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Information on EC 1.11.1.9 - glutathione peroxidase and Organism(s) Rattus norvegicus and UniProt Accession P83645

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.9 glutathione peroxidase
IUBMB 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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This record set is specific for:
Rattus norvegicus
UNIPROT: P83645
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathione peroxidase-2
-
6P229
-
-
-
-
ARMEP24
-
-
-
-
AtGPX1
-
-
-
-
c-GPx4
-
cytosolic isozyme
Cellular glutathione peroxidase
-
-
-
-
Cuticular glycoprotein GP29
-
-
-
-
DI29
-
-
-
-
EGLP
-
-
-
-
Epididymis-specific glutathione peroxidase-like protein
-
-
-
-
Extracellular glutathione peroxidase
-
-
-
-
Gastrointestinal glutathione peroxidase
-
-
-
-
glutathione peroxidase 1
-
-
glutathione peroxidase-1
-
glutathione peroxidase-2
-
-
glutathione peroxidase-4
-
-
GP30
-
-
-
-
GPRP
-
-
-
-
GSH peroxidase
GSHPx-GI
-
-
-
-
m-GPx4
-
mitochondrial isozyme
Major androgen-regulated protein
-
-
-
-
Major surface antigen GP29
-
-
-
-
n-GPx4
-
nuclear isozyme
Nt-SubC08
-
-
-
-
Odorant-metabolizing protein RY2D1
-
-
-
-
peroxidase, glutathione
-
-
-
-
phospholipid hydroperoxide glutathione peroxidase, nuclear form
-
n-PHGPx
reduced glutathione peroxidase
-
-
-
-
Salt-associated protein
-
-
-
-
selenium-glutathione peroxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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 hide
9013-66-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tert-butylhydroperoxide + GSH
?
show the reaction diagram
-
-
-
?
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
arachidonic acid 15-hydroperoxide + GSH
15-hydroxyarachidonic acid + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 5alpha-hydroperoxide + GSH
5alpha-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 7alpha-hydroperoxide + GSH
7alpha-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 7beta-hydroperoxide + GSH
7beta-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
linoleic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
lipid peroxide + GSH
? + GSSG
show the reaction diagram
-
-
-
-
?
protamine + H2O2
?
show the reaction diagram
-
snGPx acts as a protamine cysteine thiol peroxidase
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
H2O2 + GSH
H2O + GSSG
show the reaction diagram
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
selenoprotein, selenium is necessary for activity
selenium
additional information
-
selenium, zinc and tellurium have no stimulatory effect on glutathione peroxidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
diethyldithiocarbamate
-
significant inhibition of selenium-dependent enzyme after intraperitoneal injection of rats with diethyldithiocarbamate, which returns to normal at 48 h after administration of injection. It is possible that inhibition of superoxide dismutase by diethyldithiocarbamate leads to accumulation of superoxide anion which in turn inactivates selenium-dependent glutathione peroxidase by its reaction with slenium at the active site of the enzyme
iodoacetamide
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
Mercaptosuccinate
-
-
NADPH
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
tellurium
-
a decrease in specific activity is seen after combined treatment with zinc (515 mg/l) and tellurium (9.4 mg/l), but not with tellurium alone
Zn2+
-
a decrease in specific activity is seen after combined treatment with zinc (515 mg/l) and tellurium (9.4 mg/l), but not with Zn2+ alone
additional information
-
administration of lead acetate evokes decrease of GPx activity in the kidney of both male and female rats, GPx activity decreases only in male hearts
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hyperglycemia
-
increased GPX1 activity in rat VSM cell. When cells are exposed to high glucose (25 mM) for 48 h, GPX1 activity is 2.5fold greater than in cells grown in normal glucose (5 mM), while the GPX1 expression levels are the same
-
Selenite
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
cholesterol 5alpha-hydroperoxide
-
-
0.011
cholesterol 7alpha-hydroperoxide
-
-
0.003
cholesterol 7beta-hydroperoxide
-
-
0.144
cumene hydroperoxide
-
-
0.033
GSH
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25°C
0.208
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.013
-
crude enzyme, at 25°C
0.07
-
cholesterol 5alpha-hydroperoxide
0.1
-
cholesterol 7beta-hydroperoxide
