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The Mechanisms of Radical SAM/Cobalamin Methylations: An Evolving Working Hypothesis.

Authors

  • K. K. Jason Chan,

    1. Biomolecular Sciences Research Complex, EastChem School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST (UK)
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  • Stephen Thompson,

    1. Biomolecular Sciences Research Complex, EastChem School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST (UK)
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  • Prof. David O'Hagan

    Corresponding author
    1. Biomolecular Sciences Research Complex, EastChem School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST (UK)
    • Biomolecular Sciences Research Complex, EastChem School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST (UK)
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Abstract

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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.

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