ArticleAngewandte Chemie (International ed. in English)2020
An Amphipathic Alpha-Helix Guides Maturation of the Ribosomally-Synthesized Lipolanthines.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- Catalytic architecture and cyclase-mediated dimerization of a newly identified class III-c lanthipeptide synthetase.Protein science : a publication of the Protein Society · 2026Article
- Heterologous expression reveals a cryptic morphogenetic lanthipeptide durhapeptin from Streptomyces durhamensis.Antonie van Leeuwenhoek · 2026Article
- Design and Production of Geranylated Cyclic Peptides by the RiPP Enzymes SyncM and PirF.Biomacromolecules · 2025Article
- Mechanistic insights into lanthipeptide modification by a distinct subclass of LanKC enzyme that forms dimers.Nature communications · 2024Article
- Non-modular fatty acid synthases yield distinct N-terminal acylation in ribosomal peptides.Nature chemistry · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Disordered regions in proteusin peptides guide post-translational modification by a flavin-dependent RiPP brominase.Nature communications · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Heterologous Production and Structure Determination of a New Lanthipeptide Sinosporapeptin Using a Cryptic Gene Cluster in an Actinobacterium Sinosporangium siamense.Journal of microbiology (Seoul, Korea) · 2023Article
- Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks.Nature communications · 2023Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Recent Advances in Discovery, Bioengineering, and Bioactivity-Evaluation of Ribosomally Synthesized and Post-translationally Modified Peptides.ACS bio & med chem Au · 2023Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.Angewandte Chemie (International ed. in English) · 2022Article
- Correlational networking guides the discovery of unclustered lanthipeptide protease-encoding genes.Nature communications · 2022Article
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.Chembiochem : a European journal of chemical biology · 2021Article
- Aminovinyl Cysteine Containing Peptides: A Unique Motif That Imparts Key Biological Activity.JACS Au · 2021Review
- Engineering of new-to-nature ribosomally synthesized and post-translationally modified peptide natural products.Current opinion in biotechnology · 2021Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently discovered strongly anti-Gram-positive lipolanthines represent a new group of lipidated, ribosomally synthesized and post-translationally modified peptides (RiPPs). They are bicyclic octapeptides with a central quaternary carbon atom (avionin), which is installed through the cooperative action of the class-III lanthipeptide synthetase MicKC and the cysteine decarboxylase MicD. Genome mining efforts indicate a widespread distribution and unprecedented biosynthetic diversity of lipolanthine gene clusters, combining elements of RiPPs, polyketide and non-ribosomal peptide biosynthesis. Utilizing NMR spectroscopy, we show that a (θxx)θxxθxxθ (θ=L, I, V, M or T) motif, which is conserved in the leader peptides of all class-III and -IV lanthipeptides, forms an amphipathic α-helix in MicA that destines the peptide substrate for enzymatic processing. Our results provide general rules of substrate recruitment and enzymatic regulation during lipolanthine maturation. These insights will facilitate future efforts to rationally design new lanthipeptide scaffolds with antibacterial potency.
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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.