ArticleNature chemical biology2025
Plug-and-play engineering of modular polyketide synthases.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Condensation-independent intramodular translocation mechanism of the trans-AT polyketide synthase assembly line.Nature chemical biology · 2026Article
- Evolutionary strategies of late-stage diversification in bacterial biosynthetic gene clusters.Essays in biochemistry · 2026Review
- Unveiling Aziridine-Containing Natural Products by Genomic and Spectroscopic Approaches.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering an Extremely Hybrid PKS for Adipic Acid Production.ACS synthetic biology · 2026Article
- Dissection and Engineering of Modular Polyketide Synthase Extender Unit Specificity Motifs.Chembiochem : a European journal of chemical biology · 2026Article
- Investigation of Domain-Domain Interaction between Acyl Carrier Protein and Thioesterase in Modular Polyketide Synthases.JACS Au · 2026Article
- Genome-Guided Discovery of Antimalarial 4-Amino-2,4-Pentadienoate-Containing Cyclolipodepsipeptides.Angewandte Chemie (International ed. in English) · 2026Article
- Skeletal editing via multi-step engineering of a modular polyketide synthase.Nature communications · 2026Article
- Article
- Engineered strains as living factories: efficient biosynthesis and modification of natural products via synthetic biology and one-pot chemical tandem reactions.Frontiers in microbiology · 2026Review
- Gene conversion-associated successive engineering of modular polyketide synthases.Communications chemistry · 2025Article
- A metabologenomics strategy for rapid discovery of polyketides derived from modular polyketide synthases.Chemical science · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Modular polyketide synthases (PKSs) are multidomain, assembly line enzymes that biosynthesize complex antibiotics such as erythromycin and rapamycin. The modular characteristic of PKSs makes them an ideal platform for the custom production of designer polyketides by combinatorial biosynthesis. However, engineered hybrid PKS pathways often exhibit severe loss of enzyme activity, and a general principle for PKS reprogramming has not been established. Here we present a widely applicable strategy for designing hybrid PKSs. We reveal that two conserved motifs are robust cut sites to connect modules from different PKS pathways and demonstrate the custom production of polyketides with different starter units, extender units and variable reducing states. Furthermore, we expand the applicability of these cut sites to construct hybrid pathways involving cis-AT PKS, trans-AT PKS and even nonribosomal peptide synthetase. Collectively, our findings enable plug-and-play reprogramming of modular PKSs and facilitate the application of assembly line enzymes toward the bioproduction of designer molecules.
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40251436What OpenQuestion holds
Registered trials
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.