GPX2 (gene)

GPX2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2HE3

Identifiers

Aliases

GPX2, GI-GPx, GPRP, GPRP-2, GPx-2, GPx-GI, GSHPX-GI, GSHPx-2, glutathione peroxidase 2

External IDs

MGI: 106609 HomoloGene: 20479 GeneCards: GPX2

Gene ontology
Molecular function	• electron carrier activity • oxidoreductase activity • glutathione peroxidase activity • peroxidase activity
Cellular component	• cytoplasm • cytosol • extracellular exosome
Biological process	• oxidation-reduction process • response to oxidative stress • response to reactive oxygen species • cellular oxidant detoxification
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2877


14776

Ensembl


ENSG00000176153


ENSMUSG00000042808

UniProt


P18283


Q9JHC0

RefSeq (mRNA)


NM_002083


NM_030677

RefSeq (protein)


NP_002074.2


NP_109602.2

Location (UCSC)

Chr 14: 64.94 – 64.94 Mb

Chr 12: 76.79 – 76.8 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.^[3]^[4]^[5]

This gene is a member of the glutathione peroxidase family encoding a selenium-dependent glutathione peroxidase that is one of two isoenzymes responsible for the majority of the glutathione-dependent hydrogen peroxide-reducing activity in the epithelium of the gastrointestinal tract. Studies in knockout mice indicate that mRNA expression levels respond to luminal microflora, suggesting a role of the ileal glutathione peroxidases in preventing inflammation in the GI tract.^[5]

The antioxidant enzyme glutathione peroxidase 2 (Gpx2) is one out of eight known glutathione peroxidases (Gpx1-8) in humans. Mammalian Gpx1, GPx2 (this protein), Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents. In selenoproteins, the 21st amino acid selenocysteine is inserted in the nascent polypeptide chain during the process of translational recoding of the UGA stop codon.

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Chu FF, Doroshow JH, Esworthy RS (Mar 1993). "Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI". J Biol Chem. 268 (4): 2571–6. PMID 8428933.
↑ Chu FF (Feb 1994). "The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively". Cytogenet Cell Genet. 66 (2): 96–8. doi:10.1159/000133675. PMID 8287691.
1 2 "Entrez Gene: GPX2 glutathione peroxidase 2 (gastrointestinal)".

Akasaka M, Mizoguchi J, Takahashi K (1990). "A human cDNA sequence of a novel glutathione peroxidase-related protein.". Nucleic Acids Res. 18 (15): 4619. doi:10.1093/nar/18.15.4619. PMC 331311. PMID 2388849.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Chu FF, Rohan de Silva HA, Esworthy RS, et al. (1997). "Polymorphism and chromosomal localization of the GI-form of human glutathione peroxidase (GPX2) on 14q24.1 by in situ hybridization.". Genomics. 32 (2): 272–6. doi:10.1006/geno.1996.0115. PMID 8833155.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene. 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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. PMID 9501919.
Choi J, Liu RM, Kundu RK, et al. (2000). "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice.". J. Biol. Chem. 275 (5): 3693–8. doi:10.1074/jbc.275.5.3693. PMID 10652368.
Kelner MJ, Bagnell RD, Montoya MA, Lanham KA (2000). "Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents.". Gene. 248 (1-2): 109–16. doi:10.1016/S0378-1119(00)00137-2. PMID 10806356.
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. PMID 11368344.
Komatsu H, Okayasu I, Mitomi H, et al. (2001). "Immunohistochemical detection of human gastrointestinal glutathione peroxidase in normal tissues and cultured cells with novel mouse monoclonal antibodies.". J. Histochem. Cytochem. 49 (6): 759–66. doi:10.1177/002215540104900609. PMID 11373322.
Florian S, Wingler K, Schmehl K, et al. (2002). "Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue.". Free Radic. Res. 35 (6): 655–63. doi:10.1080/10715760100301181. PMID 11811519.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Müller C, Wingler K, Brigelius-Flohé R (2003). "3'UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency.". Biol. Chem. 384 (1): 11–8. doi:10.1515/BC.2003.002. PMID 12674495.
Esworthy RS, Binder SW, Doroshow JH, Chu FF (2003). "Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression.". Biol. Chem. 384 (4): 597–607. doi:10.1515/BC.2003.067. PMID 12751789.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
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. PMID 15910762.
Banning A, Deubel S, Kluth D, et al. (2005). "The GI-GPx gene is a target for Nrf2.". Mol. Cell. Biol. 25 (12): 4914–23. doi:10.1128/MCB.25.12.4914-4923.2005. PMC 1140597. PMID 15923610.
Yan W, Chen X (2006). "GPX2, a direct target of p63, inhibits oxidative stress-induced apoptosis in a p53-dependent manner.". J. Biol. Chem. 281 (12): 7856–62. doi:10.1074/jbc.M512655200. PMID 16446369.
Singh A, Rangasamy T, Thimmulappa RK, et al. (2007). "Glutathione peroxidase 2, the major cigarette smoke-inducible isoform of GPX in lungs, is regulated by Nrf2.". Am. J. Respir. Cell Mol. Biol. 35 (6): 639–50. doi:10.1165/rcmb.2005-0325OC. PMC 2643293. PMID 16794261.

PDB gallery

2he3: Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)

Oxidoreductases: peroxidases (EC 1.11)

1.11.1.1-14	Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 2 3 4 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase

1.11.1.15 (peroxiredoxin)	1 2 3 4 5 6

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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GPX2 (gene)

References

Further reading