ArticleInsect biochemistry and molecular biology2014
Expression and characterization of an epoxide hydrolase from Anopheles gambiae with high activity on epoxy fatty acids.
Article in Insect biochemistry and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- The soluble epoxide hydrolase inhibitor TPPU alleviates Aβ-mediated neuroinflammatory responses in Drosophila melanogaster and cellular models of alzheimer's disease.Journal of inflammation (London, England) · 2025Article
- Identification of four secretory phospholipase AFrontiers in endocrinology · 2023Article
- Meloxicam methyl group determines enzyme specificity for thiazole bioactivation compared to sudoxicam.Toxicology letters · 2021Article
- EpOMEs act as immune suppressors in a lepidopteran insect, Spodoptera exigua.Scientific reports · 2020Article
- Inhibitors of Eicosanoid Biosynthesis Reveal that Multiple Lipid Signaling Pathways Influence Malaria Parasite Survival inInsects · 2019Article
- Nitric Oxide Mediates Insect Cellular Immunity via Phospholipase A2 Activation.Journal of innate immunity · 2018Article
- Article
- Ingestion of the epoxide hydrolase inhibitor AUDA modulates immune responses of the mosquito, Culex quinquefasciatus during blood feeding.Insect biochemistry and molecular biology · 2016Article
- Epoxide hydrolase activities and epoxy fatty acids in the mosquito Culex quinquefasciatus.Insect biochemistry and molecular biology · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In insects, epoxide hydrolases (EHs) play critical roles in the metabolism of xenobiotic epoxides from the food resources and in the regulation of endogenous chemical mediators, such as juvenile hormones. Using the baculovirus expression system, we expressed and characterized an epoxide hydrolase from Anopheles gambiae (AgEH) that is distinct in evolutionary history from insect juvenile hormone epoxide hydrolases (JHEHs). We partially purified the enzyme by ion exchange chromatography and isoelectric focusing. The experimentally determined molecular weight and pI were estimated to be 35 kD and 6.3 respectively, different than the theoretical ones. The AgEH had the greatest activity on long chain epoxy fatty acids such as 14,15-epoxyeicosatrienoic acids (14,15-EET) and 9,10-epoxy-12Z-octadecenoic acids (9,10-EpOME or leukotoxin) among the substrates evaluated. Juvenile hormone III, a terpenoid insect growth regulator, was the next best substrate tested. The AgEH showed kinetics comparable to the mammalian soluble epoxide hydrolases, and the activity could be inhibited by AUDA [12-(3-adamantan-1-yl-ureido) dodecanoic acid], a urea-based inhibitor designed to inhibit the mammalian soluble epoxide hydrolases. The rabbit serum generated against the soluble epoxide hydrolase of Mus musculus can both cross-react with natural and denatured forms of the AgEH, suggesting immunologically they are similar. The study suggests there are mammalian sEH homologs in insects, and epoxy fatty acids may be important chemical mediators in insects.
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