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Trends Biochem Sci. 2007 Mar;32(3):101-10. Epub 2007 Feb 8.

S-adenosylmethionine as an oxidant: the radical SAM superfamily.

Author information

1
Department of Biochemistry, University of Wisconsin-Madison, 1710 University Avenue, Madison, WI 53726, USA.

Erratum in

  • Trends Biochem Sci. 2007 May;32(5):209.

Abstract

A recently discovered superfamily of enzymes function using chemically novel mechanisms, in which S-adenosylmethionine (SAM) serves as an oxidizing agent in DNA repair and the biosynthesis of vitamins, coenzymes and antibiotics. Members of this superfamily, the radical SAM enzymes, are related by the cysteine motif CxxxCxxC, which nucleates the [4Fe-4S] cluster found in each. A common thread in the novel chemistry of these proteins is the use of a strong reducing agent--a low-potential [4Fe-4S](1+) cluster--to generate a powerful oxidizing agent, the 5'-deoxyadenosyl radical, from SAM. Recent results are beginning to determine the unique biochemistry for some of the radical SAM enzymes, for example, lysine 2,3 aminomutase, pyruvate formate lyase activase and biotin synthase.

PMID:
17291766
DOI:
10.1016/j.tibs.2007.01.002
[Indexed for MEDLINE]

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