ArticleJournal of lipid research2012
Lysophosphatidic acids are new substrates for the phosphatase domain of soluble epoxide hydrolase.
Article in Journal of lipid research, 2012. 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, 41 citations in OpenAlex.
- Fragment-Based Discovery of Fenamic Acids as Pan-Species Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain.ACS chemical biology · 2026Article
- Inactivation of the Phosphatase Activity of Soluble Epoxide Hydrolase Modulates SIRT3 and Attenuates Experimental Pulmonary Hypertension.Comprehensive Physiology · 2026Article
- Intradomain Allosteric Regulation of Soluble Epoxide Hydrolase by Its Substrates.International journal of molecular sciences · 2024Article
- Mice deficient in the phosphatase activity of sEH show decreased levels of the endocannabinoid 2-AG in the olfactory bulb and depressive-like behavior.FEBS letters · 2024Article
- Inhibitory Activity of Glycosides fromJournal of microbiology and biotechnology · 2024Article
- From Classical to Alternative Pathways of 2-Arachidonoylglycerol Synthesis: AlterAGs at the Crossroad of Endocannabinoid and Lysophospholipid Signaling.Molecules (Basel, Switzerland) · 2024Review
- Hydrogen Peroxide Induces Ethanol-inducible CYP2E1Current drug metabolism · 2024Article
- In Silico Modeling and Structural Analysis of Soluble Epoxide Hydrolase Inhibitors for Enhanced Therapeutic Design.Molecules (Basel, Switzerland) · 2023Article
- Soluble epoxide hydrolase maintains steady-state lipid turnover linked with autocrine signaling in peritoneal macrophages.iScience · 2023Article
- CRISPR/Cas9-mediated inactivation of the phosphatase activity of soluble epoxide hydrolase prevents obesity and cardiac ischemic injury.Journal of advanced research · 2023Article
- Redox Regulation of Soluble Epoxide Hydrolase-Implications for Cardiovascular Health and Disease.Cells · 2022Review
- Impact of SMTP Targeting Plasminogen and Soluble Epoxide Hydrolase on Thrombolysis, Inflammation, and Ischemic Stroke.International journal of molecular sciences · 2021Review
- Crossing signals: bioactive lipids in the microvasculature.American journal of physiology. Heart and circulatory physiology · 2020Review
- Discovery of the First in Vivo Active Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain.Journal of medicinal chemistry · 2019Article
- N-Substituted amino acid inhibitors of the phosphatase domain of the soluble epoxide hydrolase.Biochemical and biophysical research communications · 2019Article
- 15-deoxy-ΔCommunications biology · 2019Article
- Soluble epoxide hydrolase as a therapeutic target for pain, inflammatory and neurodegenerative diseases.Pharmacology & therapeutics · 2017Review
- Structure-activity relationships of the plasminogen modulator SMTP with respect to the inhibition of soluble epoxide hydrolase.The Journal of antibiotics · 2015Article
- Role of phosphatase activity of soluble epoxide hydrolase in regulating simvastatin-activated endothelial nitric oxide synthase.Scientific reports · 2015Article
- Arachidonic acid monooxygenase: Genetic and biochemical approaches to physiological/pathophysiological relevance.Prostaglandins & other lipid mediators · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that has a C-terminus epoxide hydrolase domain and an N-terminus phosphatase domain. The endogenous substrates of epoxide hydrolase are known to be epoxyeicosatrienoic acids, but the endogenous substrates of the phosphatase activity are not well understood. In this study, to explore the substrates of sEH, we investigated the inhibition of the phosphatase activity of sEH toward 4-methylumbelliferyl phosphate by using lecithin and its hydrolyzed products. Although lecithin itself did not inhibit the phosphatase activity, the hydrolyzed lecithin significantly inhibited it, suggesting that lysophospholipid or fatty acid can inhibit it. Next, we investigated the inhibition of phosphatase activity by lysophosphatidyl choline, palmitoyl lysophosphatidic acid, monopalmitoyl glycerol, and palmitic acid. Palmitoyl lysophosphatidic acid and fatty acid efficiently inhibited phosphatase activity, suggesting that lysophosphatidic acids (LPAs) are substrates for the phosphatase activity of sEH. As expected, palmitoyl, stearoyl, oleoyl, and arachidonoyl LPAs were efficiently dephosphorylated by sEH (Km, 3-7 μM; Vmax, 150-193 nmol/min/mg). These results suggest that LPAs are substrates of sEH, which may regulate physiological functions of cells via their metabolism.
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