EPHX2 Protein, Human (sf9, His)

The EPHX2 protein is a bifunctional enzyme with distinct activities in its C-terminal and N-terminal domains. The C-terminal domain exhibits epoxide hydrolase activity, acting on both alkene oxides and arene oxides. This functionality plays a crucial role in xenobiotic metabolism by degrading potentially toxic epoxides and contributes to determining steady-state levels of physiological mediators. On the other hand, the N-terminal domain of EPHX2 possesses lipid phosphatase activity, displaying 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. Additionally, it exhibits phosphatase activity toward lyso-glycerophospholipids, with some lower activity observed toward lysolipids of sphingolipid and isoprenoid phosphates. These multifaceted enzymatic activities highlight the diverse roles of EPHX2 in cellular processes, including xenobiotic metabolism and lipid homeostasis.