9 results about "Phosphotransferase" patented technology

The present invention relates to a novel and efficient method for sialylation of a glycoside comprising mixing said glycoside with sialic acid, cytidine monophosphate, nucleoside triphosphate and one or more cell-free extracts of a microorganism, the present invention relates to a microorganism comprising one or more endogenous polypeptides having inorganic diphosphatase activity and one or more endogenous polypeptides having phosphotransferase activity, and wherein the one or more cell-free extracts comprise: at least one polypeptide having cytidine monophosphate kinase activity, at least one polypeptide having N-acyl neuraminic acid cytidyltransferase activity, and at least one polypeptide having sialyltransferase activity, thereby sialylating the glycoside.

This invention relates to the field of biotechnology, and discloses an engineered *Yarrowia lipolytica* strain that produces p-coumaric acid using glucose as a substrate, its construction method, and its applications. Construction method: A tyrosine ammonia-lyase gene is integrated using a CRISPR / Cas9 localization and integration method. TAL In *Yarrowia lipophila* strains, the DAHP synthase gene was enhanced. ARO4 , DHS1 and AROG Overexpression of tyrosine synthase TYR Genes and histidine phosphotransferases HIS5 The protease gene was further integrated to synthesize exogenous phenylalanine deamination and hydroxylation pathway genes for p-coumaric acid, including phenylalanine ammonia-lyase gene, cinnamate hydroxylase gene, and P450 reductase gene. The p-coumaric acid produced by the engineered *Yarrowia lipolytica* strain of this invention can reach a maximum yield of 1.7 g / L in shake flasks, and a yield of 30 g / L in a 5 L fed-batch fermentation tank, demonstrating significant industrial application value.

The invention discloses an OMV vaccine capable of preventing group B streptococcus III serotype infection and a preparation method thereof. The invention belongs to the field of synthetic biology, and particularly relates to an OMV vaccine capable of preventing group B streptococcus III serotype infection and a preparation method of the OMV vaccine. The recombinant escherichia coli contains a lipoid A deacylase coding gene, a lipoid A dephosphatase coding gene and a group B streptococcus capsular polysaccharide length control gene coding gene; the gene does not contain an acetyl glucosamine phosphotransferase coding gene, an escherichia coli O antigen synthesis gene cluster coding gene, a lipoid A myristoyl transferase coding gene, an escherichia coli O antigen chain length control gene coding gene, a lipoid A palmitoyl transferase coding gene and an escherichia coli sialic acid degradation gene cluster coding gene. The composition also contains a group B streptococcus III capsular polysaccharide synthesis cluster coding gene. The recombinant escherichia coli can be used for producing an OMV vaccine for preventing group B streptococcus III serotype infection.

This invention discloses a streptomycin resistance gene, its encoded protein, and its applications, belonging to the field of plant pathology technology. This invention discovers a novel streptomycin resistance gene derived from *Tomato Canker*. aph(3) This gene is located on a newly discovered plasmid pCM3 of *Tomato Canker*, encoding a protein APH(3) belonging to the aminoglycoside antibiotic phosphotransferase family. This invention verified the function of this gene through gene knockout, functional complementation, and heterologous expression experiments. Simultaneously, mass spectrometry analysis demonstrated that APH(3) catalyzes the phosphorylation of streptomycin molecules, generating streptomycin monophosphate, thereby eliminating its inhibitory activity against bacteria. Strains carrying this gene exhibit significant resistance to streptomycin. This invention relates to a streptomycin resistance gene. aph(3) It can be widely used in the study of pathogen resistance mechanisms, screening of resistant strains, and selection of molecular markers, and has important scientific research and application value.

The present application relates to the field of agricultural biotechnology, and in particular to a method for constructing an engineered strain of Rhodopseudomonas palustris for producing inositol using glucose, glycerol and CO2 as carbon sources, and the strain. The present application mutates the gene nagE encoding N-acetylglucosamine-specific phosphotransferase system in the genome of Rhodopseudomonas palustris (G265R), and knocks out the gene nagR encoding a transcriptional regulator of the GntR family, so that Rhodopseudomonas palustris can efficiently utilize glucose. On this basis, an engineered strain of Rhodopseudomonas palustris H16 is constructed for synthesizing inositol using renewable substrates (glucose and glycerol) and CO2 as carbon source. Based on this technology, not only the synthesis of bioactive substances can be achieved, but also a method for efficiently eliminating greenhouse gases in the atmosphere.

Provided are amino acid sequences for modified, truncated forms of human GlcNA-1-Phosphotransferase (PTase) that retain phosphotransferase activity and the ability to phosphorylate proteins, lysosomal or non-lysosomal. Truncated forms of PTase lacking or with modified linkers and / or lacking the C-terminal transmembrane and cytosolic domain are demonstrated to retain phosphotransferase activity and the ability to phosphorylate target proteins.

The invention provides a method for synthesizing p-hydroxybenzaldehyde from p-hydroxybenzoic acid through light-driven enzyme catalysis. A used reaction system comprises carboxylic acid reductase (CAR), a photosynthesis unit, ferredoxin (Fdx) and phosphotransferase (PAP). According to the method, light energy is utilized to drive spinach capsule membranes to co-regenerate NADPH and ATP, and the problem that carboxylic acid reductase needs coenzyme supply of NADPH and ATP at the same time is solved. According to the method, a light energy driven enzyme catalysis method is adopted, a biological photosynthetic reaction is used for replacing a traditional high-energy-consumption and high-pollution chemical process, and green and efficient synthesis of p-hydroxybenzaldehyde is achieved through cooperation of double-coenzyme light regeneration and enzyme specific catalysis.

The application discloses a recombinant escherichia coli for producing N-acetylneuraminic acid as well as a construction method and application thereof, and belongs to the technical field of genetic engineering. The recombinant escherichia coli can grow in glucose and glycerol double carbon sources, synthesize N-acetylneuraminic acid and has extremely low acetic acid generation by knocking out 6-phosphofructokinase, introducing a glycerol kinase mutant, replacing PTS phosphotransferase I with a glucose-promoted diffusion transporter and optimizing a promoter. On this basis, the application further knocks out the 6-phosphofructokinase coding gene pfkB, introduces a heterologous ED pathway from Pseudomonas aeruginosa, and further improves the yield under the hole plate level to 9.44 g / L through copy number optimization and RBS intensity optimization.

This invention provides a method for producing allicinol from recombinant *Escherichia coli* using glycerol and glucose as substrates. Using *E. coli* K-12 as the substrate host, a pathway for the synthesis of allicinol from glycerol and glucose is constructed by expressing genes fucA, yqaB, aldO, and rdh, and knocking out the glucose-specific phosphotransferase system IIBC component gene ptsG. Subsequently, genes mzwf, mgnd, alsE, and a6PP are introduced, while genes pfkA, gnd, and edd are knocked out to regulate the flux of the glycolysis and pentose phosphate pathways, thereby directing more carbon sources to the allicinol synthesis pathway. Finally, the formate dehydrogenase gene fdh and the glycerol kinase mutant gene glpK22 are introduced, and the methylglyoxal synthase gene mgsA is knocked out to construct a cofactor NADH cycle system and optimize the allicinol synthesis pathway, thus enabling *E. coli* to efficiently produce allicinol from glycerol and glucose through fermentation.