Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes - Archive ouverte HAL
Article Dans Une Revue Nature Chemical Biology Année : 2012

Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes

Résumé

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.
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Dates et versions

hal-01004114 , version 1 (11-06-2014)

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Stéphane S. Pierre, Alain A. Guillot, Alhosna A. Benjdia, Corine C. Sandstrom, Philippe P. Langella, et al.. Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes. Nature Chemical Biology, 2012, 8 (12), pp.957 - 959. ⟨10.1038/NCHEMBIO.1091⟩. ⟨hal-01004114⟩
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