0.18
-
cholesterol 7alpha-hydroperoxide
1.462
-
after 112.46fold purification, at 25°C
402
-
linolenic acid hydroperoxide
408
-
linoleic acid hydroperoxide
472
-
cumene hydroperoxide
511
-
arachidonic acid 15-hydroperoxide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
less than 20% of maximal activity below
7.2 - 7.6
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
vascular smooth muscles cell
Manually annotated by BRENDA team
-
L6 myoblast
Manually annotated by BRENDA team
-
the intrinsically low level of Gpx activity in the islets sets up the beta cell as an organelle particularly susceptible to oxidative stress secondary to high levels of glucose. Adenoviral overexpression of Gpx increases Gpx activity and protects islets against adverse effects of ribose
Manually annotated by BRENDA team
additional information
-
glial cells are devoid of GPx4
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
presence of 5% O2 improves the glutathione peroxidase activity, p110-PI3K/Thr308-Akt pathway and differentiation while 1% O2 decreases all these parameters compared to 21% O2. N-acetylcysteine (0.5 mM) can prevent the deleterious effects of hypoxia (1% O2) on the L6 myoblast proliferation and enhances the myoblast differentiation when exposed to 21% O2
physiological function
-
anti-oxidant enzyme, essential for cell survival during oxidative stress
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPX2_RAT
190
0
22014
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
SDS-PAGE, truncated and active form of snGPx produced by cleavage at the N-terminal end
34000
-
SDS-PAGE, inactive full-length enzyme
75000 - 85500
88000
-
Toyopearl HW-65 column chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
GPX5
homotetramer
-
alpha4, 4 * 17000-20000, SDS-PAGE, amino acid composition
monomer
-
GPX4
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8
-
a decrease in pH to 6.8 or an increase to 8.0 drastically suppresses the enzyme activity, since at these pH values, glutathione peroxidase becomes unstable
695719
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 25
-
freezing the preparation with subsequent thawing with a gradual increase in temperature from 0°C to 25°C causes a 75% loss of the enzyme activity compared to the initial level
30 - 70
-
glutathione peroxidase activity is retained after incubation at 30°C for 3.5 h and at 40°C for 1.5 h, an increase in the incubation temperature to 50°C and 70°C leads to inactivation of the enzyme within 1 h and 40 min, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilization by glutathione or dithiothreitol
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
-
in the presence of glycerol, the enzyme activity decreases by 40% of the initial value if the enzyme is stored at 0-4°C for 24 h and by 90% if the enzyme is frozen
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM phosphate buffer, pH 7.0, 1 mM EDTA, 0.1 M NaCl, 50% glycerol
-
0-4°C, 50 mM potassium phosphate buffer (pH 7.4), 24 h, no loss of activity
-
4°C, 1 month, less than 50% loss of activity
-
frozen, 1 mM dithiothreitol, 3 months stable, or 2 mM glutathione, 1 month, 15-22% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, Sephadex G-25 gel filtration, and Toyopearl HW-65 column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a selenium deficient diet decreases glutathione reductase activity
-
feeding selenium-enriched Agaricus bisporus (0.001 mg Se/g feed) increases expression and activity of glutathione peroxidase-1 in rat colon by 1.65fold
feeding selenium-enriched Agaricus bisporus (0.001 mg Se/g feed)increases expression of glutathione peroxidase-2 in rat colon by 2.3fold
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
activity is important in predicting tissue redox state
medicine
-
the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, M.; Iwami, K.; Yasumoto, K.
Purification and immunochemical analysis of rat liver glutathione peroxidase
Agric. Biol. Chem.
46
41-46
1982
Rattus norvegicus
-
Manually annotated by BRENDA team
Yoshimura, S.; Komatsu, N.; Watanabe, K.
Purification and immunohistochemical localization of rat liver glutathione peroxidase
Biochim. Biophys. Acta
621
130-137
1980
Rattus norvegicus
Manually annotated by BRENDA team
Nakamura, W.; Hosoda, S.; Hayashi, K.
Purification and properties of rat liver glutathione peroxidase
Biochim. Biophys. Acta
358
251-261
1974
Rattus norvegicus
-
Manually annotated by BRENDA team
Splittgerber, A.G.; Tappel, A.L.
