45 results about "Coa transferase" patented technology

Recombinant hosts for producing polyhydroxyalkanoates and methods of producing polyhydroxyalkanoates from renewable carbon substrates are provided. Certain recombinant hosts that produce 5 carbon chemicals such as 5-aminopentanoate (5AP), 5-hydroxyvalerate (5HV), glutarate, and 1,5 pentanediol (PDO) are also provided. One embodiment provides a recombinant host expressing a gene encoding a heterologous enzyme selected from the group consisting of a polyhydroxyalkanoate synthase and a 5-hydroxyvalerate-CoA (5HV-CoA) transferase, wherein the host produces a polymer containing 5-hydroxyvalerate. Preferably, the host expresses both a polyhydroxyalkanoate synthase and a 5HV-CoA transferase. The host can be prokaryotic or eukaryotic. A preferred prokaryotic host is E. coli. The polymers produced by the recombinant hosts can be homopolymers or copolymers of 5-hydroxyvalerate. A preferred copolymer is poly(3-hydroxybutyrate-co-5-hydroxyvalerate).

The invention provides a non-naturally occurring microbial organism having a muconate pathway having at least one exogenous nucleic acid encoding a muconate pathway enzyme expressed in a sufficient amount to produce muconate. The muconate pathway including an enzyme selected from the group consisting of a beta-ketothiolase, a beta-ketoadipyl-CoA hydrolase, a beta-ketoadipyl-CoA transferase, a beta-ketoadipyl-CoA ligase, a 2-fumarylacetate reductase, a 2-fumarylacetate dehydrogenase, a trans-3-hydroxy-4-hexendioate dehydratase, a 2-fumarylacetate aminotransferase, a 2-fumarylacetate aminating oxidoreductase, a trans-3-amino-4-hexenoate deaminase, a beta-ketoadipate enol-lactone hydrolase, a muconolactone isomerase, a muconate cycloisomerase, a beta-ketoadipyl-CoA dehydrogenase, a 3-hydroxyadipyl-CoA dehydratase, a 2,3-dehydroadipyl-CoA transferase, a 2,3-dehydroadipyl-CoA hydrolase, a 2,3-dehydroadipyl-CoA ligase, a muconate reductase, a 2-maleylacetate reductase, a 2-maleylacetate dehydrogenase, a cis-3-hydroxy-4-hexendioate dehydratase, a 2-maleylacetate aminoatransferase, a 2-maleylacetate aminating oxidoreductase, a cis-3-amino-4-hexendioate deaminase, and a muconate cis/trans isomerase. Other muconate pathway enzymes also are provided. Additionally provided are methods of producing muconate.

The gene encoding a 4-hydroxybutyryl-Co A transferase has been isolated from bacteria and integrated into the genome of bacteria also expressing a polyhydroxyalkanoate synthase, to yield an improved production process for 4HB-containing polyhydroxyalkanoates using transgenic organisms, including both bacteria and plants. The new pathways provide means for producing 4HB containing PHAs from cheap carbon sources such as sugars and fatty acids, in high yields, which are stable. Useful strains are obtaining by screening strains having integrated into their genomes a gene encoding a 4HB-CoA transferase and/or PHA synthase, for polymer production. Processes for polymer production use recombinant systems that can utilize cheap substrates. Systems are provided which can utilize amino acid degradation pathways, α-ketoglutarate, or succinate as substrate.

The present invention relates to a group of glycosyl transferase and applications thereof, and specifically provides applications of the glycosyl transferase gGT29-7 and a derived polypeptide thereof in terpene compound glycosylation catalysis and new saponin synthesis, wherein the glycosyl transferase can specifically and efficiently transfer the glycosyl from a glycosyl donor to the first glycosyl on C-3 site and/or C-6 site of a tetracyclic triterpene compound so as to extend the sugar chain. The glycosyl transferase of the present invention can further be used for constructing artificial ly-synthesized rare ginsenosides and a variety of new ginsenosides and derivatives thereof.

