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Self-sacrifice in radical S-adenosylmethionine proteins.


ABSTRACT: The radical SAM superfamily of metalloproteins catalyze the reductive cleavage of S-adenosyl-l-methionine to generate a 5'-deoxyadenosyl radical (5'-dA*) intermediate that is obligate for turnover. The 5'-dA* 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.

SUBMITTER: Booker SJ 

PROVIDER: S-EPMC2637762 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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Self-sacrifice in radical S-adenosylmethionine proteins.

Booker Squire J SJ   Cicchillo Robert M RM   Grove Tyler L TL  

Current opinion in chemical biology 20071001 5


The radical SAM superfamily of metalloproteins catalyze the reductive cleavage of S-adenosyl-l-methionine to generate a 5'-deoxyadenosyl radical (5'-dA*) intermediate that is obligate for turnover. The 5'-dA* 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  ...[more]

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