ArticleBiochemistry2018
Stereospecific Formation of Z-Trisubstituted Double Bonds by the Successive Action of Ketoreductase and Dehydratase Domains from trans-AT Polyketide Synthases.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 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
- The Chemistry of Phytoplankton.Chemical reviews · 2024Review
- Diene incorporation by a dehydratase domain variant in modular polyketide synthases.Nature chemical biology · 2022Article
- Article
- Cloning, Expression, Purification, and Characterization of β-Galactosidase fromMolecules (Basel, Switzerland) · 2022Article
- Lysozyme-like Protein Produced byMolecules (Basel, Switzerland) · 2021Article
- Thioesterase-Catalyzed Aminoacylation and Thiolation of Polyketides in Fungi.Journal of the American Chemical Society · 2019Article
- Structural Basis of Polyketide Synthase O-Methylation.ACS chemical biology · 2018Article
- Strobilurin biosynthesis in Basidiomycete fungi.Nature communications · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Incubation of (±)-2-methyl-3-ketobutyryl-SNAC (3) and (±)-2-methyl-3-ketopentanoyl-SNAC (4) with BonKR2 or OxaKR5, ketoreductase domains from the bongkrekic acid (1) and oxazolomycin (2) polyketide synthases, in the presence of NADPH gave in each case the corresponding (2 R,3 S)-2-methyl-3-hydroxybutyryl-SNAC (5) or (2 R,3 S)-2-methyl-3-hydroxypentanoyl-SNAC (6) products, as established by chiral gas chromatography-mass spectrometry analysis of the derived methyl esters. Identical results were obtained by BonKR2- and OxaKR5-catalyzed reduction of chemoenzymatically prepared (2 R)-2-methyl-3-ketopentanoyl-EryACP6, (2 R)-2-methyl-3-ketobutyryl-BonACP2 (12), and (2 R)-2-methyl-3-ketopentanoyl-BonACP2 (13). The paired dehydratase domains, BonDH2 and OxaDH5, were then shown to catalyze the reversible syn dehydration of (2 R,3 S)-2-methyl-3-hydroxybutyryl-BonACP2 (14) to give the corresponding trisubstituted ( Z)-2-methylbutenoyl-BonACP2 (16).
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