*s] Amine area [mAU*s] time Bacillus megaterium SEQ ID of Arthrobacter sp. (SEQ of the variant of ω-ΤΑ QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ [h] NO 6) ID NO 6) (SEQ ID NO 18) 0 0 0 0 1 0 0 3271 2 245 0 5613 3 338 0 7056 4 403 0 7845 5 481 0 8772 6 540 0 10022 Table 8 Description of Table 8: See description of Table 6 It is derived from Table 8 and from Fig. 4 that the wild-type enzyme from Arthrobacter sp. does not produce / SJ-phenylalanine from phenylpyruvic acid, the wild-type enzyme from Bacillus megaterium produces (SJ-phenylalanine very slowly and in low amounts compared to the amount of (SJ-phenylalanine produced by the ω-variant ΤΑ. 3. Conversion of p-hydroxyphenylpyruvic acid to (SJ-tyrosine: Wild-type ω-ΤΑ proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 or from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6 or ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 they were expressed and purified as described under "General Methods", point 3. To 40 μΙ of triethanolamine buffer (200 mM solution in deionized water, pH=9.0), 10 μΙ of pyridoxal phosphate (10 mM solution in deionized water) and 10 μΙ of / so-propylamine were added at room temperature. (2 M solution in deionized water, adjusted to pH=9.0 by adding aqueous HCI). Subsequently, 20 μΙ p-hydroxyphenylpyruvic acid in DMSO / deionized water was added in a 1:1 ratio (100 mM jO-hydroxyphenylpyruvic acid solution). Finally, 20 μΙ of a solution comprising 1.5 mg / ml of the respective ω-ΤΑ protein was added thereto at room temperature and the mixture was incubated at 40°C on a rotary shaker at 800 rpm for 6 h. The transamination reaction was monitored by means of HPLC analysis of the aliquots taken at different time intervals during the reaction as described under "General Methods", item 8. Table 9 presents the results obtained for a variant of ω-ΤΑ having the amino acid sequence shown under SEQ ID NO 18 in comparison with those of the wild-type proteins from Arthrobacter sp. having the amino acid sequence shown under SEQ ID NO 3 and from Bacillus megaterium having the amino acid sequence shown under SEQ ID NO 6. The results are also shown in Fig. 5. Area of ​​amine [mAU*s] of Area of ​​amine [mAU*s] Area of ​​amine [mAU*s] QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ time Bacillus megaterium (SEQ ID of Arthrobacter sp. (SEQ of the variant of ω-ΤΑ or [h] NO 3) ID NO 6) (SEQ ID NO 18) 0 0 0 0 1 0 0 3723 2 0 0 4902 3 0 0 5891 4 0 0 6450 5 0 0 8129 6 0 0 8912 Table 9 Description of Table 9: See description of Table 6 It is derived from Table 9 and Fig. 5 that the wild-type enzymes from Arthrobacter sp. and from Bacillus megaterium do not produce / SJ-tyrosine via amination of p-hydroxyphenylpyruvic acid, whereas the ω-ΤΑ variant does produce / SJ-tyrosine very efficiently. 4. Production of ('SJ-glufosinate from 4-[hydroxy(methyl)phosphoryl]-2oxobutanoic acid by means of ω-ΤΑ variants comprising additional amino acid modifications ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 and ω-ΤΑ variants comprising additional amino acid modifications as described herein in Table 2 were co-expressed with proteins having the activity of a DAAO and having the activity of a catalase (see "General Methods", item 5) as described under "General Methods", item 6, followed by spray drying as described under "General Methods", point 9. DAAO produces 4-[hydroxy(methyl)phosphoryl]-2-oxobutanoic acid via deamination of ¿FfJ-glufosinate. 4-[H¡drox¡(met¡l)phosphor¡l]-2-oxobutanoic acid is subsequently used by ω-ΤΑ variants that have additional amino acid modifications as an amino acceptor and is converted in a reaction of amination in (SJ-glufosinate. Activity tests of ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 and of ω-ΤΑ variants comprising additional amino acid modifications as described herein in Table 2, were carried out according to the test described under “General Methods, item 7. The transamination reaction was monitored by means of HPLC analysis as described under “General Methods”, item 8 , through determination of the amount of fSJ-glufosinate produced in each reaction 5 h after the reaction started. Table 10 presents the amount of fSj-glufosinate (S-GA) produced by each of the ω-ΤΑ variants comprising additional amino acid modifications and the amount produced by the ω-ΤΑ variant having the amino acid sequence that is shown under SEQ ID NO 18. QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ Introduced mutations with respect to the amino acid sequence shown under SEQ ID NO 18 S-GA produced in 5 h [g / i] T327Q, S166G 20.01 T327Q, C384S 19.91 T327Q, E326Q 