Self-sacrifice in radical S-adenosylmethionine proteins

被引：104

作者：

Booker, Squire J. ^{[1
]}

Cicchillo, Robert M.

Grove, Tyler L.

机构：

[1] Penn State Univ, Dept Chem, University Pk, PA 16803 USA

[2] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16803 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2007年 / 11卷 / 05期

关键词：

D O I：

10.1016/j.cbpa.2007.08.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The radical SAM superfamily of metalloproteins catalyze the reductive cleavage of S-adenosyl-L-methionine to generate a 5'-deoxyadenosyl radical (5'-dA(center dot)) intermediate that is obligate for turnover. The 5'-dA(center dot) acts as a potent oxidant, initiating turnover by abstracting a hydrogen atom from an appropriate substrate. A special class of these enzymes use this strategy to functionalize unactivated C-H bonds by insertion of sulfur atoms. This review will describe the characterization of three members of this class - biotin synthase, lipoyl synthase, and MiaB protein - each of which has been shown to cannibalize itself during turnover.

引用

页码：543 / 552

页数：10

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