The present disclosure provides engineered polypeptides having imine reductase activity, polynucleotides encoding the engineered imine reductases, host cells capable of expressing the engineered imine reductases, and methods of using these engineered polypeptides with a range of ketone and amine substrate compounds to prepare secondary and tertiary amine product compounds.

The present invention relates to a method including culturing a C.sub.1 compound-assimilating bacterium, which is a methylotroph, and/or a yeast by using a medium comprising, for example, a C.sub.1 compound and/or glycerol as a carbon source, to thereby produce EGT.

The present invention relates to a method including culturing a C.sub.1 compound-assimilating bacterium, which is a methylotroph, and/or a yeast by using a medium comprising, for example, a C.sub.1 compound and/or glycerol as a carbon source, to thereby produce EGT.

The present invention relates to microbial factories, in particular yeast factories, for production of ergothioneine. Also provided are methods for producing ergothioneine in a yeast cell, as well as useful nucleic acids, polypeptides, vectors and host cells.

The present invention relates to microbial factories, in particular yeast factories, for production of ergothioneine. Also provided are methods for producing ergothioneine in a yeast cell, as well as useful nucleic acids, polypeptides, vectors and host cells.

Provided are a transaminase mutant and a method for producing a chiral amine using the same. An amino acid sequence of the transaminase mutant is an amino acid sequence obtained by mutation occurred in an amino acid sequence as shown in SEQ ID NO: 1, and the mutation includes at least one of the following mutation sites: position 3, position 5, position 8, position 25, position 32, position 45, position 56, position 59, position 60, position 84, position 86, position 164, position 176, position 178, position 180, position 187, position 197, position 206, position 207, position 242, position 245, position 319 and position 324.

A process for the preparation of Brivaracetam, an anti-convulsion drug, is provided comprising enzymatic conversion of (2RS)-2-[ (4R)-2-oxo-4-propyl-pyrrolidin-1-yl] butyric acid methyl ester selectively into (2S)-2-[ (4R)-2-oxo-4-propyl-pyrrolidin-1-yl] butyric acid having high chiral purity, using protease from Bacillus licheniformis. Converting the chirally pure acid into an amide results in Brivaracetam.

A process for the preparation of Brivaracetam, an anti-convulsion drug, is provided comprising enzymatic conversion of (2RS)-2-[(4R)-2-oxo-4-propyl-pyrrolidin-1-yl] butyric acid methyl ester selectively into (2S)-2-[(4R)-2-oxo-4-propyl-pyrrolidin-1-yl] butyric acid having high chiral purity, using protease from Bacillus licheniformis. Converting the chirally pure acid into amide results in Brivaracetam.

The systems and methods herein include engineering a host to produce psilocybin using engineered enzymes, genetic changes, and exogenous psilocybin precursor addition (e.g., addition of L-tryptophan to a growing culture of a psilocybin producing recombinant host strain). The process occurs in genetically engineered host cell(s) that can produce psilocybin.

The systems and methods herein include engineering a host to produce psilocybin using engineered enzymes, genetic changes, and exogenous psilocybin precursor addition (e.g., addition of L-tryptophan to a growing culture of a psilocybin producing recombinant host strain). The process occurs in genetically engineered host cell(s) that can produce psilocybin.