19.66 T327Q 19 .01 T327Q, E326F 18.92 T327C 18.53 T327I 17.97 T327M 17.92 F164Y 17.71 F164S 16.9 T327V 16.82 T409R 16.66 T327S 16.17 V271I 15.47 S329G 15.31 T409P 15.25 L414M 15.14 Q165K 1R4 1 .42 L414H 14.32 Q165C 14.23 T327V 14.02 F164C 13.87 T409K 12.82 None 12.76 QL7 ίΠΠ / ίΖηΖ / Ε / ΥΙ Table 10 Description of Table 10: For identification of amino acid changes, the numbers in column 1 identify the amino acid position in the amino acid sequence shown under SEQ ID NO 18. The character appearing before the number identifies the amino acid present in the respective position in the amino acid sequence shown under SEQ ID NO 18. The character appearing after the number identifies the amino acid present at the respective position in the amino acid sequences of the ω-ΤΑ variants comprising additional amino acid modifications . Two numbers provided in the same column row, each with a character appearing before and after the number, identify two simultaneous amino acid substitutions (replacements) compared to the amino acid sequence shown in SEQ ID NO 18. It is derived from Table 10, that ω-ΤΑ variants comprising additional amino acid modifications produce more fS)-glufosinate compared to ω-ΤΑ variants having the amino acid sequence shown under SEQ ID NO 18 . QL7 Líin / LZAZ / E / Yli NOVELTY OF THE INVENTION

Claims

Having described the present invention as above, the following claims are considered novel and are therefore claimed as property:

1. A protein possessing the activity of a ω-transaminase (ω-TA), wherein the protein is selected from the group comprising a) proteins comprising the amino acid sequence from positions 1 to 477 as shown under SEQ ID NO 3, furthermore, the amino acid at position 25 is different from F, the amino acid at position 64 is different from L, the amino acid at position 88 is different from T, the amino acid at position 157 is different from T, the amino acid at position 165 is different from R, the amino acid at position 169 is different from V, the amino acid at position 174 is different from E, the amino acid at position 187 is different from S, the amino acid at position 197 is different from M, and the amino acid at position 239 is different from S and the amino acid at position 327 isdifferent from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; b) proteins comprising the amino acid sequence from positions 1 to 479 as shown under SEQ ID NO 6, in addition to the amino acid at position 25 being different from F, the amino acid at position 64 being different from L, the amino acid at position 88 being different from T, the amino acid at position 157 being different from T, the amino acid at position 165 being different from R, the amino acid at position 169 being different from V, the amino acid at position 174 being different from E, the amino acid at position 187 being different from S, and the amino acid at position 197 being different from T.amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; c) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 9, in addition to the amino acid at position 25 being different from F, the amino acid at position 64 being different from L, the amino acid at position 88 being different from T, the amino acid at position 157 being different from T, the amino acid at position 165 being different from R, the amino acid at position 169 being different from V, the amino acid at position 174 being different from E, and the amino acid at theposition 187 is different from S and the amino acid in position 197 is different from M and the amino acid in position 239 is different from S and the amino acid in position 327 is different from S and the amino acid in position 328 is different from V and the amino acid in position 384 is different from Y and the amino acid in position 389 is different from I and the amino acid in position 391 is different from D and the amino acid in position 396 is different from K and the amino acid in position 410 is different from H and the amino acid in position 414 is different from P; d) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 12, in addition to the amino acid at position 25 being different from F, the amino acid at position 64 being different from L, the amino acid at position 88 being different from T, the amino acid at position 157 being different from T, the amino acid at position 165 being different from R, and the amino acid at position 169 beingdifferent from V and the amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from T, the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; e) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 