S-adenosylmethionine as an oxidant:: the radical SAM superfamily

被引：138

作者：

Wang, Susan C. ^{[1
]}

Frey, Perry A. ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Biochem, Madison, WI 53726 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2007年 / 32卷 / 03期

关键词：

D O I：

10.1016/j.tibs.2007.01.002

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 recently discovered superfamily of enzymes function using chemically novel mechanisms, in which S-adenosylmethionine (SAM) serves as an oxidizing agent in DNA repair and the biosynthesis of vitamins, coenzymes and antibiotics. Members of this superfamily, the radical SAM enzymes, are related by the cysteine motif CxxxCxxC, which nucleates the [4Fe-4S] cluster found in each. A common thread in the novel chemistry of these proteins is the use of a strong reducing agent-a low-potential [4Fe-4S](1+) cluster-to generate a powerful oxidizing agent, the 5'-deoxyadenosyl radical, from SAM. Recent results are beginning to determine the unique biochemistry for some of the radical SAM enzymes, for example, lysine 2,3 aminomutase, pyruvate formate lyase activase and biotin synthase.

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页码：101 / 110

页数：10

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