ReviewThe Journal of biological chemistry2015
SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes.
Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed.
- Mechanistic insight into radicalNatural product reports · 2026Review
- The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Radical SAM Enzyme BlsE Can Operate as a Dehydratase, Dehydrogenase, or Epimerase upon Mutation of a Single Active Site Serine Residue.Journal of the American Chemical Society · 2026Article
- Characterization of C3' Epimerization of the Thioheptose Core in the Biosynthesis of AlbomycinACS catalysis · 2025Article
- The radical SAM enzyme NirJ cleaves off two propionate side chains with the release of acrylate during heme dThe FEBS journal · 2025Article
- RadicalNature catalysis · 2025Article
- Radical SAM Enzyme WprB Catalyzes Uniform Cross-Link Topology between Trp-C5 and Arg-Cγ on the Precursor Peptide.ACS chemical biology · 2025Article
- Mechanistic Insights Into Post-Translational α-Keto-β-Amino Acid Formation by a Radical S-Adenosyl Methionine Peptide Splicease.Angewandte Chemie (International ed. in English) · 2025Article
- Aromatic side-chain crosslinking in RiPP biosynthesis.Nature chemical biology · 2025Review
- Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024Article
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Radical-Mediated Nucleophilic Peptide Cross-Linking in Dynobactin Biosynthesis.Journal of the American Chemical Society · 2024Article
- Fused radical SAM and αKG-HExxH domain proteins contain a distinct structural fold and catalyse cyclophane formation and β-hydroxylation.Nature chemistry · 2024Article
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Genome Mining for New Enzyme Chemistry.ACS catalysis · 2024Review
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- Hydrogen-Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE.ACS central science · 2024Article
- Structural, Biochemical, and Bioinformatic Basis for Identifying Radical SAM Cyclopropyl Synthases.ACS chemical biology · 2024Article
- Benzylic Radical Stabilization Permits Ether Formation During Darobactin Biosynthesis.bioRxiv : the preprint server for biology · 2023Article
- How nature incorporates sulfur and selenium into bioactive natural products.Current opinion in chemical biology · 2023Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate isomerase (TIM) barrel fold with N- and C-terminal extensions that tailor the structure of the enzyme to its specific function. One extension, termed a SPASM domain, binds two auxiliary [4Fe-4S] clusters and is present within peptide-modifying enzymes. The first structure of a SPASM-containing enzyme, anaerobic sulfatase-maturating enzyme (anSME), revealed unexpected similarities to two non-SPASM proteins, butirosin biosynthetic enzyme 2-deoxy-scyllo-inosamine dehydrogenase (BtrN) and molybdenum cofactor biosynthetic enzyme (MoaA). The latter two enzymes bind one auxiliary cluster and exhibit a partial SPASM motif, coined a Twitch domain. Here we review the structure and function of auxiliary cluster domains within the SAM radical enzyme superfamily.
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