The Mechanisms of Radical SAM/Cobalamin Methylations: An Evolving Working Hypothesis.
Article first published online: 25 MAR 2013
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Volume 14, Issue 6, pages 675–677, April 15, 2013
How to Cite
Chan, K. K. J., Thompson, S. and O'Hagan, D. (2013), The Mechanisms of Radical SAM/Cobalamin Methylations: An Evolving Working Hypothesis. ChemBioChem, 14: 675–677. doi: 10.1002/cbic.201200762
- Issue published online: 8 APR 2013
- Article first published online: 25 MAR 2013
- Manuscript Received: 10 DEC 2012
- cobalamin enzymes;
- enzyme mechanism;
- radical SAM methyltransferase;
- tryptophan methyltransferase
All about Me: Pierre and co-workers have revealed mechanistic details of a tryptophan methyltransferase (TsrM) involved in the biosynthesis of the thiopeptide antibiotic, thiostrepton. Utilising cobalamin and a [4Fe–4S] cluster to generate 2-methyltryptophan from tryptophan, a key difference between this enzyme and other radical SAM methyltransferases is that the reaction is not initiated by a single-electron reduction of SAM to generate 5′-dA⋅.