化学修饰酶对氨基酸酯水解具有相当显著的对映选择性。

Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes.

作者信息

Yano Yoshihiro, Shimada Kenji, Okai Jiro, Goto Koichi, Matsumoto Yoko, Ueoka Ryuichi

机构信息

Division of Applied Chemistry, Graduate School of Sojo University, 4-22-1 Ikeda, Kumamoto 860-0082, Japan.

出版信息

J Org Chem. 2003 Feb 21;68(4):1314-8. doi: 10.1021/jo0265075.

DOI:10.1021/jo0265075

PMID:12585870

Abstract

The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-alpha-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-alpha-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl-D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified alpha-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.

摘要

研究了化学修饰酶癸酰-α-胰凝乳蛋白酶和癸酰-胰蛋白酶对对映体底物的水解（脱酰基）作用。癸酰-α-胰凝乳蛋白酶的反应活性低于天然酶，尽管有趣的是，与天然酶相比，其对映选择性显著增强。特别是，对于对硝基苯基 N-十二烷酰-D（L）-苯丙氨酸酯的水解裂解，实现了明显完全的对映选择性催化。然而，癸酰-胰蛋白酶未观察到对映选择性的增强。这些结果表明，通过添加疏水基团进行化学修饰的α-胰凝乳蛋白酶促进了对疏水酯水解的对映选择性。