15 furthermore that the amino acid at position 25 is different from F and the amino acid at position 64 is different from L and the amino acid at position 88 is different from T and the amino acid at position 157 is different from T and theamino acid at position 165 is different from R and the amino acid at position 169 is different from V and the amino acid at position 174 is different from E and the amino acid at position 187 is different from S and the amino acid at position 197 is different from M and the amino acid at position 239 is different from S and the amino acid at position 327 is different from S and the amino acid at position 328 is different from V and the amino acid at position 384 is different from Y and the amino acid at position 389 is different from I and the amino acid at position 391 is different from D and the amino acid at position 396 is different from K and the amino acid at position 410 is different from H and the amino acid at position 414 is different from P; f) proteins having an amino acid sequence that has at least 60%, preferably 70%, more preferably 80%, even more preferably 90%, still more preferably 95%, still more preferably 96%, with particular preference 97%,with highest preference 98% or with special preference 99% identity with any of the amino acid sequences shown under a), b), c), d), e), or f), given that in each QL7 iРР / ίЖηЖ / E / YI case the amino acid corresponding to position 25 is different from F and the amino acid corresponding to position 64 is different from L and the amino acid corresponding to 88 is different from T and the amino acid corresponding to position 157 is different from T and the amino acid corresponding to position 165 is different from R and the amino acid corresponding to position 169 is different from V and the amino acid corresponding to position 174 is different from E and the amino acid corresponding to position 187 is different from S and the amino acid corresponding to position 197 is different from T or M and the amino acid corresponding to position 239 is different from S and the amino acid corresponding to position 327 is different from S and the The amino acid corresponding to position 328 is differentof V and the amino acid corresponding to position 384 is different from Y and the amino acid corresponding to position 389 is different from I and the amino acid corresponding to position 391 is different from D and the amino acid corresponding to position 396 is different from K and the amino acid corresponding to position 410 is different from H and the amino acid corresponding QLZLnn / Lznz / E / Yi to position 414 is different from P.

2. The protein according to claim 1 selected from the group comprising a) proteins comprising the amino acid sequence as defined in claim 1, section a) further wherein the amino acid at position 2 is different from S and the amino acid at position 48 is different from D and the amino acid at position 164 is different from Y and the amino acid at position 202 is different from D and the amino acid at position 205 is different from L and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 311 is different from L and the amino acid at position 353 is different from F and the amino acid at position 359 is different from D and the amino acid at position 424 is different from K and the amino acid at position 475 is different from A and the amino acid at position 476 is different from L and the amino acid at position 477 is removed;b) proteins comprising the amino acid sequence as defined in claim 1, section b) furthermore, the amino acid at position 46 is different from T and the amino acid at position 60 is different from C and the amino acid at position 185 is different from C and the amino acid at position 186 is different from S and the amino acid at position 195 is different from S and the amino acid at position 205 is different from Y and the amino acid at position 252 is different from V and the amino acid at position 268 is different from S and the amino acid at position 409 is different from R and the amino acid at position 436 is different from A and the amino acids at positions 477 and 478 and 479 are deleted;c) proteins comprising the amino acid sequence as defined in claim 1, section c) furthermore, the amino acid at position 2 is different from S and the amino acid at position 48 is different from D and the amino acid at position 69 is different from P and the amino acid at position 90 is different from S and the amino acid at position 164 is different from Y and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 268 is different