Steady state and pre-steady state kinetic properties of rat liver selenium-glutathione peroxidase
J. Biol. Chem.
254
9807-9813
1979
Rattus norvegicus
Manually annotated by BRENDA team
Zakowski, J.J.; Tappel, A.L.
Purification and properties of rat liver mitochondrial glutathione peroxidase
Biochim. Biophys. Acta
526
65-76
1978
Rattus norvegicus
Manually annotated by BRENDA team
Stults, F.H.; Forstrom, J.W.; Chiu, D.T.Y.; Tappel, A.L.
Rat liver glutathione peroxidase: purification and study of multiple forms
Arch. Biochem. Biophys.
183
490-497
1977
Rattus norvegicus
Manually annotated by BRENDA team
Chiu, D.T.Y.; Stults, F.H.; Tappel, A.L
Purification and properties of rat lung soluble glutathione peroxidase
Biochim. Biophys. Acta
445
558-566
1976
Rattus norvegicus
Manually annotated by BRENDA team
Hiratsuka, A.; Yamane, H.; Yamazaki, S.; Ozawa, N.; Watabe, T.
Subunit Ya-specific glutathione peroxidase activity toward cholesterol 7-hydroperoxides of glutathione S-transferases in cytosols from rat liver and skin
J. Biol. Chem.
272
4763-4769
1997
Rattus norvegicus
Manually annotated by BRENDA team
Marinho, H.S.; Antunes, F.; Pinto, R.E.
Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides
Free Radic. Biol. Med.
22
871-883
1997
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Rogers, L.K.; Gupta, S.; Welty, S.E.; Hansen, T.N.; Smith, C.V.
Nuclear and nucleolar glutathione reductase, peroxidase, and transferase activities in livers of male and female Fischer-344 Rats
Toxicol. Sci.
69
279-285
2002
Rattus norvegicus
Manually annotated by BRENDA team
Garberg, P.; Engman, L.; Tolmachev, V.; Lundqvist, H.; Gerdes, R.G.; Cotgreave, I.A.
Binding of tellurium to hepatocellular selenoproteins during incubation with inorganic tellurite: consequences for the activity of selenium-dependent glutathione peroxidase
Int. J. Biochem. Cell Biol.
31
291-301
1999
Rattus norvegicus
Manually annotated by BRENDA team
Singh, A.K.; Dhaunsi, G.S.; Gupta, M.P.; Orak, J.K.; Asayama, K.; Singh, I.
Demonstration of glutathione peroxidase in rat liver peroxisomes and its intraorganellar distribution
Arch. Biochem. Biophys.
315
331-338
1994
Rattus norvegicus
Manually annotated by BRENDA team
Sindhu, R.K.; Ehdaie, A.; Farmand, F.; Dhaliwal, K.K.; Nguyen, T.; Zhan, C.D.; Roberts, C.K.; Vaziri, N.D.
Expression of catalase and glutathione peroxidase in renal insufficiency
Biochim. Biophys. Acta
1743
86-92
2005
Rattus norvegicus
Manually annotated by BRENDA team
Ren, X.; Jemth, P.; Board, P.G.; Luo, G.; Mannervik, B.; Liu, J.; Zhang, K.; Shen, J.
A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase
Chem. Biol.
9
789-794
2002
Rattus norvegicus
Manually annotated by BRENDA team
Antunes, F.; Han, D.; Cadenas, E.
Relative contributions of heart mitochondria glutathione peroxidase and catalase to H(2)O(2) detoxification in in vivo conditions
Free Radic. Biol. Med.
33
1260-1267
2002
Rattus norvegicus
Manually annotated by BRENDA team
Prabhu, H.R.
In vivo inhibition of selenium dependent glutathione peroxidase and superoxide dismutase in rats by diethyldithiocarbamate
Indian J. Exp. Biol.
40
258-261
2002
Rattus norvegicus
Manually annotated by BRENDA team
Tanaka, Y.; Tran, P.O.; Harmon, J.; Robertson, R.P.
A role for glutathione peroxidase in protecting pancreatic beta cells against oxidative stress in a model of glucose toxicity
Proc. Natl. Acad. Sci. USA
99
12363-12368
2002
Rattus norvegicus
Manually annotated by BRENDA team
Drew, J.E.; Farquharson, A.J.; Arthur, J.R.; Morrice, P.C.; Duthie, G.G.
