Enhancement of enantioselectivity in the Bacillus subtilis protease-catalyzed hydrolysis of N-free amino acid esters using the ester grouping-modification approach.
The generality of enantioselectivity enhancement through the modification of the alcohol moiety of a substrate ester was ascertained, for in the Bacillus subtilis protease-catalyzed hydrolysis of N-unprotected amino acid esters the enantioselectivity was enhanced largely by switching the conventional methyl ester to esters with a longer alkyl chain such as the isobutyl ester (from E = 3 to E = 130-170 in the case of 4-fluorophenylalanine esters) as in the enzymatic hydrolysis mediated by Aspergillus oryzae protease. There was indeed a profound dependence of E on the nature of the ester grouping.
Miyazawa
Toshifumi
T
Department of Chemistry, Faculty of Science and Engineering, Konan University, Kobe 658-8501, Japan. miyazawa@base2.ipc.konan-u.ac.jp
Minowa
Hiroe
H
Yamada
Takashi
T
D000596:Amino Acids / Q000737:chemistry*; D001236:Aspergillus oryzae / Q000201:enzymology*; D001412:Bacillus subtilis / Q000201:enzymology*; D002384:Catalysis; D004789:Enzyme Activation; D004952:Esters; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000737:chemistry*
D000596:Amino Acids; D004952:Esters; D010447:Peptide Hydrolases