GPX2 Human

Glutathione Peroxidase 2 (GPX2) is a member of the glutathione peroxidase family, which consists of eight known enzymes (GPX1-8) in humans . These enzymes play a crucial role in protecting the organism from oxidative damage by reducing lipid hydroperoxides to their corresponding alcohols and free hydrogen peroxide to water . GPX2, specifically, is an intestinal and extracellular enzyme .

The primary function of GPX2 is to detoxify hydrogen peroxide, making it one of the most important antioxidant enzymes in humans . It is involved in the neutralization of reactive oxygen species (ROS), which are harmful byproducts of cellular metabolism that can cause significant damage to cellular components if not properly managed .

GPX2, like other glutathione peroxidases, contains a selenocysteine residue at its active site. The enzyme catalyzes the reduction of hydrogen peroxide by oxidizing the selenol group of the selenocysteine residue to a selenenic acid (RSeOH) intermediate . This intermediate is then reduced back to the selenol form by glutathione (GSH), completing the catalytic cycle and producing water and oxidized glutathione (GS-SG) as byproducts .

Recombinant human GPX2 is produced using genetic engineering techniques where the GPX2 gene is cloned and expressed in suitable host cells, such as E. coli or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes .

GPX2 has been studied extensively for its role in cancer biology. It has been identified as a metabolic driver of the tumor immune microenvironment and immune checkpoint inhibitor response . Overexpression of GPX2 has been associated with “cold” tumors, which have poor baseline immune cell infiltration and respond unfavorably to immune checkpoint inhibitors . This makes GPX2 a potential target for cancer immunotherapy.