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Radicals from S-adenosylmethionine and their application to biosynthesis

Radicals from S-adenosylmethionine and their application to biosynthesis
Radicals from S-adenosylmethionine and their application to biosynthesis
The radical SAM superfamily of enzymes catalyzes a broad spectrum of biotransformations by employing a common obligate intermediate, the 5?-deoxyadenosyl radical (DOA). Radical formation occurs via the reductive cleavage of S-adenosylmethionine (SAM or AdoMet). The resultant highly reactive primary radical is a potent oxidant that enables the functionalization of relatively inert substrates, including unactivated C–H bonds. The reactions initiated by the DOA are breathtaking in their efficiency, elegance and in many cases, the complexity of the biotransformation achieved. This review describes the common features shared by enzymes that generate the DOA and the intriguing variations or modifications that have recently been reported. The review also highlights selected examples of the diverse biotransformations that ensue.

1367-5931
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9

Roach, Peter L. (2010) Radicals from S-adenosylmethionine and their application to biosynthesis. Current Opinion in Chemical Biology. (doi:10.1016/j.cbpa.2010.11.015). (PMID:21159543)

Record type: Article

Abstract

The radical SAM superfamily of enzymes catalyzes a broad spectrum of biotransformations by employing a common obligate intermediate, the 5?-deoxyadenosyl radical (DOA). Radical formation occurs via the reductive cleavage of S-adenosylmethionine (SAM or AdoMet). The resultant highly reactive primary radical is a potent oxidant that enables the functionalization of relatively inert substrates, including unactivated C–H bonds. The reactions initiated by the DOA are breathtaking in their efficiency, elegance and in many cases, the complexity of the biotransformation achieved. This review describes the common features shared by enzymes that generate the DOA and the intriguing variations or modifications that have recently been reported. The review also highlights selected examples of the diverse biotransformations that ensue.

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Published date: 13 December 2010

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Local EPrints ID: 177017
URI: http://eprints.soton.ac.uk/id/eprint/177017
ISSN: 1367-5931
PURE UUID: b5bb239a-4a4b-47cf-a912-8b8d625a41a7
ORCID for Peter L. Roach: ORCID iD orcid.org/0000-0001-9880-2877

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Date deposited: 31 Mar 2011 10:57
Last modified: 14 Mar 2024 02:41

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Author: Peter L. Roach ORCID iD

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