| Literature DB >> 21568844 |
N A Kuznetsov1, V V Koval, O S Fedorova.
Abstract
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.Entities:
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Year: 2011 PMID： 21568844 DOI： 10.1134/s0006297911010123
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN： 0006-2979 Impact factor: 2.487