The University of Southampton
University of Southampton Institutional Repository

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.

Full text not available from this repository.

More information

Published date: 13 December 2010

Identifiers

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

Catalogue record

Date deposited: 31 Mar 2011 10:57
Last modified: 05 Nov 2019 01:54

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×