Human Epoxide hydrolase 2,EPHX2 ELI

Bifunctional enzyme (PubMed:12574510).

The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687).

Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity).

Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687, PubMed:21217101).

{ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654, ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:22798687}.; Bifunctional enzyme (PubMed:12574510).

The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid (PubMed:12574510).

Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (PubMed:22217705, PubMed:22387545).

{ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:22217705, ECO:0000269|PubMed:22387545}.