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Radical S-adenosylmethionine enzymes: mechanism, control and function

Record type: Article

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 50-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.

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Citation

Challand, Martin R., Driesener, R and Roach, Peter L. (2011) Radical S-adenosylmethionine enzymes: mechanism, control and function Natural Product Reports, 28, (10), pp. 1696-1721. (doi:10.1039/C1np00036e).

More information

Published date: 21 July 2011
Organisations: Chemistry

Identifiers

Local EPrints ID: 336608
URI: http://eprints.soton.ac.uk/id/eprint/336608
ISSN: 0265-0568
PURE UUID: e9bd07ff-de0a-49f8-9338-0dd5b9689e2a

Catalogue record

Date deposited: 30 Mar 2012 12:50
Last modified: 18 Jul 2017 06:07

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Contributors

Author: Martin R. Challand
Author: R Driesener
Author: Peter L. Roach

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