ArticleProceedings of the National Academy of Sciences of the United States of America2009
A different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydim.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 66 citations in OpenAlex.
- QSAR-Based Ecotoxicological Assessment of Novel Imidazole Derivatives for Sustainable Crop Protection.Molecules (Basel, Switzerland) · 2026Article
- Structure of the endogenous insect acetyl-coA carboxylase carboxyltransferase domain.The Journal of biological chemistry · 2024Article
- Identification of potential bioactive compounds ofBiochemistry and biophysics reports · 2023Article
- Mining Fatty Acid Biosynthesis for New Antimicrobials.Annual review of microbiology · 2022Review
- Simultaneous Determination of Pyridate, Quizalofop-ethyl, and Cyhalofop-butyl Residues in Agricultural Products Using Liquid Chromatography-Tandem Mass Spectrometry.Foods (Basel, Switzerland) · 2022Article
- Article
- Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants.Nature communications · 2020Article
- Farnesol attenuates oxidative stress and liver injury and modulates fatty acid synthase and acetyl-CoA carboxylase in high cholesterol-fed rats.Environmental science and pollution research international · 2020Article
- Targeted, random mutagenesis of plant genes with dual cytosine and adenine base editors.Nature biotechnology · 2020Article
- Remodeling of Chlamydomonas Metabolism Using Synthetic Inducers Results in Lipid Storage during Growth.Plant physiology · 2019Article
- Target-Site Mutations Conferring Herbicide Resistance.Plants (Basel, Switzerland) · 2019Review
- Herbicidal Activity and Molecular Docking Study of Novel ACCase Inhibitors.Frontiers in plant science · 2018Article
- Alteration of histone H3 lysine 9 dimethylation in peripheral white blood cells of septic patients with trauma and cancer.Molecular medicine reports · 2016Article
- Mechanism of metamifop inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in Echinochloa crus-galli.Scientific reports · 2016Article
- Development and characterization of mutant winter wheat (Triticum aestivum L.) accessions resistant to the herbicide quizalofop.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2015Article
- Structure, activity, and inhibition of the Carboxyltransferase β-subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2014Article
- Article
- Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013Review
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- The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.Protein science : a publication of the Protein Society · 2012Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Acetyl-CoA carboxylases (ACCs) are crucial metabolic enzymes and are attractive targets for drug discovery. Haloxyfop and tepraloxydim belong to two distinct classes of commercial herbicides and kill sensitive plants by inhibiting the carboxyltransferase (CT) activity of ACC. Our earlier structural studies showed that haloxyfop is bound near the active site of the CT domain, at the interface of its dimer, and a large conformational change in the dimer interface is required for haloxyfop binding. We report here the crystal structure at 2.3 A resolution of the CT domain of yeast ACC in complex with tepraloxydim. The compound has a different mechanism of inhibiting the CT activity compared to haloxyfop, as well as the mammalian ACC inhibitor CP-640186. Tepraloxydim probes a different region of the dimer interface and requires only small but important conformational changes in the enzyme, in contrast to haloxyfop. The binding mode of tepraloxydim explains the structure-activity relationship of these inhibitors, and provides a molecular basis for their distinct sensitivity to some of the resistance mutations, as compared to haloxyfop. Despite the chemical diversity between haloxyfop and tepraloxydim, the compounds do share two binding interactions to the enzyme, which may be important anchoring points for the development of ACC inhibitors.
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