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See 1 citation in Nat Chem Biol 2012:

Nat Chem Biol. 2012 Dec;8(12):957-9. doi: 10.1038/nchembio.1091. Epub 2012 Oct 14.

Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes.

Author information

1
Institut National de la Recherche Agronomique, UMR 1319 Micalis, Jouy-en-Josas, France.

Abstract

Methylation is among the most widespread chemical modifications encountered in biomolecules and has a pivotal role in many major biological processes. In the biosynthetic pathway of the antibiotic thiostrepton A, we identified what is to our knowledge the first tryptophan methyltransferase. We show that it uses unprecedented chemistry to methylate inactivated sp(2)-hybridized carbon atoms, despite being predicted to be a radical SAM enzyme.

PMID:
23064318
DOI:
10.1038/nchembio.1091
[Indexed for MEDLINE]

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