ReviewBiochemistry2017
Radical S-Adenosylmethionine Enzymes Involved in RiPP Biosynthesis.
Review in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- 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
- 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
- Anticancer Ribosomally Synthesized and Post-Translationally Modified Peptides from Plants: Structures, Therapeutic Potential, and Future Directions.Current issues in molecular biology · 2024Review
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Unusual cysteine modifications in natural product biosynthesis.RSC chemical biology · 2024Review
- N-Cα Bond Cleavage Catalyzed by a Multinuclear Iron Oxygenase from a Divergent Methanobactin-like RiPP Gene Cluster.Journal of the American Chemical Society · 2024Article
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Evolutionary Spread of Distinct O-methyltransferases Guides the Discovery of Unique Isoaspartate-Containing Peptides, Pamtides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Benzylic Radical Stabilization Permits Ether Formation During Darobactin Biosynthesis.bioRxiv : the preprint server for biology · 2023Article
- Identification of peptides from honeybee gut symbionts as potential antimicrobial agents against Melissococcus plutonius.Nature communications · 2023Article
- Cytochromes P450 Associated with the Biosyntheses of Ribosomally Synthesized and Post-translationally Modified Peptides.ACS bio & med chem Au · 2023Review
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Sactipeptide Engineering by Probing the Substrate Tolerance of a Thioether-Bond-Forming Sactisynthase.Angewandte Chemie (International ed. in English) · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- RaS-RiPPs in Streptococci and the Human Microbiome.ACS bio & med chem Au · 2022Review
- Radical SAM-dependent ether crosslink in daropeptide biosynthesis.Nature communications · 2022Article
- Diverse Protein Architectures and α-ACS chemical biology · 2022Article
- Pathways of thymidine hypermodification.Nucleic acids research · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) display a diverse range of structures and continue to expand as a natural product class. Accordingly, RiPPs exhibit a wide array of bioactivities, acting as broad and narrow spectrum growth suppressors, antidiabetics, and antinociception and anticancer agents. Because of these properties, and the complex repertoire of post-translational modifications (PTMs) that give rise to these molecules, RiPP biosynthesis has been intensely studied. RiPP biosynthesis often involves enzymes that perform unique chemistry with intriguing reaction mechanisms, which attract chemists and biochemists alike to study and re-engineer these pathways. One particular type of RiPP biosynthetic enzyme is the so-called radical S-adenosylmethionine (rSAM) enzyme, which utilizes radical-based chemistry to install several distinct PTMs. Here, we describe the rSAM enzymes characterized over the past decade that catalyze six reaction types from several RiPP biosynthetic pathways. We present the current state of mechanistic understanding and conclude with possible directions for future characterization of this enzyme family.
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Registered trials
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.