Glutathione peroxidase 1 (GPx1)

Glutathione peroxidase 1 is a cytosolic and mitochondrial enzyme found ubiquitously in human tissues[1][2][3][5]. It catalyzes the reduction of hydrogen peroxide and soluble hydroperoxides, using reduced glutathione (GSH) as the electron donor, thereby defending cells from oxidative damage[1][2][3][7]. As a selenoenzyme, its activity depends on incorporation of the amino acid selenocysteine, requiring adequate dietary selenium[1][3]. GPx1 forms a homotetramer and represents the prototype of the glutathione peroxidase family, which also includes several related isozymes[1][2]. Deficiencies or genetic variants in GPx1 are linked to increased risk of cancer, cardiovascular, and neurological diseases, whereas overexpression or mimetic therapy might offer benefits against oxidative stress–associated pathologies[1][3][5][9]. GPx1 is a major antioxidant enzyme essential for cellular health, redox signaling, and the limitation of oxidative damage in human biology[1][3][5].

Other names

GPx-1GSHPx-1Cellular glutathione peroxidasePhospholipid-hydroperoxide glutathione peroxidase1.11.1.9 (Enzyme Commission number)

Drugs that mimic or boost GPx1 act by reducing hydrogen peroxide and lipid hydroperoxides, protecting cells from oxidative stress and damage. Selenium supplementation increases GPx1 activity by providing selenocysteine for functional enzyme assembly. Ebselen and similar molecules catalytically reduce peroxides, replicating or enhancing GPx1 activity.