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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.

Published in

Nature Chemical Biology
2012, volume: 8, number: 12, pages: 957-959
Publisher: NATURE PUBLISHING GROUP

SLU Authors

UKÄ Subject classification

Organic Chemistry

Publication identifier

  • DOI: https://doi.org/10.1038/NCHEMBIO.1091

Permanent link to this page (URI)

https://res.slu.se/id/publ/41971