from T and the amino acid at position 311 is different from L and the amino acid at position 318 is different from E and the amino acid at position 322 is different from R and the amino acid at position 353 is different from S and the amino acid at position 424 is different from K and the amino acid at position 452 is different from E;d) proteins comprising the amino acid sequence as defined in claim 1, section d) furthermore, the amino acid at position 46 is different from T and the amino acid at position 60 is different from C and the amino acid at position 185 is different from C and the amino acid at position 186 is different from C and the amino acid at position 195 is different from S and the amino acid at position 205 is different from Y and the amino acid at position 252 is different from V and the amino acid at position 268 is different from S and the amino acid at position 409 is different from R and the amino acid at position 436 is different from A;e) proteins comprising the amino acid sequence as defined in claim 1, section d) furthermore, the amino acid at position 48 is different from D and the amino acid at position 164 is different from Y and the amino acid at position 242 is different from A and the amino acid at position 245 is different from A and the amino acid at position 255 is different from F and the amino acid at position 424 is different from K; f) proteins having an amino acid sequence that has at least 60% identity with any of the amino acid sequences defined under a), b), c), d) or e) wherein each amino acid position as defined under a), b), c), d) or e), respectively, is also present at the corresponding amino acid position in the amino acid sequences of the protein sequence that is at least 60% identical to the amino acid sequence as defined in each of a), b), c), d) or e).

3. The protein according to any one of claims 1 or 2 selected from the group consisting of a) proteins comprising the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18; b) proteins having an amino acid sequence that has at least 60% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18, given that the amino acids corresponding to positions 25, 64, 88, 157, 165, 169, 174, 187, 197, 239, 327, 328, 384, 389, 391, 396, 410 and 414 in SEQ ID NO 18 represent those amino acids shown in the respective positions in the QL7 ίΠΠ / ίΖηΖ / E / YΙ amino acid sequence shown under SEQ ID NO 18;c) proteins having an amino acid sequence that has at least 60% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18 given that the amino acids corresponding to positions 2, 25, 46, 48, 60, 64, 69, 88, 90, 157, 164, 165, 169, 174, 187, 195, 197, 202, 205, 239, 242, 245, 252, 255, 268, QLZLnn / Lznz / B / Yi 311,318, 322, 327, 328, 353, 359, 384, 389, 391,396, 409, 410, 414, 424, 436, 452, 475, 476 and 477 in SEQ ID NO 18 represent those amino acids that are shown in the respective positions in the amino acid sequence shown under SEQ ID NO 18.; 4. The protein according to any one of claims 1 to 3 selected from the group consisting of: a) proteins according to any one of claims 1 amino acid at position 166 is G and the amino acid at position 327 is Q; b) proteins according to any one of claims 1 amino acid at position 327 is Q and the amino acid at position 384 is S; c) proteins according to any one of claims 1 amino acid at position 326 is Q and the amino acid at position 327 is Q; d) proteins according to any one of claims 1 amino acid at position 327 is Q; e) proteins according to any one of claims 1 amino acid at position 326 is F and the amino acid at position 327 is Q; f) proteins according to any of claims 1 to 3 wherein the amino acid at position 327 is C;g) proteins according to any of the claims amino acid at position 327 is I; h) proteins according to any of the claims amino acid at position 327 is M; i) proteins according to any of the claims amino acid at position 164 is Y; j) proteins according to any of the claims amino acid at position 164 is S; k) proteins according to any of the claims amino acid at position 327 is V; l) proteins according to any of the claims amino acid at position 409 is R; m) proteins according to any of the claims a 3 given that the amino acid at position 327 is S; n) proteins according to any of the claims amino acid at position 271 is I; o) proteins according to any of claims 1 amino acid in 329 is G;p) proteins according to any of the claims, 1 amino acid at position 409 is P; q) proteins according to any of the claims, 1 amino acid at position 414 is M; r) proteins according to any of the claims, 1 amino acid at position 165 is