Chemistry Letters

Enantioselective hydrolysis of N-Acyl Amino Acid Esters by Tripeptide-type L-Histidine Derivative in a Bilayer Vesicular System.

K Ohkubo, H Ishida, K Yamaki, M Kawata

Index: Ohkubo, Katsutoshi; Ishida, Hitoshi; Yamaki, Kazuhiro; Kawata, Masahiko Chemistry Letters, 1991 , # 10 p. 1723 - 1726

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Citation Number: 6

Abstract

Peculiar enantioselective hydrolysis of N-acyl amino acid esters was found in the bilayer vesicular systems containing the tripeptide-type histidine derivative, ZL-Leu-L-His-L-Leu. The enantioselectivity for the hydrolysis of long chain N-acyl phenylalanine p-nitrophenyl ester, C 16-Phe-PNP, appeared in the binding process and was governed by an entropy factor.