Reshaping the Substrate Binding Pocket of β-Amino Acid Dehydrogenase for the Synthesis of Aromatic β-Amino Acids

By reshaping the substrate-binding pocket of β-amino acid dehydrogenase (β-AADH), some variants were obtained with up to 2560-fold enhanced activity toward the model substrates (S)-β-homophenylalanine and (R)-β-phenylalanine. A few aromatic β-amino acids were prepared with >99% ee and high isolated yields via either kinetic resolution of racemates or reductive amination of the corresponding β-keto acids. This work expands the catalytic capability of β-AADHs and highlights their practical application in the synthesis of pharmaceutically relevant β-amino acids.