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

Chan K. K. Jason | Zendy; Thompson Stephen | Zendy; O'Hagan David | Zendy

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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 ⋅ .

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