ArticleJournal of the American Chemical Society2021
Substrate Sequence Controls Regioselectivity of Lanthionine Formation by ProcM.
Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Cyclic Peptides as Modulators of Protein-Protein Interactions: A Survival Guide from Discovery Platforms to AI-Driven Design.International journal of molecular sciences · 2026Review
- Structure, Biosynthesis, and Bioactivity of Nostolysamides.Biochemistry · 2026Article
- Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026Article
- An Unusual Ring Pattern in the Rosβ Lanthipeptide of the Two-Component Lantibiotic Roseocin.Journal of natural products · 2026Article
- Computational structure prediction of lanthipeptides with NMR data reveals underappreciated peptide flexibility.Protein science : a publication of the Protein Society · 2025Article
- Substrate prediction for RiPP biosynthetic enzymesDigital discovery · 2025Article
- Kinetic Analysis of Cyclization by the Substrate-Tolerant Lanthipeptide Synthetase ProcM.ACS catalysis · 2024Article
- Use of a head-to-tail peptide cyclase to prepare hybrid RiPPs.Chemical communications (Cambridge, England) · 2024Article
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Kinetic Analysis of Lanthipeptide Cyclization by Substrate-Tolerant ProcM.bioRxiv : the preprint server for biology · 2024Article
- Substrate Prediction for RiPP Biosynthetic Enzymes via Masked Language Modeling and Transfer Learning.ArXiv · 2024Article
- The Minimum Protein Staple? - Towards 'bio'-Baldwin's rulesChemical science · 2024Article
- Benzylic Radical Stabilization Permits Ether Formation During Darobactin Biosynthesis.bioRxiv : the preprint server for biology · 2023Article
- Deep Learning-Driven Library Design for theACS central science · 2023Article
- Sequence controlled secondary structure is important for the site-selectivity of lanthipeptide cyclization.Chemical science · 2023Article
- Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks.Nature communications · 2023Article
- Article
- Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM.ACS synthetic biology · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Class V Lanthipeptide Cyclase Directs the Biosynthesis of a Stapled Peptide Natural Product.Journal of the American Chemical Society · 2022Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Lanthipeptides belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs). The (methyl)lanthionine cross-links characteristic to lanthipeptides are essential for their stability and bioactivities. In most bacteria, lanthipeptides are maturated from single precursor peptides encoded in the corresponding biosynthetic gene clusters. However, cyanobacteria engage in combinatorial biosynthesis and encode as many as 80 substrate peptides with highly diverse sequences that are modified by a single lanthionine synthetase into lanthipeptides of different lengths and ring patterns. It is puzzling how a single enzyme could exert control over the cyclization processes of such a wide range of substrates. Here, we used a library of ProcA3.3 precursor peptide variants and show that it is not the enzyme ProcM but rather its substrate sequences that determine the regioselectivity of lanthionine formation. We also demonstrate the utility of trapped ion mobility spectrometry-tandem mass spectrometry (TIMS-MS/MS) as a fast and convenient method to efficiently separate lanthipeptide constitutional isomers, particularly in cases where the isomers cannot be resolved by conventional liquid chromatography. Our data allowed identification of factors that are important for the cyclization outcome, but also showed that there are no easily identifiable predictive rules for all sequences. Our findings provide a platform for future deep learning approaches to allow such prediction of ring patterns of products of combinatorial biosynthesis.
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Registered trials
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