title: Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.
abstract: The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous alpha-amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.
authors.affiliation: Department of Chemistry, Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland.
authors.forename: Patricia
authors.initials: P
authors.lastname: Busca
authors.forename: Francesca
authors.initials: F
authors.lastname: Paradisi
authors.forename: Eamonn
authors.initials: E
authors.lastname: Moynihan
authors.forename: Anita R
authors.initials: AR
authors.lastname: Maguire
authors.forename: Paul C
authors.initials: PC
authors.lastname: Engel
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D000594:Amino Acid Oxidoreductases; C022342:phenylalanine oxidase