GPX3: Human glutathione peroxidase 3
PDB Code: 2R37
The reactions carried out by the glutathione peroxidase (GPX) family constitute an important mechanism in the protection against oxidative stress by scavenging and inactivating hydrogen and lipid peroxides to water or lipid hydroxyls in a glutathione-dependent reductive reaction. At least seven glutathione peroxidases (GPX1-7) exist in mammalian cells: cytoplasmic GPX1, gastrointestinal GPX2, plasma GPX3, phospholipid hydroperoxidase GPX4, epididymal GPX5, olfactory GPX6, and non-selenocysteine containing phospholipid hydroperoxidase GPX7.
The wild-type enzymes typically contain an active site selenocysteine that is encoded by the UGA stop codon which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Replacement of this residue by a cysteine, as occurs in GPX7 and GPX5, dramatically decreases the catalytic activity.
GPX3, like the majority of mammalian glutathione peroxidases, is tetrameric. This cytosolic enzyme is expressed in liver, kidney, heart and gonads, and is also found in plasma, serum, and cerebrospinal fluid. Deregulated GPX3 levels/activities are found in a variety of diseases: increased levels were found in asthma, HIV-infected patients, heart of diabetic mouse. Low levels were found in plasma of children with chronic renal failure and patients with prostate cancer. GPX3 activity is also severely reduced in seminal fluid of infertile males and may be a new useful marker of gonadal function in men.
The crystal structure confirms a tetrameric form of GPX3. The active site SelCys73 was mutated to Gly to facilitate protein production in E. coli .

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