ArticleNature chemical biology2018
Substrate-assisted enzymatic formation of lysinoalanine in duramycin.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
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- Pseudokinases can catalyse peptide cyclization through thioether crosslinking.Nature chemistry · 2026Article
- Inhibitors of Lysinoalanine Cross-Linking in the Flagella Hook as Antimicrobials against Spirochetes.ACS chemical biology · 2025Article
- Enabling Access to Novel Bacterial Biosynthetic Potential From ONT Draft Genomic Data.Microbial biotechnology · 2025Article
- Empowering canonical biochemicals with cross-linked novelty: Recursions in applications of protein cross-links.Proteins · 2025Review
- Genome Mining ofMicroorganisms · 2024Article
- De novo design of diverse small molecule binders and sensors using Shape Complementary Pseudocycles.bioRxiv : the preprint server for biology · 2023Article
- Lysinoalanine cross-linking is a conserved post-translational modification in the spirochete flagellar hook.PNAS nexus · 2023Article
- AlphaFold Accurately Predicts the Structure of Ribosomally Synthesized and Post-Translationally Modified Peptide Biosynthetic Enzymes.Biomolecules · 2023Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Development of Duramycin-Based Molecular Probes for Cell Death Imaging.Molecular imaging and biology · 2022Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Dehydroamino acid chemical biology: an example of functional group interconversion on proteins.RSC chemical biology · 2020Article
- Characterization of a Dehydratase and Methyltransferase in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides in Lachnospiraceae.Chembiochem : a European journal of chemical biology · 2020Article
- A subfamily roadmap of the evolutionarily diverse glycoside hydrolase family 16 (GH16).The Journal of biological chemistry · 2019Article
- Structure and chemistry of lysinoalanine crosslinking in the spirochaete flagella hook.Nature chemical biology · 2019Article
- Genomic analysis of siderophore β-hydroxylases reveals divergent stereocontrol and expands the condensation domain family.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dehydroamino acids: chemical multi-tools for late-stage diversification.Organic & biomolecular chemistry · 2019Review
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6 authors at 2 institutions in 2 countries.
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Abstract
Duramycin is a heavily post-translationally modified peptide that binds phosphatidylethanolamine. It has been investigated as an antibiotic, an inhibitor of viral entry, a therapeutic for cystic fibrosis, and a tumor and vasculature imaging agent. Duramycin contains a β-hydroxylated Asp (Hya) and four macrocycles, including an essential lysinoalanine (Lal) cross-link. The mechanism of Lal formation is not known. Here we show that Lal is installed stereospecifically by DurN via addition of Lys19 to a dehydroalanine. The structure of DurN reveals an unusual dimer with a new fold. Surprisingly, in the structure of duramycin bound to DurN, no residues of the enzyme are near the Lal cross-link. Instead, Hya15 of the substrate makes interactions with Lal, suggesting it acts as a base to deprotonate Lys19 during catalysis. Biochemical data suggest that DurN preorganizes the reactive conformation of the substrate, such that the Hya15 of the substrate can serve as the catalytic base for Lal formation.
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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.