Binding site of acyl moiety in ester hydrolysis by Candida rugosa lipase

被引：2

作者：

Goto, M

Kawasaki, M

Kometani, T

Nonaka, T

Mitsui, Y

机构：

[1] Toyama Natl Coll Technol, Dept Chem & Biochem Engn, Toyama 9398630, Japan

[2] Toyama Prefectural Univ, Fac Engn, Toyama 9390398, Japan

[3] Nagaoka Univ Technol, Fac Engn, Nagaoka, Niigata 9402188, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2001年 / 11卷 / 4-6期

关键词：

Candida rugosa lipase; specific activity; hydrolysis; tunnel structure; p-nitrophenyl ester;

D O I：

10.1016/S1381-1177(00)00077-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The sizes of the large, medium, and small substituent recognition sites (L, M, and S pockets, respectively) in Candida rugosa lipase (CRL) were roughly estimated by measuring the specific hydrolytic activity against several p-nitrophenyl esters. These relative sizes were assessed as L pocket > phenyl, ethyl > M pocket > methyl > S pocket > hydrogen. The hydrolysis of a series of p-nitrophenyl esters of omega -substituted fatty acids was also examined. In this series, p-nitrophenyl esters having one methylene between the ester-carbonyl carbon and cyclohexyl, phenyl, or isopropyl moiety largely demonstrated decreases in hydrolytic activity. (C) 2001 Elsevier Science B.V. All rights reserved.

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收藏

页码：1029 / 1033

页数：5

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