CRYSTAL STRUCTURE OF A NOVEL (R)-SELECTIVE AMINE TRANSAMINASE AND APPROACHES TO BROADEN ITS SUBSTRATE SCOPE BY RATIONAL ENGINEERING

摘要

We recently identified a novel (R)-selective amine transaminase (ATA); now we want to broaden its substrate scope since ATAs are promising biocatalysts for the production of chiral amines [1]. In general, aminotransferases are pyridoxal-5'-phosphate (PLP)-dependent enzymes, which reversibly catalyze the transfer of an amino group from an amino donor to a ketone or aldehyde, resulting in the formation of chiral amines.