ArticleNature chemical biology2024
Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Insights into the stereochemical mechanism of the BCommunications biology · 2026Article
- 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
- 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
- Leader-Independent C‑Terminal Modification by a RadicalACS bio & med chem Au · 2025Article
- Characterization of C3' Epimerization of the Thioheptose Core in the Biosynthesis of AlbomycinACS catalysis · 2025Article
- Multicolumn Two-Dimensional Liquid Chromatography Screening Platform for Stereopeptidomics and Application to Antimicrobial Peptide Polyene and Lipopeptide.Analytical chemistry · 2025Article
- Direct Detection of the α-Carbon Radical Intermediate Formed by OspD: Mechanistic Insights into RadicalJournal of the American Chemical Society · 2024Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
D-Amino acid residues, found in countless peptides and natural products including ribosomally synthesized and post-translationally modified peptides (RiPPs), are critical for the bioactivity of several antibiotics and toxins. Recently, radical S-adenosyl-L-methionine (SAM) enzymes have emerged as the only biocatalysts capable of installing direct and irreversible epimerization in RiPPs. However, the mechanism underpinning this biochemical process is ill-understood and the structural basis for this post-translational modification remains unknown. Here we report an atomic-resolution crystal structure of a RiPP-modifying radical SAM enzyme in complex with its substrate properly positioned in the active site. Crystallographic snapshots, size-exclusion chromatography-small-angle x-ray scattering, electron paramagnetic resonance spectroscopy and biochemical analyses reveal how epimerizations are installed in RiPPs and support an unprecedented enzyme mechanism for peptide epimerization. Collectively, our study brings unique perspectives on how radical SAM enzymes interact with RiPPs and catalyze post-translational modifications in 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.