ArticleBiochemistry2016
Epimerase and Reductase Activities of Polyketide Synthase Ketoreductase Domains Utilize the Same Conserved Tyrosine and Serine Residues.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular basis for depsipeptide HDAC inhibitor combinatorial biosynthesis.Nature communications · 2026Article
- Total Synthesis of Ussuriedine via a Late-Stage Stevens Rearrangement: Implications for Biosynthesis.Journal of the American Chemical Society · 2026Article
- Resistance Gene-Guided Discovery of a Fungal Spirotetramate as an Acetolactate Synthase Inhibitor.Journal of the American Chemical Society · 2025Article
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- Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain.Beilstein journal of organic chemistry · 2024Article
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- Sea Urchin Polyketide Synthase SpPks1 Produces the Naphthalene Precursor to Echinoderm Pigments.Journal of the American Chemical Society · 2022Article
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- Article
- Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase.Journal of structural biology · 2018Article
- Engineering modular polyketide synthases for production of biofuels and industrial chemicals.Current opinion in biotechnology · 2018Review
- Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates.Chemical communications (Cambridge, England) · 2017Article
- Engineered polyketides: Synergy between protein and host level engineering.Synthetic and systems biotechnology · 2017Review
- Elucidation of the Cryptic Methyl Group Epimerase Activity of Dehydratase Domains from Modular Polyketide Synthases Using a Tandem Modules Epimerase Assay.Journal of the American Chemical Society · 2017Article
- Pathogenicity-associated protein domains: The fiercely-conserved evolutionary signatures.Gene reports · 2017Review
- Mechanism and Stereochemistry of Polyketide Chain Elongation and Methyl Group Epimerization in Polyether Biosynthesis.Journal of the American Chemical Society · 2017Article
- Towards Precision Engineering of Canonical Polyketide Synthase Domains: Recent Advances and Future Prospects.Molecules (Basel, Switzerland) · 2017Review
- Polyketide stereocontrol: a study in chemical biology.Beilstein journal of organic chemistry · 2017Review
- Nature as organic chemist.The Journal of antibiotics · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The role of the conserved active site tyrosine and serine residues in epimerization catalyzed by polyketide synthase ketoreductase (PKS KR) domains has been investigated. Both mutant and wild-type forms of epimerase-active KR domains, including the intrinsically redox-inactive EryKR3° and PicKR3° as well as redox-inactive mutants of EryKR1, were incubated with [2-(2)H]-(2R,3S)-2-methyl-3-hydroxypentanoyl-SACP ([2-(2)H]-2) and 0.05 equiv of NADP(+) in the presence of the redox-active, epimerase-inactive EryKR6 domain. The residual epimerase activity of each mutant was determined by tandem equilibrium isotope exchange, in which the first-order, time-dependent washout of isotope from 2 was monitored by liquid chromatography-tandem mass spectrometry with quantitation of the deuterium content of the diagnostic pantetheinate ejection fragment (4). Replacement of the active site Tyr or Ser residues, alone or together, significantly reduced the observed epimerase activity of each KR domain with minimal effect on substrate binding. Our results demonstrate that the epimerase and reductase activities of PKS KR domains share a common active site, with both reactions utilizing the same pair of Tyr and Ser residues.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.