K; s) proteins according to any of the claims, 1 amino acid at position 414 is R; t) proteins according to any of the claims, 1 amino acid at position 414 is H; u) proteins according to any of the claims, 1 amino acid at position 165 is C; v) proteins according to any of the claims, 1 amino acid at position 327 is V; w) proteins according to any of the claims, 1 amino acid at position 164 is C;x) proteins according to any of claims 1 to 3 wherein the amino acid at position 409 is K.; 5. The protein according to claim 4 selected from the group comprising a) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, further wherein the amino acid S at position 166 in SEQ ID NO 18 is substituted by G and the amino acid T at position 327 in SEQ ID NO 18 is substituted by Q; b) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, further wherein the amino acid T at position 327 in SEQ ID NO 18 is substituted by Q and the amino acid C at position 384 in SEQ ID NO 18 is substituted by S; c) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the fact that amino acid E at position 326 in SEQ ID NO 18 is substituted by O and amino acid T at position 327 in SEQ ID NO 18 is substituted by Q; d) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid T at position 327 in SEQ ID NO 18 is substituted by Q; e) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid E at position 326 in SEQ ID NO 18 is substituted by F and amino acid T at position 327 in SEQ ID NO 18 is substituted by Q; f) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the amino acid T at position 327 in SEQ ID NO 18 being substituted by C; g) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the amino acid T at position 327 in SEQ ID NO 18 being substituted by I; h) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the amino acid T at position 327 in SEQ ID NO 18 being substituted by M; i) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the amino acid F at position 164 in SEQ ID NO 18 being substituted by Y; j) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the fact that amino acid F at position 164 in SEQ ID NO 18 is substituted by S; k) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid T at position 327 in SEQ ID NO 18 is substituted by V; i) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid T at position 409 in SEQ ID NO 18 is substituted by R; m) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid T at position 327 in SEQ ID NO 18 is substituted by S; n) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the fact that amino acid V at position 271 in SEQ ID NO 18 is substituted by I; o) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid S at position 329 in SEQ ID NO 18 is substituted by G; p) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid T at position 409 in SEQ ID NO 18 is substituted by P; (q) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the amino acid L at position 414 in SEQ ID NO 18 being substituted by M; (r) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the fact that amino acid Q at position 165 in SEQ ID NO 18 is substituted by K; s) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid L at position 414 in SEQ ID NO 18 is substituted by R; t) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid L at position 414 in SEQ ID NO 18 is substituted by H; u) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the fact that amino acid Q at position 165 in SEQ ID NO 18 is substituted by O; v) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18,in addition to the amino acid T at position 327 in SEQ ID NO 18 being substituted by V; w) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, in addition to the amino acid F at position 164 in SEQ ID NO 18 being substituted by C; x) proteins having the amino acid sequence from positions 1 to 476 in the amino acid sequence shown under SEQ ID NO 18, furthermore, amino acid T at position 409 in SEQ ID NO 18 is substituted by K; and y) proteins having an amino acid sequence that has at least 60% identity with any of the amino acid sequences defined under a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w), ox), given that each amino acid position as defined under a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w), ox), respectively,It is also present at the corresponding amino acid position in the amino acid sequences of the protein sequence that has at least 60% identity with any of the amino acid sequences defined under each of a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w), ox). QL7 ίΠη / ίΖίΙΖ / Ε / ΥΙ, 6. A nucleic acid molecule encoding a protein according to any of claims 1 to 5.

