Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes

Pierre, Stephane; Guillot, Alain; Benjdia, Alhosna; Sandström, Corine; Langella, Philippe; Berteau, Olivier

doi:10.1038/NCHEMBIO.1091

Research article2012Peer reviewed

Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes

Pierre, Stephane; Guillot, Alain; Benjdia, Alhosna; Sandström, Corine; Langella, Philippe; Berteau, Olivier

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

Sandström, Corine
- Department of Molecular Sciences, Swedish University of Agricultural Sciences

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