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Kinetic Resolution of Aliphatic β‐Amino Acid Amides by β‐Aminopeptidases
Author(s) -
Heck Tobias,
Seebach Dieter,
Osswald Steffen,
ter Wiel Matthijs K. J.,
Kohler HansPeter E.,
Geueke Birgit
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900184
Subject(s) - kinetic resolution , chemistry , amino acid , resolution (logic) , combinatorial chemistry , organic chemistry , stereochemistry , biochemistry , catalysis , enantioselective synthesis , computer science , artificial intelligence
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.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.