ArticleACS chemical biology2014
High divergence of the precursor peptides in combinatorial lanthipeptide biosynthesis.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 67 citations in OpenAlex.
- Structure, Biosynthesis, and Bioactivity of Nostolysamides.Biochemistry · 2026Article
- Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026Article
- Direct Cloning and Heterologous Expression of the Dmxorosin Biosynthetic Gene Cluster fromInternational journal of molecular sciences · 2025Article
- Kinetic Analysis of Cyclization by the Substrate-Tolerant Lanthipeptide Synthetase ProcM.ACS catalysis · 2024Article
- Biosynthesis of Antimicrobial Ornithine-Containing Lacticin 481 Analogues by Use of a Combinatorial Biosynthetic Pathway inACS synthetic biology · 2024Article
- Facile Halogenation of Antimicrobial Peptides As Demonstrated by Producing Bromotryptophan-Labeled Nisin Variants with Enhanced Antimicrobial Activity.Journal of natural products · 2024Article
- Kinetic Analysis of Lanthipeptide Cyclization by Substrate-Tolerant ProcM.bioRxiv : the preprint server for biology · 2024Article
- Uncovering the diversity and distribution of biosynthetic gene clusters of prochlorosins and other putative RiPPs in marineMicrobiology spectrum · 2024Article
- The First Lanthipeptide from Lactobacillus iners, Inecin L, Exerts High Antimicrobial Activity against Human Vaginal Pathogens.Applied and environmental microbiology · 2023Article
- Phylogeny-guided genome mining of roseocin family lantibiotics to generate improved variants of roseocin.AMB Express · 2023Article
- 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
- Structural Analysis of Class I Lanthipeptides fromACS chemical biology · 2021Article
- Pathway information extracted from 25 years of pathway figures.Genome biology · 2020Article
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crossroads of Antibiotic Resistance and Biosynthesis.Journal of molecular biology · 2019Review
- Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale.Nature chemical biology · 2019Article
- Roads to Rome: Role of Multiple Cassettes in Cyanobactin RiPP Biosynthesis.Journal of the American Chemical Society · 2018Article
- RiPP antibiotics: biosynthesis and engineering potential.Current opinion in microbiology · 2018Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Lanthionine-containing peptides (lanthipeptides) are a rapidly growing family of polycyclic peptide natural products belonging to the large class of ribosomally synthesized and post-translationally modified peptides (RiPPs). These compounds are widely distributed in taxonomically distant species, and their biosynthetic systems and biological activities are diverse. A unique example of lanthipeptide biosynthesis is the prochlorosin synthetase ProcM from the marine cyanobacterium Prochlorococcus MIT9313, which transforms up to 29 different precursor peptides (ProcAs) into a library of lanthipeptides called prochlorosins (Pcns) with highly diverse sequences and ring topologies. Here, we show that many ProcM-like enzymes from a variety of bacteria have the capacity to carry out post-translational modifications on highly diverse precursor peptides, providing new examples of natural combinatorial biosynthesis. We also demonstrate that the leader peptides come from different evolutionary origins, suggesting that the combinatorial biosynthesis is tied to the enzyme and not a specific type of leader peptide. For some precursor peptides encoded in the genomes, the leader peptides apparently have been truncated at the N-termini, and we show that these N-terminally truncated peptides are still substrates of the enzymes. Consistent with this hypothesis, we demonstrate that about two-thirds of the ProcA N-terminal sequence is not essential for ProcM activity. Our results also highlight the potential of exploring this class of natural products by genome mining and bioengineering.
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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.