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Radical S-adenosylmethionine enzymes: mechanism, control and function

Radical S-adenosylmethionine enzymes: mechanism, control and function
Radical S-adenosylmethionine enzymes: mechanism, control and function
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.
0265-0568
1696-1721
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
Driesener, R
2bf3020f-4b50-4ba6-be3e-9c785559f37f
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
Driesener, R
2bf3020f-4b50-4ba6-be3e-9c785559f37f
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9

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

Record type: Article

Abstract

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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Published date: 21 July 2011
Organisations: Chemistry

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Local EPrints ID: 336608
URI: http://eprints.soton.ac.uk/id/eprint/336608
ISSN: 0265-0568
PURE UUID: e9bd07ff-de0a-49f8-9338-0dd5b9689e2a
ORCID for Peter L. Roach: ORCID iD orcid.org/0000-0001-9880-2877

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Date deposited: 30 Mar 2012 12:50
Last modified: 14 Mar 2024 10:45

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Contributors

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

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