PRDX6 Protein, Human (His)

PRDX6, a thiol-specific peroxidase, demonstrates a crucial role in cellular defense against oxidative stress by catalyzing the reduction of hydrogen peroxide and various organic hydroperoxides to water and alcohols, respectively. This multifunctional enzyme exhibits the ability to reduce H(2)O(2) as well as short-chain organic, fatty acid, and phospholipid hydroperoxides. Additionally, PRDX6 possesses phospholipase activity, allowing it to either reduce the oxidized sn-2 fatty acyl group of phospholipids through peroxidase activity or hydrolyze the sn-2 ester bond of phospholipids through phospholipase activity. These functions are dependent on its binding to phospholipids at acidic pH and to oxidized phospholipids at cytosolic pH. Beyond its peroxidase activity, PRDX6 serves a critical role in phospholipid homeostasis and acts as an acyl-CoA-dependent lysophospholipid acyltransferase, facilitating the conversion of lysophosphatidylcholine (LPC) into phosphatidylcholine (PC). The enzyme exhibits a clear preference for LPC as the lysophospholipid and palmitoyl CoA as the fatty acyl substrate.