Kinetic resolution of aliphatic beta-amino acid amides by beta-aminopeptidases.
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.
Heck
Tobias
T
Eawag, Das Wasserforschungs-Institut des ETH-Bereichs, Uberlandstrasse 133, 8600 Dübendorf, Switzerland.
Seebach
Dieter
D
Osswald
Steffen
S
Ter Wiel
Matthijs K J
MK
Kohler
Hans-Peter E
HP
Geueke
Birgit
B
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
D000577:Amides; D000596:Amino Acids; D000626:Aminopeptidases