ReviewProtein science : a publication of the Protein Society2015
The structural basis for specificity in lipoxygenase catalysis.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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95 citing papers in PubMed, 213 citations in OpenAlex.
- Bioassay-Guided Evaluation and LC-MS/MS Characterization of FiveMolecules (Basel, Switzerland) · 2026Article
- Inactivation of Lipase in Grains: Processing Methods, Kinetics, and Storage Stability.Comprehensive reviews in food science and food safety · 2026Review
- Maize LipoxygenasePlants (Basel, Switzerland) · 2026Article
- 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
- A Multistep Computational Approach to Achieve a Complete Human 5-Lipoxygenase Structure and Provide a Pharmacophore Model for Further Drug Design.Molecular informatics · 2026Article
- A Lipoxygenase 3 mutation reverses growth phenotypes in an Arabidopsis Plastid Lipase 3 overexpression line.PloS one · 2026Article
- Octadecanoids as emerging lipid mediators in cnidarian-dinoflagellate symbiosis.Communications biology · 2025Article
- Lipidomic Screening of Marine Diatoms Reveals Release of Dissolved Oxylipins Associated with Silicon Limitation and Growth Phase.Marine drugs · 2025Article
- Biochemical Consequences of a Leucine-to-Cysteine Clamp Substitution in Lipoxygenases.Biomolecules · 2025Article
- The presence of substrate warrants oxygen access tunnels toward the catalytic site of lipoxygenases.Redox biology · 2025Article
- Murine Alox8 versus the human ALOX15B ortholog: differences and similarities.Pflugers Archiv : European journal of physiology · 2024Review
- Design, synthesis, and pharmacological evaluation of indazole carboxamides of N-substituted pyrrole derivatives as soybean lipoxygenase inhibitors.Molecular diversity · 2024Article
- Organizing the Chaos: Novel Insights into the Regulation of Z-3-Hexenal Production in Damaged Maize Leaves.Plants (Basel, Switzerland) · 2024Article
- Impact ofBiochemistry · 2024Article
- 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
- Targeting ferroptosis opens new avenues in gliomas.International journal of biological sciences · 2024Review
- Novel Multi-Target Agents Based on the Privileged Structure of 4-Hydroxy-2-quinolinone.Molecules (Basel, Switzerland) · 2023Article
35 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
Many intriguing facets of lipoxygenase (LOX) catalysis are open to a detailed structural analysis. Polyunsaturated fatty acids with two to six double bonds are oxygenated precisely on a particular carbon, typically forming a single chiral fatty acid hydroperoxide product. Molecular oxygen is not bound or liganded during catalysis, yet it is directed precisely to one position and one stereo configuration on the reacting fatty acid. The transformations proceed upon exposure of substrate to enzyme in the presence of O2 (RH + O2 → ROOH), so it has proved challenging to capture the precise mode of substrate binding in the LOX active site. Beginning with crystal structures with bound inhibitors or surrogate substrates, and most recently arachidonic acid bound under anaerobic conditions, a picture is consolidating of catalysis in a U-shaped fatty acid binding channel in which individual LOX enzymes use distinct amino acids to control the head-to-tail orientation of the fatty acid and register of the selected pentadiene opposite the non-heme iron, suitably positioned for the initial stereoselective hydrogen abstraction and subsequent reaction with O2 . Drawing on the crystal structures available currently, this review features the roles of the N-terminal β-barrel (C2-like, or PLAT domain) in substrate acquisition and sensitivity to cellular calcium, and the α-helical catalytic domain in fatty acid binding and reactions with O2 that produce hydroperoxide products with regio and stereospecificity. LOX structures combine to explain how similar enzymes with conserved catalytic machinery differ in product, but not substrate, specificities.
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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.