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

Article abstract of DOI:10.1246/cl.1991.1723

Peculiar enantioselective hydrolysis of N-acyl amino acid esters was found in the bilayer vesicular systems containing the tripeptide-type histidine derivative, Z-L-Leu-L-His-L-Leu.The enantioselectivity for the hydrolysis of long chain N-acyl phenylalanine p-nitrophenyl ester, C16-Phe-PNP, appeared in the binding process and was governed by an entropy factor.