ArticleBiochemistry2016
Biochemical and Spectroscopic Characterization of a Radical S-Adenosyl-L-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link.
Article in Biochemistry, 2016. 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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Who cites it
40 citing papers in PubMed, 61 citations in OpenAlex.
- AApplied and environmental microbiology · 2026Article
- RadicalJournal of the American Chemical Society · 2026Article
- Structural, Biochemical, and Bioinformatic Basis for Identifying Radical SAM Cyclopropyl Synthases.ACS chemical biology · 2024Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Bioinformatic mining for RiPP biosynthetic gene clusters in Bacteroidales reveals possible new subfamily architectures and novel natural products.Frontiers in microbiology · 2023Article
- Characterization of a Radical SAM Oxygenase for the Ether Crosslinking in Darobactin Biosynthesis.Journal of the American Chemical Society · 2022Article
- Leveraging Substrate Promiscuity of a RadicalACS central science · 2022Article
- Identification of a poly-cyclopropylglycine-containing peptide via bioinformatic mapping of radical S-adenosylmethionine enzymes.The Journal of biological chemistry · 2022Article
- How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery.ACS bio & med chem Au · 2022Review
- Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy.Applied magnetic resonance · 2022Review
- New Role for Radical SAM Enzymes in the Biosynthesis of Thio(seleno)oxazole RiPP Natural Products.Biochemistry · 2021Article
- Current Advancements in Sactipeptide Natural Products.Frontiers in chemistry · 2021Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Radical SAM Enzymes and Ribosomally-Synthesized and Post-translationally Modified Peptides: A Growing Importance in the Microbiomes.Frontiers in chemistry · 2021Review
- Post-translational formation of strained cyclophanes in bacteria.Nature chemistry · 2020Article
- The unusual structure of Ruminococcin C1 antimicrobial peptide confers clinical properties.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Two antimicrobial genes from Aegilops tauschii Cosson identified by the Bacillus subtilis expression system.Scientific reports · 2020Article
- Article
- Electron Paramagnetic Resonance Spectroscopic Identification of the Fe-S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE.Biochemistry · 2019Article
- Reconstitution and Substrate Specificity of the Thioether-Forming RadicalACS chemical biology · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Peptide-derived natural products are a class of metabolites that afford the producing organism a selective advantage over other organisms in their biological niche. While the polypeptide antibiotics produced by the nonribosomal polypeptide synthetases (NRPS) are the most widely recognized, the ribosomally synthesized and post-translationally modified peptides (RiPPs) are an emerging group of natural products with diverse structures and biological functions. Both the NRPS derived peptides and the RiPPs undergo extensive post-translational modifications to produce structural diversity. Here we report the first characterization of the six cysteines in forty-five (SCIFF) [Haft, D. H. and Basu M. K. (2011) J. Bacteriol. 193, 2745-2755] peptide maturase Tte1186, which is a member of the radical S-adenosyl-l-methionine (SAM) superfamily. Tte1186 catalyzes the formation of a thioether cross-link in the peptide Tte1186a encoded by an orf located upstream of the maturase, under reducing conditions in the presence of SAM. Tte1186 contains three [4Fe-4S] clusters that are indispensable for thioether cross-link formation; however, only one cluster catalyzes the reductive cleavage of SAM. Mechanistic imperatives for the reaction catalyzed by the thioether forming radical SAM maturases will be discussed.
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