ArticleJournal of the American Chemical Society2018
Investigation of Substrate Recognition and Biosynthesis in Class IV Lanthipeptide Systems.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Hybrid genome assembly and comprehensive genomic analysis of Lactiplantibacillus pentosus LP309 reveal its probiotic and technological potential.BMC genomics · 2026Article
- Characterization of six bioactive compounds from two soil-derivedResearch in pharmaceutical sciences · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Direct Cloning and Heterologous Expression of the Dmxorosin Biosynthetic Gene Cluster fromInternational journal of molecular sciences · 2025Article
- Genome mining of Lactiplantibacillus plantarum PA21: insights into its antimicrobial potential.BMC genomics · 2024Article
- The untapped potential of actinobacterial lanthipeptides as therapeutic agents.Molecular biology reports · 2023Review
- Core-dependent post-translational modifications guide the biosynthesis of a new class of hypermodified peptides.Nature communications · 2023Article
- Article
- Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks.Nature communications · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Bioinformatic prediction and experimental validation of RiPP recognition elements.Methods in enzymology · 2023Article
- Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.Angewandte Chemie (International ed. in English) · 2022Article
- Unexpected Methyllanthionine Stereochemistry in the Morphogenetic Lanthipeptide SapT.Journal of the American Chemical Society · 2022Article
- Article
- Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.Chembiochem : a European journal of chemical biology · 2021Article
- Semisynthetic Macrocyclic Lipo-lanthipeptides Display Antimicrobial Activity Against Bacterial Pathogens.ACS synthetic biology · 2021Article
- Exploring structural signatures of the lanthipeptide prochlorosin 2.8 using tandem mass spectrometry and trapped ion mobility-mass spectrometry.Analytical and bioanalytical chemistry · 2021Article
- Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.Applied and environmental microbiology · 2021Review
- Synthetic biology approaches to actinomycete strain improvement.FEMS microbiology letters · 2021Review
- Review
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Authors and funding
2 authors.
Funding
Abstract
Lanthipeptides belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs) and are subdivided into four classes. The first two classes have been heavily studied, but less is known about classes III and IV. The lanthipeptide synthetases of classes III and IV share a similar organization of protein domains: A lyase domain at the N-terminus, a central kinase domain, and a C-terminal cyclase domain. Here, we provide deeper insight into class IV enzymes (LanLs). A series of putative producer strains was screened to identify production conditions of four new venezuelin-like lanthipeptides, and an Escherichia coli based heterologous production system was established for a fifth. The latter not only allowed production of fully modified core peptide but was also employed as the basis for mutational analysis of the precursor peptide to identify regions important for enzyme recognition. These experiments were complemented by in vitro binding studies aimed at identifying the region of the leader peptide recognized by the LanL enzymes as well as determining which domain of the enzyme is recognizing the substrate peptide. Combined, these studies revealed that the kinase domain is mediating the interaction with the precursor peptide and that a putatively α-helical stretch of residues at the center to N-terminal region of the leader peptide is important for enzyme recognition. In addition, a combination of in vitro assays and tandem mass spectrometry was used to elucidate the order of dehydration events in these systems.
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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.