Mechanism of recognition and repair of damaged DNA by human 8-oxoguanine DNA glycosylase hOGG1

被引：25

作者：

Kuznetsov, N. A. ^{[1
]}

Koval, V. V. ^{[1
]}

Fedorova, O. S. ^{[1
]}

机构：

[1] Russian Acad Sci, Siberian Branch, Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2011年 / 76卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

conformational dynamics; pre-steady-state kinetics; human 8-oxoguanine DNA glycosylase; hOGG1; SUBSTRATE RECOGNITION; BIOCHEMICAL EXPLORATION; STRUCTURAL BASIS; EXCISION-REPAIR; HUMAN HOMOLOG; OGG1; GENE; ENZYME; CLONING; PROTEIN; EXPRESSION;

D O I：

10.1134/S0006297911010123

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：

Recent data on structural and biochemical features of human 8-oxoguanine DNA glycosylase (hOGG1) has enabled detailed evaluation of the mechanism by which the damaged DNA bases are recognized and eliminated from the chain. Pre-steady-state kinetic studies with recording of conformational transitions of the enzyme and DNA substrate significantly contribute to understanding of this mechanism. In this review we particularly focus on the interrelationship between the conformational changes of interacting molecules and kinetics of their interaction and on the nature of each elementary step during the enzymatic process. Exhaustive analysis of these data and detailed mechanism of hOGG1-catalyzed reaction are proposed.

引用

页码：118 / 130

页数：13

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