ReviewThe Journal of biological chemistry2015
The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine 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 21 papers.
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Who cites it
21 citing papers in PubMed, 57 citations in OpenAlex.
- Analysis of key nodes and metabolic pathways in the protein network of secondary metabolism in Panax quinquefolius L. enhanced by arbuscular mycorrhizal fungi.BMC plant biology · 2026Article
- Transition-metal-catalyzed C-S bond formation: recent developments and pharmaceutical applications.Frontiers in chemistry · 2026Review
- A general copper-catalysed enantioconvergent C(spNature chemistry · 2024Article
- Two Radical SAM Enzymes Are Necessary and Sufficient for the In Vitro Production of the Oxetane Nucleoside Antiviral Agent Albucidin.Angewandte Chemie (International ed. in English) · 2022Article
- ThnL, a B12-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- Visible-Light-Induced, Graphene Oxide-Promoted C3-Chalcogenylation of Indoles Strategy under Transition-Metal-Free Conditions.Molecules (Basel, Switzerland) · 2022Article
- Identification of the key functional genes in salt-stress tolerance of Cyanobacterium3 Biotech · 2021Article
- First Step in Catalysis of the RadicalJournal of the American Chemical Society · 2020Article
- Rapid SERS Detection of Thiol-Containing Natural Products in Culturing Complex.International journal of analytical chemistry · 2020Article
- Article
- X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.Biochemistry · 2018Article
- Into the Wild: Parallel Transcriptomics of the Tsetse-Wigglesworthia Mutualism within Kenyan Populations.Genome biology and evolution · 2017Article
- Structural Insights into Thioether Bond Formation in the Biosynthesis of Sactipeptides.Journal of the American Chemical Society · 2017Article
- On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.Frontiers in chemistry · 2017Review
- Transformations of the FeS Clusters of the Methylthiotransferases MiaB and RimO, Detected by Direct Electrochemistry.Biochemistry · 2016Article
- Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.Nature chemistry · 2016Article
- Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosL.Frontiers in chemistry · 2016Review
- Radical S-adenosylmethionine (SAM) enzymes in cofactor biosynthesis: a treasure trove of complex organic radical rearrangement reactions.The Journal of biological chemistry · 2015Review
- Introduction to the thematic minireview series on radical S-adenosylmethionine (SAM) enzymes.The Journal of biological chemistry · 2015Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfur atoms are present as thiol and thioether functional groups in amino acids, coenzymes, cofactors, and various products of secondary metabolic pathways. The biosynthetic pathways for several sulfur-containing biomolecules require the substitution of sulfur for hydrogen at unreactive aliphatic or electron-rich aromatic carbon atoms. Examples discussed in this review include biotin, lipoic acid, methylthioether modifications found in some nucleic acids and proteins, and thioether cross-links found in peptide natural products. Radical S-adenosyl-L-methionine (SAM) enzymes use an iron-sulfur cluster to catalyze the reduction of SAM to methionine and a highly reactive 5'-deoxyadenosyl radical; this radical can abstract hydrogen atoms at unreactive positions, facilitating the introduction of a variety of functional groups. Radical SAM enzymes that catalyze sulfur insertion reactions contain a second iron-sulfur cluster that facilitates the chemistry, either by donating the cluster's endogenous sulfide or by binding and activating exogenous sulfide or sulfur-containing substrates. The use of radical chemistry involving iron-sulfur clusters is an efficient anaerobic route to the generation of carbon-sulfur bonds in cofactors, secondary metabolites, and other natural products.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.