ArticleProceedings of the National Academy of Sciences of the United States of America2022
Ribosomally derived lipopeptides containing distinct fatty acyl moieties.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Exploring RiPP-derivedRSC chemical biology · 2026Article
- Systems-level genomic and functional characterization of lipopeptide biosurfactant pathways in Bacillus albus MITWPUB5.World journal of microbiology & biotechnology · 2026Article
- Iterative acylation on mature lasso peptides by widespread acetyltransferases.Nature chemical biology · 2026Article
- Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Structure, Biosynthesis, and Bioactivity of Nostolysamides.Biochemistry · 2026Article
- Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Peptide Prenylation Follows Divergent Substrate Engagement Rules.Journal of the American Chemical Society · 2025Article
- Peptide Arginases from Cryptic Pathways Install Ornithine Residues in Uncharacterized Members of Orphan RiPP Families.Chembiochem : a European journal of chemical biology · 2025Article
- Synthetic Linear Lipopeptides and Lipopeptoids Induce Apoptosis and Oxidative Stress: In Vitro Cytotoxicity and SAR Evaluation Against Cancer Cell Lines.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Sterically Controlled C(spOrganic letters · 2025Article
- Glucoselipid Biosurfactant Biosynthesis Operon ofMicroorganisms · 2025Article
- Comparative Analysis of Signature Sequences from Adenylation Domains Situated within Bacterial-Origin Nonribosomal Peptide Synthetase Modules.Journal of microbiology and biotechnology · 2025Article
- Design and Production of Geranylated Cyclic Peptides by the RiPP Enzymes SyncM and PirF.Biomacromolecules · 2025Article
- Salamandamide Lipodipeptides Are Biosynthetic Intermediate Shunt Products of the Nonamodular Nonribosomal Peptide Assembly Lines of the Viscosin Family.Journal of natural products · 2025Article
- Chemical diversity of cyanobacterial natural products.Natural product reports · 2025Review
- Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin.Nature communications · 2024Article
- Biosynthesis of Antimicrobial Ornithine-Containing Lacticin 481 Analogues by Use of a Combinatorial Biosynthetic Pathway inACS synthetic biology · 2024Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopeptides represent a large group of microbial natural products that include important antibacterial and antifungal drugs and some of the most-powerful known biosurfactants. The vast majority of lipopeptides comprise cyclic peptide backbones N-terminally equipped with various fatty acyl moieties. The known compounds of this type are biosynthesized by nonribosomal peptide synthetases, giant enzyme complexes that assemble their products in a non-gene-encoded manner. Here, we report the genome-guided discovery of ribosomally derived, fatty-acylated lipopeptides, termed selidamides. Heterologous reconstitution of three pathways, two from cyanobacteria and one from an arctic, ocean-derived alphaproteobacterium, allowed structural characterization of the probable natural products and suggest that selidamides are widespread over various bacterial phyla. The identified representatives feature cyclic peptide moieties and fatty acyl units attached to (hydroxy)ornithine or lysine side chains by maturases of the GCN5-related
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