7. A nucleic acid molecule according to claim 6 encoding a protein having the activity of a ω-TA selected from the group comprising a) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 17; b) nucleic acid molecules encoding a protein comprising the amino acid sequence from position 1 to 476 in the amino acid sequence as shown under SEQ ID NO 18; c) nucleic acid molecules having at least 60% identity with the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence shown under SEQ ID NO 17, given that the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO 17 has the nucleotide sequenceath and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO 17 has the sequenceof nucleotides ccn and the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon at nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gary the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 has the sequence of The codon corresponding to nucleotide positions 1228 to 1230 in QL7 ίΠη / ίΖίΙΖ / E / YΥΙ SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 inSEQ ID NO 17 has the nucleotide sequence yin; d) nucleic acid molecules having at least 60% identity with the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence shown under SEQ ID NO 17, given that the codon corresponding to nucleotide positions 4 to 6 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 136 to 138 in SEQ ID NO 17 has the nucleotide sequence atgy the codon corresponding to nucleotide positions 142 to 144 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 178 to 180 in SEQ ID NO 17 has the nucleotide sequence tay and The codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO 17 has the sequenceof nucleotides ath and the codon corresponding to nucleotide positions 205 to 207 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 268 to 270 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID N017 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 490 to 492 in SEQ ID NO 17 has the nucleotide sequence tty and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to the positions of the Nucleotides 505 to 507 in SEQ ID NO 17 has the gene nucleotide sequence and codon corresponding to positions 520 to 522 in SEQ ID NO 17has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 553 to 555 in SEQ ID N017 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 556 to 558 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 583 to 585 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 604 to 606 in SEQ ID N017 has the nucleotide sequence aayy the The codon corresponding to nucleotide positions 613 to 615 in SEQ ID NO 17 has the nucleotide sequence tgyy, and the codon corresponding to nucleotide positions 715 to 717 inSEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 724 to 726 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 733 to 735 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 754 to 756 in SEQ ID N017 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 763 to 765 in SEQ ID NO 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 802 to 804 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 931 to 933 in SEQ ID NO 17 has the sequence of nucleotides gtn and the codon corresponding to the positions of nucleotides 952 to 954 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to the positions of theNucleotides 964 to 966 in SEQ ID N017 has the nucleotide sequence aary and the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1057 to 1059 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1075 to 1077 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID N017 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gary the codon corresponding toThe nucleotide positions 1186 to 1188 in SEQ ID NO 17 have the nucleotide sequence gary; the codon corresponding to the nucleotide positions 1225 to 1227 in SEQ ID NO 17 has the nucleotide sequence acn; and the codon corresponding to the nucleotide positions 1228 to 1230 in SEQ ID NO 17 has the nucleotide sequence mgn; and the codon corresponding to the nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn; and the codon corresponding to the nucleotide positions 1270 to 1272 in SEQ ID NO 17 has the nucleotide sequence gary; and the codon corresponding to the nucleotide positions 1306 to 1308 in SEQ ID NO 17 has the nucleotide sequence gtn. The nucleotide positions 1354 to 1356 in SEQ ID NO 17 have the nucleotide sequence ggn\ e) nucleic acid molecules that hybridize with the complementary strand of the nucleic acid molecules defined under a),b), c), and d), given that the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 190 to 192 in SEQ ID NO QL7 iРР / įЖηЖ / E / YI 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the nucleotide sequence gene and the codon corresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 559 to 561 inSEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon at nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1150 to 1152 in SEQ ID NO 17 has the nucleotide sequence tgy and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to 1173 in SEQ ID NO 17 has the nucleotide sequence gary the codon corresponding to nucleotide positions 1186 to 1188 in SEQ ID NO 17 has the nucleotide sequence gary the codon corresponding to nucleotide positions 1228 to1230 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 1240 to 1242 in SEQ ID NO 17 has the nucleotide sequence ytn; f) nucleic acid molecules that hybridize