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The Mechanisms of Radical SAM/Cobalamin Methylations: An Evolving Working Hypothesis.
Author(s) -
Chan K. K. Jason,
Thompson Stephen,
O'Hagan David
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200762
Subject(s) - thiostrepton , cobalamin , methyltransferase , tryptophan , chemistry , biochemistry , enzyme , stereochemistry , methylation , amino acid , rna , ribosome , vitamin b12 , gene
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 ⋅ .