| Function | A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of PUFA. Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools. In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15-lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent. Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone. Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole. Catalyzes the sulfoxidation of fenbedazole. |
| Protein Name | Cytochrome P450 2j2Albendazole MonooxygenaseHydroxylatingAlbendazole MonooxygenaseSulfoxide-FormingArachidonic Acid EpoxygenaseCypiij2Hydroperoxy Icosatetraenoate Isomerase |
| Database Links | Reactome: R-HSA-211935Reactome: R-HSA-211981Reactome: R-HSA-2142670 |
| Cellular Localisation | Endoplasmic Reticulum MembranePeripheral Membrane ProteinMicrosome Membrane |
| Alternative Antibody Names | Anti-Cytochrome P450 2j2 antibodyAnti-Albendazole Monooxygenase antibodyAnti-Hydroxylating antibodyAnti-Albendazole Monooxygenase antibodyAnti-Sulfoxide-Forming antibodyAnti-Arachidonic Acid Epoxygenase antibodyAnti-Cypiij2 antibodyAnti-Hydroperoxy Icosatetraenoate Isomerase antibodyAnti-CYP2J2 antibody |
Information sourced from Uniprot.org
