ArticleNature chemical biology2022
Diene incorporation by a dehydratase domain variant in modular polyketide synthases.
Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular basis for depsipeptide HDAC inhibitor combinatorial biosynthesis.Nature communications · 2026Article
- Stereochemical Dissection of the Strobilurin PKS Reveals the Complex Biosynthetic Logic of Iterative EZE Triene Construction.Angewandte Chemie (International ed. in English) · 2026Article
- Biosurfactant biosynthesis by Alcanivorax borkumensis and its role in oil biodegradation.Nature chemical biology · 2025Article
- The Discovery of Weddellamycin, a Tricyclic Polyene Macrolactam Antibiotic from an Antarctic Deep-Sea-DerivedMarine drugs · 2024Article
- Antibiotic Skeletal Diversification via Differential Enoylreductase Recruitment and Module Iteration inJournal of the American Chemical Society · 2024Article
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Authors and funding
7 authors at 3 institutions in 5 countries.
Funding
Abstract
Modular polyketide synthases (PKSs) are biosynthetic assembly lines that construct structurally diverse natural products with wide-ranging applications in medicine and agriculture. Various mechanisms contribute to structural diversification during PKS-mediated chain assembly, including dehydratase (DH) domain-mediated elimination of water from R and S-configured 3-hydroxy-thioesters to introduce E- and Z-configured carbon-carbon double bonds, respectively. Here we report the discovery of a DH domain variant that catalyzes the sequential elimination of two molecules of water from a (3R, 5S)-3,5-dihydroxy thioester during polyketide chain assembly, introducing a conjugated E,Z-diene into various modular PKS products. We show that the reaction proceeds via a (2E, 5S)-2-enoyl-5-hydroxy-thioester intermediate and involves an additional universally conserved histidine residue that is absent from the active site of most conventional DH domains. These findings expand the diverse range of chemistries mediated by DH-like domains in modular PKSs, highlighting the catalytic versatility of the double hotdog fold.
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Registered trials
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