SUBSTRATE-DECREASED MODIFICATION BY DIETHYL PYROCARBONATE OF 2 HISTIDINES IN ISOCITRATE LYASE FROM ESCHERICHIA-COLI

被引：21

作者：

KO, YH ^{[1
]}

VANNI, P ^{[1
]}

MUNSKE, GR ^{[1
]}

MCFADDEN, BA ^{[1
]}

机构：

[1] WASHINGTON STATE UNIV,DEPT BIOCHEM & BIOPHYS,PULLMAN,WA 99164

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 30期

关键词：

D O I：

10.1021/bi00244a012

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 inactivation of tetrameric 188-kDa isocitrate lyase from Escherichia coli at pH 6.8 (37-degrees-C) by diethyl pyrocarbonate, exhibiting saturation kinetics, is accompanied by modification of histidine residues 266 and 306. Substrates isocitrate, glyoxylate, or glyoxylate plus succinate protect the enzyme from inactivation, but succinate alone does not. Removal of the carbethoxy groups from inactivated enzyme by treatment with hydroxylamine restores activity of isocitrate lyase. The present results suggest that the group-specific modifying reagent diethyl pyrocarbonate may be generally useful in determining the position of active site histidine residues in enzymes.

引用

页码：7451 / 7456

页数：6

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