Novel sites of cytosolic glutathione peroxidase expression in colon
FEBS Lett.
579
6135-6139
2005
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bertelsmann, H.; Kuehbacher, M.; Weseloh, G.; Kyriakopoulos, A.; Behne, D.
Sperm nuclei glutathione peroxidases and their occurrence in animal species with cysteine-containing protamines
Biochim. Biophys. Acta
1770
1459-1467
2007
Equus caballus, Homo sapiens, no activity in Gallus gallus, Rattus norvegicus, no activity in Onchorhynchus mykiss
Manually annotated by BRENDA team
Eybl, V.; Kotyzova, D.; Sykora, J.; Topolcan, O.; Pikner, R.; Mihaljevic, M.; Brtko, J.; Glattre, E.
Effects of selenium and tellurium on the activity of selenoenzymes glutathione peroxidase and type I iodothyronine deiodinase, trace element thyroid level, and thyroid hormone status in rats
Biol. Trace Elem. Res.
117
105-114
2007
Rattus norvegicus
Manually annotated by BRENDA team
Bartel, J.; Bartz, T.; Wolf, C.; Charkiewicz, E.; Kuhbacher, M.; Pohl, T.; Kyriakopoulos, A.
Activity of the glutathione peroxidase-2. Differences in the selenium-dependent expression between colon and small intestine
Cancer Genomics Proteomics
4
369-372
2007
Rattus norvegicus (P83645)
Manually annotated by BRENDA team
Robertson, R.P.; Harmon, J.S.
Pancreatic islet beta-cell and oxidative stress: the importance of glutathione peroxidase
FEBS Lett.
581
3743-3748
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Savaskan, N.E.; Borchert, A.; Braeuer, A.U.; Kuhn, H.
Role for glutathione peroxidase-4 in brain development and neuronal apoptosis: specific induction of enzyme expression in reactive astrocytes following brain injury
Free Radic. Biol. Med.
43
191-201
2007
Rattus norvegicus
Manually annotated by BRENDA team
Thirunavukkarasu, C.; Premkumar, K.; Sheriff, A.K.; Sakthisekaran, D.
Sodium selenite enhances glutathione peroxidase activity and DNA strand breaks in hepatoma induced by N-nitrosodiethylamine and promoted by phenobarbital
Mol. Cell. Biochem.
310
129-139
2008
Rattus norvegicus
Manually annotated by BRENDA team
Sobekova, A.; Holovska, K.; Lenartova, V.; Legath, J.; Javorsky, P.
The alteration of glutathione peroxidase activity in rat organs after lead exposure
Acta Physiol. Hung.
96
37-44
2009
Rattus norvegicus
Manually annotated by BRENDA team
Shulgin, K.; Popova, T.; Rakhmanova, T.
Isolation and purification of glutathione peroxidase
Appl. Biochem. Microbiol.
44
247-250
2008
Rattus norvegicus
-
Manually annotated by BRENDA team
Gallo, G.; Martino, G.
Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats
Reprod. Biol. Endocrinol.
7
7-7
2009
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Maseko, T.; Howell, K.; Dunshea, F.; Ng, K.
Selenium-enriched Agaricus bisporus increases expression and activity of glutathione peroxidase-1 and expression of glutathione peroxidase-2 in rat colon
Food Chem.
146
327-333
2014
Rattus norvegicus, Rattus norvegicus (P04041)
Manually annotated by BRENDA team
Nogales, F.; Ojeda, M.L.; Fenutria, M.; Murillo, M.L.; Carreras, O.
Role of selenium and glutathione peroxidase on development, growth, and oxidative balance in rat offspring
Reproduction
146
659-667
2013
Rattus norvegicus
Manually annotated by BRENDA team
Hidalgo, M.; Marchant, D.; Quidu, P.; Youcef-Ali, K.; Richalet, J.P.; Beaudry, M.; Besse, S.; Launay, T.
Oxygen modulates the glutathione peroxidase activity during the L6 myoblast early differentiation process
Cell. Physiol. Biochem.
33
67-77
2014
Rattus norvegicus
Manually annotated by BRENDA team