IMPORTANCE OF HISTIDINE RESIDUE-25 OF RAT HEME OXYGENASE FOR ITS CATALYTIC ACTIVITY

被引：53

作者：

ISHIKAWA, K ^{[1
]}

SATO, M ^{[1
]}

ITO, M ^{[1
]}

YOSHIDA, T ^{[1
]}

机构：

[1] YAMAGATA UNIV,SCH MED,DEPT MOLEC & PATHOL BIOCHEM,YAMAGATA 99023,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 182卷 / 03期

基金：

日本学术振兴会;

关键词：

D O I：

10.1016/0006-291X(92)91828-E

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：

A truncated, soluble, and enzymatically active rat heme oxygenase lacking its membrane-associative, C-terminal segment was expressed in E. coli strain JM109. The roles of its four histidine residues were examined by determining the enzymatic activities of mutant enzymes in which each of these residues in turn was replaced by alanine. Mutation of histidine residue 25 to alanine resulted in marked decrease in activity for heme breakdown, indicating that this histidine residue has an important role in the heme oxygenase reaction. © 1992.

引用

页码：981 / 986

页数：6

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