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Information on EC 1.11.1.9 - glutathione peroxidase and Organism(s) Mus musculus
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1.11.1.9 glutathione peroxidaseIUBMB Comments
A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).
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Word Map
- 1.11.1.9
- dismutase
- catalase
- sod
- malondialdehyde
- necrosis
-
thiobarbituric
- erythrocyte
- wistar
- tnf
-
tbars
- glutathione-s-transferase
- s-transferase
- cholesterol
-
reperfusion
- hippocampus
- ischemia
- myocardial
- selenite
- gssg
- triglyceride
-
hepatotoxicity
- creatinine
-
defenses
- aminotransferase
- caspase-3
-
anti-oxidant
- bcl-2
-
neuroprotective
-
sacrificed
-
albino
- cardiac
-
selenoproteins
- alpha-tocopherol
- mn-sod
-
2-related
-
hepatoprotective
- streptozotocin
-
acid-reactive
- melatonin
-
dienes
- myeloperoxidase
-
ccl4-induced
-
8-ohdg
-
uric
- analysis
-
gavage
- medicine
-
nephrotoxicity
- synthesis
-
pro-oxidant
- peroxidases
- ccl4
- oxygenase-1
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutathione peroxidase, gpx, gsh-px, ebselen, gshpx, gpx-1, gsh peroxidase, glutathione peroxidase 1, plasma glutathione peroxidase, selenium-dependent glutathione peroxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6P229
-
-
-
-
ARMEP24
-
-
-
-
AtGPX1
-
-
-
-
Cellular glutathione peroxidase
-
-
-
-
Cuticular glycoprotein GP29
-
-
-
-
DI29
-
-
-
-
EGLP
-
-
-
-
Epididymis-specific glutathione peroxidase-like protein
-
-
-
-
Extracellular glutathione peroxidase
-
-
-
-
Gastrointestinal glutathione peroxidase
-
-
-
-
GP30
-
-
-
-
GPRP
-
-
-
-
GPX
GPX1
GPx4
GSH peroxidase
-
-
-
-
GSHPx-GI
-
-
-
-
Major androgen-regulated protein
-
-
-
-
Major surface antigen GP29
-
-
-
-
Nt-SubC08
-
-
-
-
Odorant-metabolizing protein RY2D1
-
-
-
-
peroxidase, glutathione
-
-
-
-
reduced glutathione peroxidase
-
-
-
-
Salt-associated protein
-
-
-
-
selenium-glutathione peroxidase
-
-
-
-
GPX
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
glutathione:hydrogen-peroxide oxidoreductase
A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).
CAS REGISTRY NUMBER
COMMENTARY
9013-66-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
GPX1 protects against diquat-induced cell death, but promotes peroxynitrite induced cell death. GPX1 seems to play contrasting roles in coping with reactive oxygen species vs. reactive nitrogen species
-
-
?
additional information
?
-
-
Gpx2 affords resistance to gastrointestinal pathology in Se-depleted mice
-
-
?
additional information
?
-
does not accept thioredoxin as hydrogen donor
-
-
?
additional information
?
-
-
glutathione peroxidase 2 inhibits malignant characteristics of tumor cells, such as migration and invasion, by counteracting cyclooxygenase-2 expression but is required for the growth of transformed intestinal cells and may, therefore, facilitate tumor cell growth
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
GPX1 protects against diquat-induced cell death, but promotes peroxynitrite induced cell death. GPX1 seems to play contrasting roles in coping with reactive oxygen species vs. reactive nitrogen species
-
-
?
additional information
?
-
-
Gpx2 affords resistance to gastrointestinal pathology in Se-depleted mice
-
-
?
additional information
?
-
-
glutathione peroxidase 2 inhibits malignant characteristics of tumor cells, such as migration and invasion, by counteracting cyclooxygenase-2 expression but is required for the growth of transformed intestinal cells and may, therefore, facilitate tumor cell growth
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
injection of the O-GlcNAcase inhibitor 1,2-dideoxy-2'-propyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline increases GPX1 activity in the mouse liver
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
overexpression of glutathione peroxidase attenuates myocardial remodeling and preserves diastolic function in diabetic heart
isozyme n-GPx-4 is specifically expressed in late spermatocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
methylmercury neurotoxicity is associated with inhibition of glutathione peroxidase
physiological function
physiological function
-
anti-oxidant enzyme, essential for cell survival during oxidative stress
physiological function
-
glutathione peroxidase activity increases in the brain of mice treated with a derivative of acetaldehyde ammonia during long-term intermittent normobaric hypoxia
physiological function
in mice overexpressing isoform Gpx1, activator protein AP-1 and albumin D box-binding protein (DBP) mRNA and protein levels are elevated in pacreatic islets compared with the wild-type islet. Their mRNA abundances in the cultured islets are elevated by ebselen and N-acetylcysteine, but decreased by H2O2. Both AP-1 and DBP can bind to the regenerating islet-derived protein Reg2 promoter in the overexpressing islets. Deleting the AP-1 and/or DBP binding domains in the Reg2 promoter attenuates and/or abolishes the inhibition of Reg2 promoter activation by ebselen as the Gpx1 mimic
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GPX8_MOUSE
209
1
24148
Swiss-Prot
Secretory Pathway (Reliability: 3)
GPX3_MOUSE
226
0
25424
Swiss-Prot
Secretory Pathway (Reliability: 2)
GPX5_MOUSE
221
0
25393
Swiss-Prot
Secretory Pathway (Reliability: 1)
GPX6_MOUSE
221
0
24903
Swiss-Prot
Secretory Pathway (Reliability: 1)
GPX7_MOUSE
186
0
21061
Swiss-Prot
Secretory Pathway (Reliability: 1)
GPX1_MOUSE
201
0
22329
Swiss-Prot
Mitochondrion (Reliability: 3)
GPX2_MOUSE
190
0
21990
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant plasmid is introduced into Agrobacterium tumefaciens strain Ag11 amd transformation of Lycopersicon esculentum is performed
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adult male Swiss mice treated with 40 mg/ml methylmercury for 21 days show about 50% decrease in GPx activity in the brain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
method of measuring of glutathione peroxidase activity using H2O2. At a concentration of reduced glutathione of 0.55 mM, the concentration of H2O2 of 0.192 mM is saturating for glutathione peroxidase. The duration of incubation does not exceed 60 sec, if 13% homogenate is used
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsushima, S.; Kinugawa, S.; Ide, T.; Matsusaka, H.; Inoue, N.; Ohta, Y.; Yokota, T.; Sunagawa, K.; Tsutsui, H.
