The invention discloses a glutamate dehydrogenase mutant and an application thereof. The mutant is one of the following: a mutant of the amino acid sequence of SEQ ID NO. 1 which has a mutation at lysine at position 402 to phenylalanine or aspartic acid; a mutant which has a mutation at isoleucine at position 406 to phenylalanine or threonine; a mutant which has a mutation at threonine at position 121 and leucine at position 123; a mutant which has a mutation at alanine at position 379 and leucine at position 383. In the invention, the catalytic activity of glutamate dehydrogenase derived from Pseudomonas putida to 2-carbonyl-4-(hydroxymethylphosphonoyl)butanoic acid (PPO) is significantly improved by a molecular transformation method combining directed evolution and a semi-rational design; and the issue of low glutamate dehydrogenase activity in the process of preparing L-glufosinate by reductive amination is solved.

A microorganism is transformed to be capable of producing guanidinoacetic acid (GAA). A method can be used for the fermentative production of GAA using such a microorganism. A corresponding method can be used for the fermentative production of creatine.

A microorganism is transformed to be capable of producing guanidinoacetic acid (GAA). A method can be used for the fermentative production of GAA using such a microorganism. A corresponding method can be used for the fermentative production of creatine.

The present disclosure provides engineered transaminase polypeptides for the production of amines, polynucleotides encoding the engineered transaminases, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases to prepare compounds useful in the production of active pharmaceutical agents.

The present invention relates to an enzyme-catalyzed enantioselective method for preparing primary amines from the corresponding imines by using imine reductase enzymes.

Non-naturally occurring microorganisms are provided that produce taurine and/or taurine precursors, e.g., hypotaurine, sulfoacetaldehyde, or cysteate, utilizing exogenously added enzyme activities. Methods of producing taurine and/or taurine precursors in microbial cultures, and feed and nutritional supplement compositions that include taurine and/or taurine precursors produced in the microbial cultures, such as taurine- and/or taurine precursor-containing biomass, are also provided.

Microorganisms and bioprocesses are provided that convert gaseous C1 containing substrates, such as syngas, producer gas, and renewable H.sub.2 combined with CO.sub.2, into nutritional and other useful bioproducts.

The present invention provides a polypeptide tag and its application in the synthesis of pharmaceutical chemicals, the recombinant nitrilase was obtained by connecting a polypeptide tag to the N-terminus of the amino acid sequence of the nitrilase; wherein amino acids at both ends of the polypeptide tag are uncharged glycine G, and the rest are a random combination of any one or more of glycine G, histidine H, glutamic acid E, aspartic acid D, lysine K and arginine R; The activity of the recombinant nitrilase in the preparation of 1-cyanocyclohexyl acetic acid is up to 3034.7 U/g dcw, the polypeptide tag significantly improves the soluble expression of nitrilase, and the whole cell catalyst hydrolyzes 1M substrate with the same concentration 30 minutes faster than the mother enzyme. The method provided by the present invention can also be used for the biocatalytic reaction of other pharmaceutical intermediates as the substrate catalyzed by the nitrilase, improving the activity of the whole cell catalyst in reaction, and also improving the solubility of other types of nitrilases and the activity of the corresponding whole cell catalysts.

The present invention relates to the provision of an enzymatic method for the preparation of 2,6-bis(hydroxymethyl) pyridine (Formula I) using as substrate 2,6-Dimethlypyridine (2,6-lutidene) and the multicomponent xylene monooxygenase comprising XylM and XylA from Pseudomonas putida (Arthrobacter siderocapsulatus). The enzymatic method of the present invention is advantageous over conventional synthetic preparations, providing access to the title compound with a one-step enzymatic procedure.

Provided is a method for manufacturing a 3-hydroxy-4-aminobenzoic acid by using a microorganism. The method for manufacturing a 3-hydroxy-4-aminobenzoic acid comprises a step of bringing a 4-aminobenzoic acid into contact with a microorganism that produces the following polypeptide (A) or (B): (A) a polypeptide consisting of an amino acid sequence shown in SEQ ID NO: 2 or a polypeptide consisting of an amino acid sequence that has at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2 and has 4-hydroxybenzoate hydroxylase activity, (B) a polypeptide consisting of an amino acid sequence shown in SEQ ID NO: 6 or a polypeptide consisting of an amino acid sequence that has at least 90% identity to the amino acid sequence shown in SEQ ID NO: 6 and has 4-hydroxybenzoate hydroxylase activity.