The invention relates to a group of glycosyl transferases and applications of the glycosyl transferases. Particularly, the invention provides applications of glycosyl transferases gGT25, gGT13, gGT30, gGT25-1, gGT25-3, gGT25-5, gGT29, gGT29-3, gGT29-4, gGT29-5, gGT29-6, gGT29-7, 3GT1, 3GT2, 3GT3 and 3GT4, and derived peptides of the glycosyl transferases in glycosylation catalysis and new saponin synthesis of terpenoids. The glycosyl transferases can specifically and efficiently catalyze hydroxyl glycosylation of C-20 bit and/or C-6 bit and/or C-3 of a tetracyclic triterpenoid compound substrate, and/or transfers the glycosyl groups from glycosyl donors to the first glycosyl groups of the C-3 bit and C-6 bit of the tetracyclic triterpenoid compound to extend a carbohydrate chain. The glycosyl transferases disclosed by the invention can also be applied to building synthetic rare ginsenosides and a plurality of novel ginsenosides and derivatives of the ginsenosides.

The invention discloses glycosyl transferase participating in neoandrographolide biosynthesis as well as coding genes and application thereof. The protein provided by the invention is derived from herba andrographitis, and is (a1) or (a5) as follows: (a1) a protein composed of an amino acid sequence shown as a sequence 1 in a sequence table; and (a5) a protein composed of an amino acid sequence shown as a sequence 3 in the sequence table. The invention further discloses application of the protein serving as glycosyl transferase. The glycosyl transferase participates in plant growth and development and secondary metabolism processes. The discovery of the glycosyl transferase and coding genes thereof has important significance. The invention provides a basis for further describing biosynthesis of glycoside compounds in the herba andrographitis, contributes to analyzing a biosynthetic pathway of glycoside active ingredients in the herba andrographitis, and provides novel material basis and gene resources for new drug research and development.

The invention discloses a method for synthetizing chiral cyclic alkyl amino acid by amino transferase. The commercialized material ketonic acid or corresponding soluble ketonic acid salt compound in the market is selected as an initial material; the initial material is dissolved into phosphate buffer, and added to an amino supply body; pyridoxal phosphate (PLP) and amino transferase main enzyme are added to a system containing the amino supply body and main material ketonic acid or corresponding soluble ketonic acid salt compound to react under constant temperature, and obtaining a product with a high ee value, wherein n is equal to 1, 2, 3, 4, 5, or obtaining a product wherein n is equal to 0 and 1. The method is stable in technological condition, simple to operate, high in yield, low in cost, and suitable for large-scale production, and beneficial for environmental protection; and a novel train of thought and a method are provided for the preparation of chiral cyclic alkyl amino acid compound.

The present invention relates to a recombinant microorganism having an enhanced ability to produce ethanol and butanol and a method for preparing ethanol and butanol using the same, and more particularly to a recombinant microorganism having an enhanced ability to produce ethanol and butanol, into which a gene encoding CoA transferase and a gene encoding alcohol/aldehyde dehydrogenase are introduced, and to a method for preparing ethanol and butanol using the same. The recombinant microorganism according to the present invention, obtained by manipulating metabolic pathways of microorganisms, is capable of producing butanol and ethanol exclusively without producing any byproduct, and thus is useful as a microorganism producing industrial solvents and transportation fuel.

The industrial production process of fruit oligosaccharide with cane sugar as material includes two parts, the industrial production of immobilized fructose-base transferase preparation and the production of fruit oligosaccharide by means of the enzyme preparation. Selected excellent strain capable of secreting fructose-base transferase is cultured in proper culture medium, the obtained mycelium is wall broken, and the enzyme is separated and purified through centrifugal process and superfiltering process and reagent immobilized. Fruit oligosaccharide is then produced through batched reaction process or column reaction process with the immobilized fructose-base transferase. The fruit oligosaccharide may be used to produce fruit oligosaccharide syrup without passing through active carbon decoloring and exchange column desalting.