Overexpression of glutathione peroxidase attenuates myocardial remodeling and preserves diastolic function in diabetic heart
Am. J. Physiol. Heart Circ. Physiol.
291
H2237-H2245
2006
Mus musculus
Herbette, S.; Menn, A.L.; Rousselle, P.; Ameglio, T.; Faltin, Z.; Branlard, G.; Eshdat, Y.; Julien, J.L.; Drevet, J.R.; Roeckel-Drevet, P.
Modification of photosynthetic regulation in tomato overexpressing glutathione peroxidase
Biochim. Biophys. Acta
1724
108-118
2005
Mus musculus
McLean, C.W.; Mirochnitchenko, O.; Claus, C.P.; Noble-Haeusslein, L.J.; Ferriero, D.M.
Overexpression of glutathione peroxidase protects immature murine neurons from oxidative stress
Dev. Neurosci.
27
169-175
2005
Homo sapiens, Mus musculus
Lei, X.G.; Cheng, W.H.
New roles for an old selenoenzyme: evidence from glutathione peroxidase-1 null and overexpressing mice
J. Nutr.
135
2295-2298
2005
Mus musculus
Esworthy, R.S.; Yang, L.; Frankel, P.H.; Chu, F.F.
Epithelium-specific glutathione peroxidase, Gpx2, is involved in the prevention of intestinal inflammation in selenium-deficient mice
J. Nutr.
135
740-745
2005
Mus musculus
Drevet, J.R.
The antioxidant glutathione peroxidase family and spermatozoa: a complex story
Mol. Cell. Endocrinol.
250
70-79
2006
Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Yang, M.S.; Chan, H.W.; Yu, L.C.
Glutathione peroxidase and glutathione reductase activities are partially responsible for determining the susceptibility of cells to oxidative stress
Toxicology
226
126-130
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Savaskan, N.E.; Ufer, C.; Kuehn, H.; Borchert, A.
Molecular biology of glutathione peroxidase 4: from genomic structure to developmental expression and neural function
Biol. Chem.
388
1007-1017
2007
Mus musculus (Q5XJZ8)
Chrissobolis, S.; Didion, S.P.; Kinzenbaw, D.A.; Schrader, L.I.; Dayal, S.; Lentz, S.R.; Faraci, F.M.
Glutathione peroxidase-1 plays a major role in protecting against angiotensin II-induced vascular dysfunction
Hypertension
51
872-877
2008
Mus musculus
Banning, A.; Kipp, A.; Schmitmeier, S.; Loewinger, M.; Florian, S.; Krehl, S.; Thalmann, S.; Thierbach, R.; Steinberg, P.; Brigelius-Flohe, R.
Glutathione peroxidase 2 inhibits cyclooxygenase-2-mediated migration and invasion of HT-29 adenocarcinoma cells but supports their growth as tumors in nude mice
Cancer Res.
68
9746-9753
2008
Mus musculus
Yang, W.H.; Park, S.Y.; Ji, S.; Kang, J.G.; Kim, J.-E.; Song, H.; Mook-Jung, I.; Choe, K.-M.; Cho, J.W.
O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation
Biochem. Biophys. Res. Commun.
391
756-761
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Franco, J.L.; Posser, T.; Dunkley, P.R.; Dickson, P.W.; Mattos, J.J.; Martins, R.; Bainy, A.C.; Marques, M.R.; Dafre, A.L.; Farina, M.
Methylmercury neurotoxicity is associated with inhibition of the antioxidant enzyme glutathione peroxidase
Free Radic. Biol. Med.
47
449-457
2009
Homo sapiens, Mus musculus
Razygraev, A.; Yushina, A.; Titovich, I.
A method of measuring glutathione peroxidase activity in murine brain in pharmacological experiments
Bull. Exp. Biol. Med.
165
292-295
2018
Mus musculus
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