Kinetics of inhibition of β-glucosidase from Ampullarium crossean by bromoacetic acid

被引：23

作者：

Chen, QX ^{[1
]}

Zhang, Z ^{[1
]}

Zhou, XW ^{[1
]}

Zhuang, ZL ^{[1
]}

机构：

[1] Xiamen Univ, Dept Biol, Xiamen 361005, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2000年 / 32卷 / 07期

关键词：

beta-glucosidase; bromoacetic acid; inhibition; kinetics;

D O I：

10.1016/S1357-2725(00)00020-0

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 kinetics of inhibition of beta-glucosidase from Ampullarium crossean by bromoacetic acid (BrAc) has been studied. The results show that the enzyme can be irreversibly and completely inactivated at high BrAc concentration, while at low BrAc concentration, inhibition of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reactions of BrAc with the enzyme were determined. The presence of the substrate offers obvious protection of the enzyme against inhibition by BrAc. The above results suggest that the histidine residue is essential for activity and is situated at or near the active site of the enzyme. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：717 / 723

页数：7

共 18 条

[1] AMYLASES, ALPHA AND BETA [J].