ArticleNature chemical biology2021
Structural basis for non-radical catalysis by TsrM, a radical SAM methylase.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 62 citations in OpenAlex.
- Toward understanding the catalytic mechanism for two classes of bacterial phospholipid N-methyltransferases.The FEBS journal · 2026Article
- Copper(II/III) Redox Couple Enables C─H Methylation via a Radical Mechanism Analogous to SAM Enzymes.Angewandte Chemie (International ed. in English) · 2026Article
- Mechanistic insight into radicalNatural product reports · 2026Review
- S-Adenosyl-d-Methionine as a Non-Physiological Substrate for a Wide Range of SAM-Dependent Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- The Expanding Reactivity of Cobamide-Containing Proteins: From Mechanistic Understanding to Non-native Biocatalysis.ACS catalysis · 2026Article
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026Article
- The cobalamin-binding domain of cobalamin-dependent radical S-adenosylmethionine enzymes: Familiarity in unfamiliar places.Journal of inorganic biochemistry · 2026Review
- Novel chemistry and structural perspectives in vitamin BChemical science · 2026Review
- Structural basis for iterative methylation by a cobalamin-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026Article
- The Biosynthetic Pathway to the Pyrroloiminoquinone Marine Natural Product Ammosamide C.Journal of the American Chemical Society · 2025Article
- Structural Basis for Iterative Methylation by a Cobalamin-dependent Radical S-Adenosylmethionine Enzyme in Cystobactamids Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Radical Fluoromethylation Enabled by Cobalamin-Dependent Radical SAM Enzymes.ACS bio & med chem Au · 2025Article
- Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024Article
- S-adenosyl-L-methionine is the unexpected methyl donor for the methylation of mercury by the membrane-associated HgcAB complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Substrate Specificity of a Methyltransferase Involved in the Biosynthesis of the Lantibiotic Cacaoidin.Biochemistry · 2024Article
- A modular and synthetic biosynthesis platform for de novo production of diverse halogenated tryptophan-derived molecules.Nature communications · 2024Article
- Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry.Beilstein journal of organic chemistry · 2024Review
- Changing Fates of the Substrate Radicals Generated in the Active Sites of the BJournal of the American Chemical Society · 2023Article
- Twenty Years of Radical SAM! The Genesis of the Superfamily.ACS bio & med chem Au · 2022Article
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Authors and funding
9 authors at 5 institutions in 1 country.
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Abstract
Tryptophan 2C methyltransferase (TsrM) methylates C2 of the indole ring of L-tryptophan during biosynthesis of the quinaldic acid moiety of thiostrepton. TsrM is annotated as a cobalamin-dependent radical S-adenosylmethionine (SAM) methylase; however, TsrM does not reductively cleave SAM to the universal 5'-deoxyadenosyl 5'-radical intermediate, a hallmark of radical SAM (RS) enzymes. Herein, we report structures of TsrM from Kitasatospora setae, which are the first structures of a cobalamin-dependent radical SAM methylase. Unexpectedly, the structures show an essential arginine residue that resides in the proximal coordination sphere of the cobalamin cofactor, and a [4Fe-4S] cluster that is ligated by a glutamyl residue and three cysteines in a canonical CXXXCXXC RS motif. Structures in the presence of substrates suggest a substrate-assisted mechanism of catalysis, wherein the carboxylate group of SAM serves as a general base to deprotonate N1 of the tryptophan substrate, facilitating the formation of a C2 carbanion.
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