ArticleJournal of the American Chemical Society2017
Elucidation of the Cryptic Methyl Group Epimerase Activity of Dehydratase Domains from Modular Polyketide Synthases Using a Tandem Modules Epimerase Assay.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain.Beilstein journal of organic chemistry · 2024Article
- Heterologous Production and Biosynthesis of Threonine-16:0dioic acids with a Hydroxamate Moiety.Journal of natural products · 2023Article
- Identification, cloning and heterologous expression of biosynthetic gene cluster for desertomycin.The Journal of antibiotics · 2020Article
- pH-Rate profiles establish that polyketide synthase dehydratase domains utilize a single-base mechanism.Organic & biomolecular chemistry · 2018Article
- Molecular Basis for Olefin Rearrangement in the Gephyronic Acid Polyketide Synthase.ACS chemical biology · 2018Article
- Synthetic biology of polyketide synthases.Journal of industrial microbiology & biotechnology · 2018Article
- Stereospecific Formation of Z-Trisubstituted Double Bonds by the Successive Action of Ketoreductase and Dehydratase Domains from trans-AT Polyketide Synthases.Biochemistry · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Dehydratase (DH) domains of cryptic function are often found in polyketide synthase (PKS) modules that produce epimerized (2S)-2-methyl-3-ketoacyl-ACP (acyl carrier protein) intermediates. A combination of tandem equilibrium isotope exchange (EIX) and a newly developed Tandem Modules Epimerase assay revealed the intrinsic epimerase activity of NanDH1 and NanDH5, from modules 1 and 5, respectively, of the nanchangmycin (1) PKS as well of NigDH1, from module 1 of the nigericin (3) PKS. Unexpectedly, all three epimerase-active DH domains were also found to possess intrinsic dehydratase activity, whereas the conventional DH domains, EryDH4, from module 4 of the erythromycin synthase, and NanDH2 from module 2 of the nanchangmycin synthase, were shown to have cryptic epimerase activity.
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