with the complementary strand of the nucleic acid molecules defined under a), b), c) or d) given that the codon corresponding to nucleotide positions 4 to 6 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 73 to 75 in SEQ ID NO 17 has the nucleotide sequence mgn and the codon corresponding to nucleotide positions 136 to 138 in SEQ ID NO 17 has the nucleotide sequence atgy the codon corresponding to nucleotide positions 142 144 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 178 to 180 in SEQ ID NO 17 has the nucleotide sequence fay and the codon corresponding to thenucleotide positions 190 to 192 in SEQ ID NO 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 205 to 207 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to nucleotide positions 262 to 264 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 268 to 270 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 469 to 471 in SEQ ID N017 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 490 to 492 in SEQ ID NO 17 has the nucleotide sequence tty and the codon corresponding to nucleotide positions 493 to 495 in SEQ ID NO 17 has the nucleotide sequence car and the codon corresponding to nucleotide positions 505 to 507 in SEQ ID NO 17 has the nucleotide sequence gen and the codoncorresponding to nucleotide positions 520 to 522 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 553 to 555 in SEQ ID N017 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 556 to 558 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 559 to 561 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 583 to 585 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 589 to 591 in SEQ ID NO 17 has the nucleotide sequence gen and the codon corresponding to nucleotide positions 604 to 606 in SEQ ID N017 has the nucleotide sequence aayy the codon corresponding to the nucleotide positions 613 to 615 in SEQ ID NO 17 has the nucleotide sequencetgy and the codon corresponding to nucleotide positions 715 to 717 in SEQ ID NO 17 has the nucleotide sequence ccn and the codon corresponding to nucleotide positions 724 to 726 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 733 to 735 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 754 to 756 in SEQ ID N017 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 763 to 765 in SEQ ID NO 17 has the nucleotide sequence ath and the codon corresponding to nucleotide positions 802 to 804 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to the Nucleotide positions 931 to 933 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 952 to 954 in SEQ ID NO 17 has the sequenceof nucleotides gen and the codon corresponding to nucleotide positions 964 to 966 in SEQ ID N017 has the nucleotide sequence aary the codon corresponding to nucleotide positions 979 to 981 in SEQ ID NO 17 has the nucleotide sequence acn and the codon corresponding to nucleotide positions 982 to 984 in SEQ ID NO 17 has the nucleotide sequence ggn and the codon corresponding to nucleotide positions 1057 to 1059 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1075 to 1077 in SEQ ID NO 17 has the nucleotide sequence aay and the codon corresponding to nucleotide positions 1150 to 1152 in QLZLnn / Lznz / E / Yi SEQ ID N017 has the nucleotide sequence tay and the codon corresponding to nucleotide positions 1165 to 1167 in SEQ ID NO 17 has the nucleotide sequence ytn and the codon corresponding to nucleotide positions 1171 to1173 in SEQ ID NO 17 has the nucleotide sequence gar and the codon corresponding to nucleotide positions 1186 to 1188. In SEQ ID N017, the nucleotide sequence gary has the codon corresponding to nucleotide positions 1225 to 1227. In SEQ ID NO 17, the nucleotide sequence acn has the codon corresponding to nucleotide positions 1228 to 1230. In SEQ ID NO 17, the nucleotide sequence mgn has the codon corresponding to nucleotide positions 1240 to 1242. In SEQ ID NO 17, the nucleotide sequence ytn has the codon corresponding to nucleotide positions 1270 to 1272. In SEQ ID NO 17, the nucleotide sequence gary has the codon corresponding to nucleotide positions 1306 to 1306. 1308 in SEQ ID NO 17 has the nucleotide sequence gtn and the codon corresponding to nucleotide positions 1354 to 1356 in SEQ ID NO 17 has the nucleotide sequence ggn\ g) nucleic acid molecules that aredeviate from the nucleic acid molecules defined under a), b), c), d), e), or) due to the degeneracy of the genetic code; h) nucleic acid molecules encoding a protein having at least 60% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18, given that the amino acids corresponding to positions 25, 64, 88, 157, 165, 169, 174, 187, 239, 327, 328, 384, 389, 391, 396, 410, and 414 in SEQ ID NO 18 represent those amino acids shown in the respective positions in the amino acid sequence shown under SEQ ID NO 18; i) nucleic acid molecules encoding a protein that has at least 60% identity with the amino acid sequence from positions 1 to 476 as shown under SEQ ID NO 18 given that the amino acids corresponding to positions 2, 25, 46, 48, 60, 64, 69, 88, 90, 157, 164, 165, 169, 174, 185, 186, 187, 195, 197, 202, 205, 239, 242, 245, 252, 255, 268, 311, 318,322, 327, 328, 353, 359, 384, 389, 391, 396, 409, 410, 414, 424, 436, 452, 475 and 476 in SEQ ID NO 18 represent those amino acids that are shown in the respective positions in the amino acid sequence shown under SEQ ID NO 18; j) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16.

