title: Enhancement of enantioselectivity in the Bacillus subtilis protease-catalyzed hydrolysis of N-free amino acid esters using the ester grouping-modification approach.
abstract: 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.
authors.affiliation: Department of Chemistry, Faculty of Science and Engineering, Konan University, Kobe 658-8501, Japan. miyazawa@base2.ipc.konan-u.ac.jp
authors.forename: Toshifumi
authors.initials: T
authors.lastname: Miyazawa
authors.forename: Hiroe
authors.initials: H
authors.lastname: Minowa
authors.forename: Takashi
authors.initials: T
authors.lastname: Yamada
mesh_terms: 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*
chemical_list: D000596:Amino Acids; D004952:Esters; D010447:Peptide Hydrolases