ArticleNature communications2022
A ribosomally synthesised and post-translationally modified peptide containing a β-enamino acid and a macrocyclic motif.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Bacillus-derived antimicrobial peptides as alternatives to antibiotics in poultry: mechanisms, applications, and future prospects- a review.Archives of microbiology · 2026Review
- RadicalJournal of the American Chemical Society · 2026Article
- Pseudokinases can catalyse peptide cyclization through thioether crosslinking.Nature chemistry · 2026Article
- Advanced applications of synthetic biology technology in biosynthesis of bioactive compounds from medicinal plants.Chinese herbal medicines · 2026Review
- Exometabolite-Based Antimicrobial Formulations from Lactic Acid Bacteria as a Multi-Target Strategy Against Multidrug-ResistantAntibiotics (Basel, Switzerland) · 2025Article
- Harnessing Actinobacteria secondary metabolites for tuberculosis drug discovery: Historical trends, current status and future outlooks.Natural products and bioprospecting · 2025Review
- A Unique Class of Cyclases with a Kinase Fold Catalyzes Enethiol-Mediated Macrocyclization of Aminovinyl-Cysteine Motifs in Lanthipeptides.ACS central science · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Article
- Metagenomic study of lake microbial mats reveals protease-inhibiting antiviral peptides from a core microbiome member.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cell-free biosynthesis and engineering of ribosomally synthesized lanthipeptides.Nature communications · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Dehydroamino acid residues in bioactive natural products.Natural product reports · 2024Review
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Global Map of Specialized Metabolites Encoded in Prokaryotic Plasmids.Microbiology spectrum · 2023Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Improved production of class I lanthipeptides inChemical science · 2023Article
- Cytochromes P450 involved in bacterial RiPP biosyntheses.Journal of industrial microbiology & biotechnology · 2023Review
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Authors and funding
14 authors at 5 institutions in 4 countries.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are structurally complex natural products with diverse bioactivities. Here we report discovery of a RiPP, kintamdin, for which the structure is determined through spectroscopy, spectrometry and genomic analysis to feature a bis-thioether macrocyclic ring and a β-enamino acid residue. Biosynthetic investigation demonstrated that its pathway relies on four dedicated proteins: phosphotransferase KinD, Lyase KinC, kinase homolog KinH and flavoprotein KinI, which share low homologues to enzymes known in other RiPP biosynthesis. During the posttranslational modifications, KinCD is responsible for the formation of the characteristic dehydroamino acid residues including the β-enamino acid residue, followed by oxidative decarboxylation on the C-terminal Cys and subsequent cyclization to provide the bis-thioether ring moiety mediated by coordinated action of KinH and KinI. Finally, conserved genomic investigation allows further identification of two kintamdin-like peptides among the kin-like BGCs, suggesting the occurrence of RiPPs from actinobacteria.
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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.