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Issue 11, 2012
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Radical SAM enzymes in methylation and methylthiolation

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Abstract

Radical S-adenosyl-L-methionine (SAM) enzymes are a large and diverse superfamily with functions ranging from enzyme activation through a single H atom abstraction to complex organic and metal cofactor synthesis involving a series of steps. Though these enzymes carry out a variety of functions, they share common structural and mechanistic characteristics. All of them contain a site-differentiated [4Fe–4S] cluster, ligated by a CX3CX2C or similar motif, which binds SAM at the unique iron. The [4Fe–4S]1+ state of the cluster reductively cleaves SAM to produce a 5′-deoxyadenosyl radical, which serves to initiate the diverse reactions catalyzed by these enzymes. Recent highlights in the understanding of radical SAM enzymes will be presented, with a particular emphasis on enzymes catalyzing methylation and methythiolation reactions.

Graphical abstract: Radical SAM enzymes in methylation and methylthiolation

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Publication details

The article was received on 10 Jul 2012, accepted on 30 Aug 2012 and first published on 31 Aug 2012


Article type: Minireview
DOI: 10.1039/C2MT20136D
Citation: Metallomics, 2012,4, 1149-1154

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    Radical SAM enzymes in methylation and methylthiolation

    R. U. Hutcheson and J. B. Broderick, Metallomics, 2012, 4, 1149
    DOI: 10.1039/C2MT20136D

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