This document describes biochemical pathways for producing 2,3-dehydroadipyl-CoA methyl ester from precursors such as 2-oxoglutarate using one or more of a fatty acid O-methyltransferase, a thioesterase, a CoA-transferase and a CoA ligase, as well as recombinant hosts expressing one or more of such enzymes. 2,3-dehydroadipyl-CoA methyl ester can be enzymatically converted to adipyl-CoA using a trans-2-enoyl-CoA reductase, and a methylesterase, which in turn can be enzymatically converted to adipic acid, 6-aminohexanoate, 6-hydroxyhexanoate, caprolactam, hexamethylenediamine, or 1,6-hexanediol.

The invention relates to an emulsifier, a method for preparing said emulsifier, and to its use in various applications, primarily food and cosmetic applications. The invention also relates to the use of said emulsifier for the creation of an elastic, gelled foam. An emulsifier according to the invention is based on a starch which is enzymatically converted, using a specific type of enzyme, and modified in a specific esterification reaction.

This document describes biochemical pathways for producing 2(E)-heptenedioyl-CoA methyl ester from precursors such as 2-oxo-glutarate, acetyl-CoA, or succinyl-CoA using one or more of a fatty acid O-methyltransferase, a thioesterase, a CoA-transferase, a CoA ligase, as well as recombinant hosts expressing one or more of such enzymes. 2(E)-heptenedioyl-CoA methyl ester can be enzymatically converted to pimeloyl-CoA using a trans-2-enoyl-CoA reductase, and a methylesterase. Pimeloyl-CoA can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

The invention discloses a universal sulfo-group transferase activity analysis method. According to the method, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), sulfo-group transferase and a sulfo-group transferase specific substrate are mixed to be subjected to a sulfonation reaction to generate 3'-phosphoadenosine-phosphate, an IMPAD1 enzyme can specifically hydrolyze 3'-phosphoadenosine-5'-phosphosulfate to release a phosphate group (Pi), and Pi is subjected to fluorogenic quantitative detection through a mixed system composed of metal ions (Mn+) which has a high combining capacity with Pi and a specific fluorescent probe (FP), and quantitative analysis of an sulfo-group transferase activity can be achieved. According to the system, the combination of Mn+ and FP causes that a fluorescence system is effectively quenched, Pi generated in the reaction process effectively shields Mn+, therefore the fluorescence signal of FP is restored. Therefore, by monitoring the change situation of the fluorescence signal in the system, fluorescence reinforced sensing of the sulfo-group transferase activity can be achieved. The universal sulfo-group transferase activity analysis method is generally applicable to detection of the sulfo-group transferase activity with PASA being a sulfonic group donor.

An object of the present invention is to provide a technique for producing 1,4-butanediol by recombinant cells. Provided is a recombinant cell that is acetogenic and obligatory anaerobic, wherein the recombinant cell includes a gene encoding at least one enzyme selected from the group consisting of succinate semialdehyde dehydrogenase, succinyl-CoA synthase, CoA-dependent succinate semialdehyde dehydrogenase, 4-hydroxybutyrate dehydrogenase, 4-hydroxybutyryl-CoA transferase, 4-hydroxybutyryl-CoA reductase, 4-hydroxybutyraldehyde dehydrogenase, and alcohol dehydrogenase, the gene is expressed in the recombinant cell, and the recombinant cell produces 1,4-butandiol.

The invention includes a selective method of modifying the N-terminus of a protein using an aminoacyl tRNA transferase. In certain embodiments, the method comprises contacting a solution of the protein or peptide with a transferase and a derivative of a molecule, whereby the N-terminus of the protein or peptide is derivatized with the molecule.

The present invention relates to a recombinant microorganism to which a gene coding for 2-hydroxyisocaproate-CoA transferase and a gene coding for polyhydroxyalkanoate synthase are introduced and which has a potential of producing polyhydroxyalkanoate bearing an aromatic monomer or a long-chain 2-HA monomer and a method for producing polyhydroxyalkanoate bearing an aromatic monomer or a long-chain 2-HA monomer, using the recombinant microorganism. According to the present invention, a biodegradable polymer bearing an aromatic monomer or a long-chain 2-HA monomer can be produced.

This document describes polypeptides with dual CoA transferase and β-ketothiolase activities and variants thereof, use of such polypeptides in biosynthetic methods, and non-naturally occurring hosts comprising such polypeptides.