title: The mechanisms of radical SAM/cobalamin methylations: an evolving working hypothesis.
abstract: 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⋅.
authors.affiliation: Biomolecular Sciences Research Complex, EastChem School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST, UK.
authors.forename: K K Jason
authors.initials: KK
authors.lastname: Chan
authors.forename: Stephen
authors.initials: S
authors.lastname: Thompson
authors.forename: David
authors.initials: D
authors.lastname: O'Hagan
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology* / Q000378:metabolism; D013883:Thiostrepton / Q000378:metabolism; D014364:Tryptophan / Q000031:analogs & derivatives / Q000378:metabolism*; D014805:Vitamin B 12 / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; C095863:2-methyltryptophan; D012436:S-Adenosylmethionine; D014364:Tryptophan; D008780:Methyltransferases; C063542:tryptophan 2-methyltransferase; D013883:Thiostrepton; D014805:Vitamin B 12