ReviewMolecules (Basel, Switzerland)2020
Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026Article
- Catalytic and structural comparisons of linoleate dioxygenases and their cytochrome P450 companions with enzymes of the cyclooxygenase cascade.The Journal of biological chemistry · 2026Review
- Biochemical Consequences of a Leucine-to-Cysteine Clamp Substitution in Lipoxygenases.Biomolecules · 2025Article
- Structural and Functional Biology of Mammalian ALOX Isoforms with Particular Emphasis on Enzyme Dimerization and Their Allosteric Properties.International journal of molecular sciences · 2024Review
- Intricate Evolution of Multifunctional Lipoxygenase in Red Algae.International journal of molecular sciences · 2024Article
- Synthesis, characterization and reactivity of a Mn(III)-hydroxido complex as a biomimetic model for lipoxygenase.Journal of inorganic biochemistry · 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
- Investigating membrane-binding properties of lipoxygenases using surface plasmon resonance.Biochemical and biophysical research communications · 2023Article
- Acceptors and Effectors Alter Substrate Inhibition Kinetics of a Plant Glucosyltransferase NbUGT72AY1 and Its Mutants.International journal of molecular sciences · 2023Article
- Biochemical and hydrogen-deuterium exchange studies of the single nucleotide polymorphism Y649C in human platelet 12-lipoxygenase linked to a bleeding disorder.Archives of biochemistry and biophysics · 2023Article
- Reevaluation of a Bicyclic Pyrazoline as a Selective 15-Lipoxygenase V-Type Activator Possessing Fatty Acid Specificity.ACS omega · 2022Article
- Specific Roles of Lipoxygenases in Development and Responses to Stress in Plants.Plants (Basel, Switzerland) · 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
- Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2.Bioorganic & medicinal chemistry · 2021Article
- Novel 1,2,4-triazine-quinoline hybrids: The privileged scaffolds as potent multi-target inhibitors of LPS-induced inflammatory response via dual COX-2 and 15-LOX inhibition.European journal of medicinal chemistry · 2021Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoxygenases (LOXs) catalyze the (per) oxidation of fatty acids that serve as important mediators for cell signaling and inflammation. These reactions are initiated by a C-H activation step that is allosterically regulated in plant and animal enzymes. LOXs from higher eukaryotes are equipped with an N-terminal PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain that has been implicated to bind to small molecule allosteric effectors, which in turn modulate substrate specificity and the rate-limiting steps of catalysis. Herein, the kinetic and structural evidence that describes the allosteric regulation of plant and animal lipoxygenase chemistry by fatty acids and their derivatives are summarized.
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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.