ArticleJournal of the American Chemical Society2014
Mechanistic studies on the substrate-tolerant lanthipeptide synthetase ProcM.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 70 citations in OpenAlex.
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- Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Lactic Acid Bacteria Bacteriocins: Safe and Effective Antimicrobial Agents.International journal of molecular sciences · 2025Review
- Kinetic Analysis of Cyclization by the Substrate-Tolerant Lanthipeptide Synthetase ProcM.ACS catalysis · 2024Article
- Heterologous biosynthesis of myxobacterial lanthipeptides melittapeptins.Applied microbiology and biotechnology · 2024Article
- Radical-Mediated Nucleophilic Peptide Cross-Linking in Dynobactin Biosynthesis.Journal of the American Chemical Society · 2024Article
- Exploring the roles of ribosomal peptides in prokaryote-phage interactions through deep learning-enabled metagenome mining.Microbiome · 2024Article
- Kinetic Analysis of Lanthipeptide Cyclization by Substrate-Tolerant ProcM.bioRxiv : the preprint server for biology · 2024Article
- Sequence controlled secondary structure is important for the site-selectivity of lanthipeptide cyclization.Chemical science · 2023Article
- Total Synthesis and Structure Assignment of the Relacidine Lipopeptide Antibiotics and Preparation of Analogues with Enhanced Stability.ACS infectious diseases · 2023Article
- Phylogeny-guided genome mining of roseocin family lantibiotics to generate improved variants of roseocin.AMB Express · 2023Article
- A Silent Biosynthetic Gene Cluster from a Methanotrophic Bacterium Potentiates Discovery of a Substrate Promiscuous Proteusin Cyclodehydratase.ACS chemical biology · 2022Article
- Ribosomally derived lipopeptides containing distinct fatty acyl moieties.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Substrate Sequence Controls Regioselectivity of Lanthionine Formation by ProcM.Journal of the American Chemical Society · 2021Article
- Functional Expression and Characterization of the Highly Promiscuous Lanthipeptide Synthetase SyncM, Enabling the Production of Lanthipeptides with a Broad Range of Ring Topologies.ACS synthetic biology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Challenges and advances in genome mining of ribosomally synthesized and post-translationally modified peptides (RiPPs).Synthetic and systems biotechnology · 2020Review
- Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.Chemical science · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Lanthipeptides are a class of post-translationally modified peptide natural products. They contain lanthionine (Lan) and methyllanthionine (MeLan) residues, which generate cross-links and endow the peptides with various biological activities. The mechanism of a highly substrate-tolerant lanthipeptide synthetase, ProcM, was investigated herein. We report a hybrid ligation strategy to prepare a series of substrate analogues designed to address a number of mechanistic questions regarding catalysis by ProcM. The method utilizes expressed protein ligation to generate a C-terminal thioester of the leader peptide of ProcA, the substrate of ProcM. This thioester was ligated with a cysteine derivative that resulted in an alkyne at the C-terminus of the leader peptide. This alkyne in turn was used to conjugate the leader peptides to a variety of synthetic peptides by copper-catalyzed azide-alkyne cycloaddition. Using deuterium-labeled Ser and Thr in the substrate analogues thus prepared, dehydration by ProcM was established to occur from C-to-N-terminus for two different substrates. Cyclization also occurred with a specific order, which depended on the sequence of the substrate peptides. Furthermore, using orthogonal cysteine side-chain protection in the two semisynthetic peptide substrates, we were able to rule out spontaneous non-enzymatic cyclization events to explain the very high substrate tolerance of ProcM. Finally, the enzyme was capable of exchanging protons at the α-carbon of MeLan, suggesting that ring formation could be reversible. These findings are discussed in the context of the mechanism of the substrate-tolerant ProcM, which may aid future efforts in lanthipeptide engineering.
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