Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.
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.
Busca
Patricia
P
Department of Chemistry, Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland.
Paradisi
Francesca
F
Moynihan
Eamonn
E
Maguire
Anita R
AR
Engel
Paul C
PC
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
D000596:Amino Acids; D000594:Amino Acid Oxidoreductases; C022342:phenylalanine oxidase