| Cellular glutathione peroxidase (c-GPx, EC 1.11.1.9) is a member of a family of GPx enzymes whose function is to detoxify peroxides in the cell (Ursini, 1995). Because peroxides can decompose to form highly reactive radicals, the GPx enzymes play a critical role in protecting the cell from free radical damage, particularly lipid peroxidation. The GPx enzymes catalyze the reduction of H2O2 to water and organic peroxides (R-O-O-H) to the corresponding stable alcohols (R-O-H) using glutathione (GSH) as a source of reducing equivalents:
With the exception of phospholipid-hydroperoxide GPx, a monomer, all of the GPx enzymes are comprised of 4 identical subunits (monomer Mr 22-23 kDa). Each subunit contains a molecule of selenocysteine in the enzyme active site. The selenocysteine is thought to participate directly in electron donation to the peroxide substrate and become oxidized in the process. The enzyme then uses glutathione as an electron donor to regenerate the reduced form of the selenocysteine (Ursini, 1995). The GPx enzymes accept a wide variety of organic peroxides as substrates. However, with the exception of phospholipid hydroperoxide GPx and perhaps plGPx, the enzymes exhibit a strong preference for glutathione as a source of reducing equivalents. Phospholipid-hydroperoxide GPx (Mr 19 kDa) is the only enzyme with significant activity on esterified phospholipids and cholesterol in membranes.
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