ArticleJournal of the American Chemical Society2017
Stereospecific Formation of E- and Z-Disubstituted Double Bonds by Dehydratase Domains from Modules 1 and 2 of the Fostriecin Polyketide Synthase.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Stereochemical Dissection of the Strobilurin PKS Reveals the Complex Biosynthetic Logic of Iterative EZE Triene Construction.Angewandte Chemie (International ed. in English) · 2026Article
- Structure and Mechanisms of Assembly-Line Polyketide Synthases.Annual review of biochemistry · 2024Review
- Potassium Chloride as an Effective Alternative to Sodium Chloride in Delaying the Thermal Aggregation of Liquid Whole Egg.Foods (Basel, Switzerland) · 2024Article
- Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain.Beilstein journal of organic chemistry · 2024Article
- Diene incorporation by a dehydratase domain variant in modular polyketide synthases.Nature chemical biology · 2022Article
- Thioesterase-Catalyzed Aminoacylation and Thiolation of Polyketides in Fungi.Journal of the American Chemical Society · 2019Article
- pH-Rate profiles establish that polyketide synthase dehydratase domains utilize a single-base mechanism.Organic & biomolecular chemistry · 2018Article
- Strobilurin biosynthesis in Basidiomycete fungi.Nature communications · 2018Article
- Molecular Basis for Olefin Rearrangement in the Gephyronic Acid Polyketide Synthase.ACS chemical biology · 2018Article
- Stereospecific Formation of Z-Trisubstituted Double Bonds by the Successive Action of Ketoreductase and Dehydratase Domains from trans-AT Polyketide Synthases.Biochemistry · 2018Article
- Structural and Functional Studies of a Pyran Synthase Domain from a trans-Acyltransferase Assembly Line.ACS chemical biology · 2018Article
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3 authors.
Funding
Abstract
The dehydratase domain FosDH1 from module 1 of the fostriecin polyketide synthase (PKS) catalyzed the stereospecific interconversion of (3R)-3-hydroxybutyryl-FosACP1 (5) and (E)-2-butenoyl-FosACP1 (11), as established by a combination of direct LC-MS/MS and chiral GC-MS. FosDH1 did not act on either (3S)-3-hydroxybutyryl-FosACP1 (6) or (Z)-2-butenoyl-FosACP1 (12). FosKR2, the ketoreductase from module 2 of the fostriecin PKS that normally provides the natural substrate for FosDH2, was shown to catalyze the NADPH-dependent stereospecific reduction of 3-ketobutyryl-FosACP2 (23) to (3S)-3-hydroxybutyryl-FosACP2 (8). Consistent with this finding, FosDH2 catalyzed the interconversion of the corresponding triketide substrates (3R,4E)-3-hydroxy-4-hexenoyl-FosACP2 (18) and (2Z,4E)-2,4-hexadienoyl-FosACP2 (21). FosDH2 also catalyzed the stereospecific hydration of (Z)-2-butenoyl-FosACP2 (14) to (3S)-3-hydroxybutyryl-FosACP2 (8). Although incubation of FosDH2 with (3S)-3-hydroxybutyryl-FosACP2 (8) did not result in detectable accumulation of (Z)-2-butenoyl-FosACP2 (14), FosDH2 catalyzed the slow exchange of the 3-hydroxy group of 8 with [
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