ArticleNature chemical biology2012
Divergence of multimodular polyketide synthases revealed by a didomain structure.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 79 citations in OpenAlex.
- Engineered Modular Polyketide Synthases Elucidate How Enoylreductases Collaborate with Downstream Acyl Carrier Proteins and Ketosynthases to Set Stereocenters.Journal of the American Chemical Society · 2026Article
- Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase.Nature communications · 2025Article
- Distinct Acyl Carrier Protein Docking Sites Help Mediate the Opposite Stereoselectivities of A- and B-type Modular Polyketide Synthase Ketoreductases.Biochemistry · 2025Article
- Repurposing a Fully Reducing Polyketide Synthase toward 2-Methyl Guerbet-like Lipids.ACS catalysis · 2024Article
- Structure and Mechanisms of Assembly-Line Polyketide Synthases.Annual review of biochemistry · 2024Review
- Bioinformatic prediction of the stereoselectivity of modular polyketide synthase: an update of the sequence motifs in ketoreductase domain.Beilstein journal of organic chemistry · 2024Article
- Module-Based Polyketide Synthase Engineering forACS synthetic biology · 2023Review
- Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023Article
- Fragment antigen binding domains (FSynthetic and systems biotechnology · 2022Article
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- In vitro Cas9-assisted editing of modular polyketide synthase genes to produce desired natural product derivatives.Nature communications · 2020Article
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
- The architectures of iterative type I PKS and FAS.Natural product reports · 2018Review
- Protein-protein interactions in "cis-AT" polyketide synthases.Natural product reports · 2018Review
- The modules of trans-acyltransferase assembly lines redefined with a central acyl carrier protein.Proteins · 2018Article
- ClusterCAD: a computational platform for type I modular polyketide synthase design.Nucleic acids research · 2018Article
- Engineered polyketides: Synergy between protein and host level engineering.Synthetic and systems biotechnology · 2017Review
- The Uncommon Enzymology of Cis-Acyltransferase Assembly Lines.Chemical reviews · 2017Review
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5 authors at 3 institutions in 1 country.
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Abstract
The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 Å-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an ∼600-Å(2) interface with KR distinct from that of the related mammalian fatty acid synthase (FAS). In contrast to the ER domains of the mammalian FAS, the ER domains of the second module of the spinosyn PKS do not make contact across the two-fold axis of the synthase. This monomeric organization may have been necessary in the evolution of multimodular PKSs to enable acyl carrier proteins to access each of their cognate enzymes. The isolated ER domain showed activity toward a substrate analog, enabling us to determine the contributions of its active site residues.
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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.