Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes - PubMed (original) (raw)

Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes

Stéphane Pierre et al. Nat Chem Biol. 2012 Dec.

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.

PubMed Disclaimer

Similar articles

Cited by

References

    1. J Am Chem Soc. 2009 Jun 24;131(24):8348-9 - PubMed
    1. J Am Chem Soc. 2009 Apr 1;131(12):4327-34 - PubMed
    1. J Biol Chem. 2010 Sep 3;285(36):27525-31 - PubMed
    1. Angew Chem Int Ed Engl. 2000 Jan;39(2):393-395 - PubMed
    1. FEBS J. 2010 Apr;277(8):1906-20 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources