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Issue 10, 2011
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Radical S-adenosylmethionine enzymes: Mechanism, control and function

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Abstract

Covering: January 2007 to March 2011

The radical SAM superfamily of enzymes use an iron sulfur cluster to reduce S-adenosylmethionine, which leads to the formation of a highly reactive intermediate, usually the 5′-deoxyadenosyl radical. This potent oxidant is able to functionalize relatively inert substrates, including unactivated C–H bonds. This reactivity is evidently useful, as radical SAM enzymes are widely distributed throughout metabolism and catalyze some of the most complex and elegant biotransformations. In the first part of this review, the focus is on the mechanism of radical formation, including the features shared across the family, followed by a discussion of recent evidence for variations in cluster binding motifs and the mechanism of radical formation. In the second part, we survey how radical SAM chemistry has been applied to biosynthesis.

Graphical abstract: Radical S-adenosylmethionine enzymes: Mechanism, control and function

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Publication details

The article was received on 25 Apr 2011 and first published on 21 Jul 2011


Article type: Review Article
DOI: 10.1039/C1NP00036E
Citation: Nat. Prod. Rep., 2011,28, 1696-1721

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    Radical S-adenosylmethionine enzymes: Mechanism, control and function

    M. R. Challand, R. C. Driesener and P. L. Roach, Nat. Prod. Rep., 2011, 28, 1696
    DOI: 10.1039/C1NP00036E

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