ArticleNature chemical biology2020
Pass-back chain extension expands multimodular assembly line biosynthesis.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- The Potential of Non-Ribosomal Peptide Engineering for Creating New Antimicrobial Complexes.Molecules (Basel, Switzerland) · 2026Review
- Controlling Megasynthetase Module-Module Interactions through β-Hairpin Docking Domain Engineering.ACS chemical biology · 2025Article
- Tandem ketone reduction in pepstatin biosynthesis reveals an FNature communications · 2025Article
- Integrated genome and metabolome mining unveiled structure and biosynthesis of novel lipopeptides from a deep-sea Rhodococcus.Microbial biotechnology · 2024Article
- Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases.Marine drugs · 2024Review
- Unveiling a CAAX Protease-Like Protein Involved in Didemnin Drug Maturation and Secretion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Heterologous overproduction of oviedomycin by refactoring biosynthetic gene cluster and metabolic engineering of host strain Streptomyces coelicolor.Microbial cell factories · 2023Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- CRISPR/Cas9-assisted ssDNA recombineering for site-directed mutagenesis and saturation mutagenesis of plasmid-encoded genes.Biotechnology letters · 2023Article
- Biosynthesis of Antifungal Solanimycin May Involve an Iterative Nonribosomal Peptide Synthetase Module.ACS chemical biology · 2023Article
- The modular pYT vector series employed for chromosomal gene integration and expression to produce carbazoles and glycolipids inFEMS microbes · 2023Article
- Unexpected assembly machinery for 4(3H)-quinazolinone scaffold synthesis.Nature communications · 2022Article
- Chemometrics and genome mining reveal an unprecedented family of sugar acid-containing fungal nonribosomal cyclodepsipeptides.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Halovirs I-K, antibacterial and cytotoxic lipopeptaibols from the plant pathogenic fungus Paramyrothecium roridum NRRL 2183.The Journal of antibiotics · 2022Article
- Genome mining methods to discover bioactive natural products.Natural product reports · 2021Review
- A thorough analysis and categorization of bacterial interrupted adenylation domains, including previously unidentified families.RSC chemical biology · 2020Article
- Synthetic biology enabling access to designer polyketides.Current opinion in chemical biology · 2020Review
- Fungal siderophore biosynthesis catalysed by an iterative nonribosomal peptide synthetase.Chemical science · 2020Article
- Site-Directed Mutagenesis of Large Biosynthetic Gene ClustersACS synthetic biology · 2020Article
- Nonlinear Biosynthetic Assembly of Alpiniamide by a HybridACS chemical biology · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Modular nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) enzymatic assembly lines are large and dynamic protein machines that generally effect a linear sequence of catalytic cycles. Here, we report the heterologous reconstitution and comprehensive characterization of two hybrid NRPS-PKS assembly lines that defy many standard rules of assembly line biosynthesis to generate a large combinatorial library of cyclic lipodepsipeptide protease inhibitors called thalassospiramides. We generate a series of precise domain-inactivating mutations in thalassospiramide assembly lines, and present evidence for an unprecedented biosynthetic model that invokes intermodule substrate activation and tailoring, module skipping and pass-back chain extension, whereby the ability to pass the growing chain back to a preceding module is flexible and substrate driven. Expanding bidirectional intermodule domain interactions could represent a viable mechanism for generating chemical diversity without increasing the size of biosynthetic assembly lines and challenges our understanding of the potential elasticity of multimodular megaenzymes.
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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.