Abstract
Access to enantiopure β‐amino acids: β‐Aminopeptidases are hydrolases that possess the unique ability to cleave N‐terminal β‐amino acids from peptides and amides. Hydrolysis of racemic β‐amino acid amides catalyzed by these enzymes displays enantioselectivity with strong preference for substrates with the L‐configuration, and gives access to various aliphatic β‐amino acids of high enantiopurity.magnified image
The growing demand for enantiomerically pure β‐amino acids to be used in the pharmaceutical industry and as fine chemicals requires the development of new strategies for their synthesis. The β‐aminopeptidases BapA from Sphingosinicella xenopeptidilytica 3‐2W4, BapA from Sphingosinicella microcystinivorans Y2, and DmpA from Ochrobactrum anthropi LMG7991 are hydrolases that possess the unique ability of cleaving N‐terminal β‐amino acids from peptides and amides. Hydrolysis of racemic β^3^‐amino acid amides catalyzed by these enzymes displays enantioselectivity with a strong preference for substrates with the L‐configuration and gives access to various aliphatic β^3^‐amino acids of high enantiopurity. This approach presents a new access to enantiopure β^3^‐amino acids under mild reaction conditions and complements chemical asymmetric synthesis strategies.