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16-September-2008 16:20:32 - peroxidase glutathione peroxidase 1 Identifiers Symbol GPX1 Entrez 2876 HUGO 4553 OMIM 138320 RefSeq NM_000581 UniProt P07203 Other data EC number 1.11.1.9 Locus Chr. 3 p21.3 glutathione peroxidase 3 plasma Identifiers Symbol GPX3 Entrez 2878 HUGO 4555 OMIM 138321 RefSeq NM_002084 UniProt P22352 Other data EC number 1.11.1.9 Locus Chr. 5 q23 glutathione peroxidase 5 epididymal androgen-related protein Identifiers Symbol GPX5 Entrez 2880 HUGO 4557 OMIM 603435 RefSeq NM_001509 UniProt O75715 Other data EC number 1.11.1.9 Locus Chr. 6 p21.32 glutathione peroxidase 6 olfactory Identifiers Symbol GPX6 Entrez 257202 HUGO 4558 OMIM 607913 RefSeq NM_182701 UniProt P59796 Other data EC number 1.11.1.9 Locus Chr. 6 p21 Glutathione peroxidase PDB 1GP1, EC 1.11.1.9 is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water. Contents 1 Isozymes 2 Reaction 3 Structure 4 GP reaction mechanism 5 GP in other animals 6 History 7 References 8 See also Isozymes There are several isozymes encoded by different genes, which vary in celullar location and substrate specificity. Glutathione peroxidase 1 is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide. Reaction An example reaction that glutathione peroxidase catalyzes is: 2GSH + H2O2 → GS-SG + 2H2O, where GSH represents reduced monomeric glutathione, and GS-SG represents glutathione disulfide. Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS-SG + NADPH + H+ → 2 GSH + NADP+. Structure Glutathione peroxidase is a selenium-containing tetrameric glycoprotein, that is, a molecule with four selenocysteine amino acid residues. As the integrity of the cellular and subcellular membranes depends heavily on glutathione peroxidase, the antioxidative protective system of glutathione peroxidase itself depends heavily on the presence of selenium. GP reaction mechanism The mechanism is at the Selenocystein site, which is in a Se- form as resting state. This is oxidized by the peroxide to SeOH which is then trapped by a GSH molecule to Se-SG and by another GSH molecule to Se- again, releasing a GS-SG by-product. GP in other animals Mice genetically engineered to lack glutathione peroxidase 1 Gpx1 knockout mice are phenotypically normal, indicating that this enzyme is not critical for life. However, glutathione peroxidase 4 knockout Gpx4 knockout mice die during early embryonic development. There is some evidence that reduced levels of glutathione peroxidase 4 can increase life expectancy in mice.1 The bovine erythrocyte enzyme has a molecular weight of 84 kDa. History Glutathione peroxidase was discovered in 1957 by Gordon C. Mills. 2 References ^ Ran Q, Liang H, Ikeno Y, et al 2007. Reduction in glutathione peroxidase 4 increases life span through increased sensitivity to apoptosis. J. Gerontol. A Biol. Sci. Med. Sci. 62 9: 932-42. PMID 17895430. ^ Mills, G. Journal of Biological Chemistry 229:189-97.1957. See also Glutathione reductase v d e Oxidoreductases: peroxidases EC 1.11 Catalase - Cytochrome c peroxidase - Eosinophil peroxidase - Glutathione peroxidase - Horseradish peroxidase - Lactoperoxidase - Myeloperoxidase - Thyroid peroxidase - Deiodinase Tetraiodothyronine 5' deiodinase This EC 1.11 enzyme-related article is a stub. Retrieved from http://en..org/wiki/Glutathione_peroxidase Categories: Genes on chromosome 3 | Genes on chromosome 5 | Genes on chromosome 6 | EC 1.11.1 | Antioxidants | Selenium compounds | Oxidoreductase stubsHidden category: Protein pages needing a picture Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages Català Česky Deutsch Français Italiano Polski This page was last modified on 30 June 2008, at 16:02
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