Glutathione peroxidase (for the family) (GPX (for the family))

Glutathione peroxidases are a family of enzymes that catalyze the reduction of hydrogen peroxide and organic hydroperoxides to water and corresponding alcohols using glutathione as a reducing substrate. They are essential selenoproteins—containing a selenocysteine residue at their active site—providing a crucial antioxidant defense mechanism that protects cells and tissues from oxidative damage by reactive oxygen species (ROS). The most prominent isoforms (GPX1–GPX4, GPX6) have varying tissue distributions and specialized functions, including regulation of cell death pathways (particularly GPX4 in ferroptosis). Selenoproteins in general encompass a larger family of proteins beyond glutathione peroxidases, involved in diverse processes from redox regulation to immune modulation. Deficiency in these enzymes can contribute to a wide range of diseases, particularly those linked to oxidative stress, such as cancer, joint degeneration, cardiovascular conditions, and neurodegeneration. If you require structured data on individual enzymes (e.g., GPX1, GPX4), it is recommended to specify the exact enzyme, as “glutathione peroxidase and other selenoproteins” is too broad for precise annotation.

Other names

Glutathione peroxidase familyGPXSe-GPX (selenium glutathione peroxidase)

Increasing enzyme activity via selenium supplementation (restores antioxidant function in deficiency); Direct inhibition of GPX4 (for ferroptosis induction in cancer); Small molecule inhibitors (research context)