ArticleOrganic & biomolecular chemistry2018
pH-Rate profiles establish that polyketide synthase dehydratase domains utilize a single-base mechanism.
Article in Organic & biomolecular chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Stereochemical Dissection of the Strobilurin PKS Reveals the Complex Biosynthetic Logic of Iterative EZE Triene Construction.Angewandte Chemie (International ed. in English) · 2026Article
- Information-Rich, Dual-FunctionJournal of the American Chemical Society · 2023Article
- Diene incorporation by a dehydratase domain variant in modular polyketide synthases.Nature chemical biology · 2022Article
- AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis.Nature communications · 2022Article
- HowACS chemical biology · 2021Article
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- Structural insights into dehydratase substrate selection for the borrelidin and fluvirucin polyketide synthases.Journal of industrial microbiology & biotechnology · 2019Article
- Structural and dynamical rationale for fatty acid unsaturation inProceedings of the National Academy of Sciences of the United States of America · 2019Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
FosDH1 from module 1 of the fostriecin polyketide synthase (PKS) catalyzes the dehydration of a 3-hydroxybutyryl-SACP to the (E)-3-butenoyl-SACP. The steady-state kinetic parameters, kcat and kcat/Km, were determined over the pH range 3.0 to 9.2 for the FosDH1-catalyzed dehydration of the N-acetycsteamine thioester, 3-hydroxybutyryl-SNAC (3), to (E)-3-butenoyl-SNAC (4). The pH rate profiles for both log(kcat) and log(kcat/Km) each corresponded to a single pH-dependent ionization to give an active site general base, with a calculated pKa 6.1 ± 0.2 for kcat and pKa 5.7 ± 0.1 for kcat/Km. These results are inconsistent with the commonly suggested "two-base" (base-acid) mechanism for the dehydratases of PKS and fatty acid biosynthesis and support a simple one-base mechanism in which the universally conserved active site His residue acts as the base to deprotonate C-2 of the substrate, then redonates the proton to the C-3 hydroxyl group to promote C-O bond-cleavage and elimination of water. The carboxylate of the paired Asp or Glu residue is thought to bind and orient the hydroxyl group of the substrate in the stereoelectonically favored conformation.
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