8. A nucleic acid molecule according to any of claim 6 or 7 encoding a protein having the activity of a ω-TA selected from the group comprising a) nucleic acid molecules comprising the nucleic acid sequence QL7 iPP / iZiZ / E / YI from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, further wherein the codon at nucleotide positions 496 to 498 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence ggn and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence car, b) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,In addition, the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence cary and the codon at nucleotide positions 1150 to 1152 in SEQ ID NO 16 or SEQ ID N017 has the nucleotide sequence w / sn; c) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, furthermore, the codon at nucleotide positions 976 to 978 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence cary and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence car, d) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence car, e) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 976 to 978 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence tty and the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence car, f) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence car; g) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence ath; h) nucleic acid molecules comprising the nucleic acid sequence QL7 iРР / įЖηЖ / E / YI from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence atg\ i) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence tay; j) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,In addition to the codon at nucleotide positions 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence wsn\ k) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence gtrr, I) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence mgn; m) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence wsn; n) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 811 to 813 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence ath\ o) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 985 to 987 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence ggn-, p) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence ccrr,(q) nucleic acid molecules comprising the nucleic acid sequence QL7 iРР / įЖηЖ / E / YI 100 from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, furthermore, the codon at nucleotide positions 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence atg\; (r) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, furthermore, the codon at nucleotide positions 493 to 495 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence aar; (s) nucleic acid molecules nucleic acid comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence mgrr, t) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 1240 to 1242 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence cay, u) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, in addition to the codon at nucleotide positions 493 to 495 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence tgy,(v) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, further wherein the codon at nucleotide positions 979 to 981 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence gtrr, (w) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17, further wherein the codon at nucleotide positions 490 to 492 in SEQ ID NO 16 or SEQ ID NO 17 has the nucleotide sequence tgy, (x) nucleic acid molecules comprising the nucleic acid sequence from positions 1 to 1428 in the nucleic acid sequence as shown under SEQ ID NO 16 or SEQ ID NO 17,in addition to the codon at nucleotide positions 1225 to 1227 in SEQ ID NO 16 or SEQ ID NO 17 having the nucleotide sequence aar, and) nucleic acid molecules possessing a nucleic acid sequence that has at least 60% identity with any of the nucleic acid sequences defined under a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w), ox), given that each nucleotide sequence of the codon as defined under a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w), ox), respectively, is also present in QL7 ίΠΠ / ίΖηΖ / E / ΥΙ 101 corresponding nucleotide position of the codon in the nucleic acid sequence that has at least 60% identity with any of the nucleic acid sequences defined under each of a), b), c), d), e), f), g), h), i), j), k), l), m), n), o), p), q), r), s), t), u), v), w) ox)., 9. A recombinant nucleic acid molecule comprising a nucleic acid molecule according to any of claims 6 to 8.

10. A recombinant nucleic acid molecule according to claim 9, wherein the recombinant nucleic acid molecule is a vector or a plasmid.

11. A host cell comprising a protein according to any of claims 1 to 5 or comprising a nucleic acid molecule according to any of claims 6 to 8 or comprising a recombinant nucleic acid molecule according to any of claims 9 or 10.

12. A method for the production of an amine comprising the steps of a) providing an amine acceptor molecule; b) providing an amine donor molecule; c) contacting the amine acceptor molecule provided in step a) and the amine donor molecule provided in step b) with a protein according to any one of claims 1 to 5.

13. A method for decreasing the amount of an amine enantiomer in a composition comprising (R)- and fSJ-amine enantiomers, comprising the steps of a) providing a composition comprising (R)- and fSJ-amine enantiomers; b) providing an amine acceptor molecule; c) contacting the composition provided in step a) and the amine acceptor provided in step b) with a protein according to any one of claims 1 to 5.