title: Kinetic resolution of aliphatic beta-amino acid amides by beta-aminopeptidases.
abstract: The growing demand for enantiomerically pure beta-amino acids to be used in the pharmaceutical industry and as fine chemicals requires the development of new strategies for their synthesis. The beta-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 beta-amino acids from peptides and amides. Hydrolysis of racemic beta(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 beta(3)-amino acids of high enantiopurity. This approach presents a new access to enantiopure beta(3)-amino acids under mild reaction conditions and complements chemical asymmetric synthesis strategies.
authors.affiliation: Eawag, Das Wasserforschungs-Institut des ETH-Bereichs, Uberlandstrasse 133, 8600 Dübendorf, Switzerland.
authors.forename: Tobias
authors.initials: T
authors.lastname: Heck
authors.forename: Dieter
authors.initials: D
authors.lastname: Seebach
authors.forename: Steffen
authors.initials: S
authors.lastname: Osswald
authors.forename: Matthijs K J
authors.initials: MK
authors.lastname: Ter Wiel
authors.forename: Hans-Peter E
authors.initials: HP
authors.lastname: Kohler
authors.forename: Birgit
authors.initials: B
authors.lastname: Geueke
mesh_terms: D020561:Alphaproteobacteria / Q000201:enzymology; D000577:Amides / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry / Q000302:isolation & purification*; D000626:Aminopeptidases / Q000378:metabolism*; D055162:Biocatalysis; D007700:Kinetics; D020621:Ochrobactrum anthropi / Q000201:enzymology; D013237:Stereoisomerism
chemical_list: D000577:Amides; D000596:Amino Acids; D000626:Aminopeptidases