ArticleThe Journal of biological chemistry2014
Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid-binding site of 8R-lipoxygenase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Who cites it
39 citing papers in PubMed, 74 citations in OpenAlex.
- Description of the rate-limiting hydrogen tunneling mechanism for plant 9- and 13-lipoxygenases.Protein science : a publication of the Protein Society · 2026Article
- Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026Article
- Bacterial lipoxygenases for fatty acid oxyfunctionalization: advances and future directions.Applied microbiology and biotechnology · 2026Review
- Biochemical Consequences of a Leucine-to-Cysteine Clamp Substitution in Lipoxygenases.Biomolecules · 2025Article
- Murine Alox8 versus the human ALOX15B ortholog: differences and similarities.Pflugers Archiv : European journal of physiology · 2024Review
- Structural and Functional Biology of Mammalian ALOX Isoforms with Particular Emphasis on Enzyme Dimerization and Their Allosteric Properties.International journal of molecular sciences · 2024Review
- Identification of the Thermal Activation Network in Human 15-Lipoxygenase-2: Divergence from Plant Orthologs and Its Relationship to Hydrogen Tunneling Activation Barriers.ACS catalysis · 2024Article
- Structural and Functional Characterization of Lipoxygenases from Diatoms by Bioinformatics and Modelling Studies.Biomolecules · 2024Article
- Cryo-EM structures of human arachidonate 12S-lipoxygenase bound to endogenous and exogenous inhibitors.Blood · 2023Article
- Article
- Hydroperoxidation of Docosahexaenoic Acid by Human ALOX12 and pigALOX15-mini-LOX.International journal of molecular sciences · 2023Article
- Integracides: Tetracyclic Triterpenoids fromLife (Basel, Switzerland) · 2022Article
- Molecular Insights into Lipoxygenases in Diatoms Based on Structure Prediction: a Pioneering Study on Lipoxygenases Found in Pseudo-nitzschia arenysensis and Fragilariopsis cylindrus.Marine biotechnology (New York, N.Y.) · 2022Review
- Arachidonate 15-lipoxygenase type B: Regulation, function, and its role in pathophysiology.Frontiers in pharmacology · 2022Review
- Untangling the web of 5-lipoxygenase-derived products from a molecular and structural perspective: The battle between pro- and anti-inflammatory lipid mediators.Biochemical pharmacology · 2021Review
- Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases.Molecules (Basel, Switzerland) · 2020Review
- Structural and mechanistic insights into 5-lipoxygenase inhibition by natural products.Nature chemical biology · 2020Article
- A site-moiety map and virtual screening approach for discovery of novel 5-LOX inhibitors.Scientific reports · 2020Article
- The Soybean Lipoxygenase-Substrate Complex: Correlation between the Properties of Tunneling-Ready States and ENDOR-Detected Structures of Ground States.Biochemistry · 2020Article
- Redox phospholipidomics of enzymatically generated oxygenated phospholipids as specific signals of programmed cell death.Free radical biology & medicine · 2020Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Lipoxygenases (LOX) play critical roles in mammalian biology in the generation of potent lipid mediators of the inflammatory response; consequently, they are targets for the development of isoform-specific inhibitors. The regio- and stereo-specificity of the oxygenation of polyunsaturated fatty acids by the enzymes is understood in terms of the chemistry, but structural observation of the enzyme-substrate interactions is lacking. Although several LOX crystal structures are available, heretofore the rapid oxygenation of bound substrate has precluded capture of the enzyme-substrate complex, leaving a gap between chemical and structural insights. In this report, we describe the 2.0 Å resolution structure of 8R-LOX in complex with arachidonic acid obtained under anaerobic conditions. Subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation. Accompanying experimental work supports a model in which both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery.
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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.