Glutathione peroxidase 6 (GPx-6) is an enzyme that in humans is encoded by the GPX6gene.[5][6]
This gene product belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA 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. Expression of this gene is restricted to embryos and adult olfactory epithelium.[5]
Richard MJ, Guiraud P, Didier C, et al. (2001). "Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake: consequences on cellular resistance to UV-A radiation". Arch. Biochem. Biophys. 386 (2): 213–20. doi:10.1006/abbi.2000.2197. PMID11368344.
Opalenik SR, Ding Q, Mallery SR, Thompson JA (1998). "Glutathione depletion associated with the HIV-1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor". Arch. Biochem. Biophys. 351 (1): 17–26. doi:10.1006/abbi.1997.0566. PMID9501919.
Price TO, Ercal N, Nakaoke R, Banks WA (2005). "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells". Brain Res. 1045 (1–2): 57–63. doi:10.1016/j.brainres.2005.03.031. PMID15910762. S2CID7362454.
