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Information on EC 1.11.1.9 - glutathione peroxidase and Organism(s) Bos taurus
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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: Bos taurus
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
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
-
-
-
-
Cellular 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
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cholesterol 7beta-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
specificity for donor-substrate: free amino group near the SH group inhibits the reaction, free alpha-carboxylic group of glutamic acid residue in glutathione analogs increases reaction rate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
pregnenolone 17alpha-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
thymine hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
gamma-glutamyl-L-cysteine-methyl ester has 26% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
gamma-glutamyl-L-cysteine-methylester has 26% of glutathione activity
-
-
?
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
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cholesterol 7beta-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
specificity for donor-substrate: free amino group near the SH group inhibits the reaction, free alpha-carboxylic group of glutamic acid residue in glutathione analogs increases reaction rate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
pregnenolone 17alpha-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
thymine hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
gamma-glutamyl-L-cysteine-methylester has 26% of glutathione activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
homocysteine
-
GPx-1 is inhibited by 0.05-0.5 mM homocysteine, especially at low glutathione concentrations
methylglyoxal
-
Arg184 and Arg185, located in the glutathione binding site of the enzyme are irreversibly modified by treatment with methylglyoxal
additional information
-
dicarbonyl compounds directly inactivate the enzyme, resulting in an increase in intracellular peroxides, which are responsible for oxidative cellular damage
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
pGPx is expressed during bovine adipocyte differentiation, transcriptional control of pGPx in cattle might be carried out by C/EBPdelta
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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_BOVIN
209
1
23983
Swiss-Prot
Secretory Pathway (Reliability: 3)
GPX7_BOVIN
186
0
20908
Swiss-Prot
Secretory Pathway (Reliability: 2)
GPX1_BOVIN
205
0
22659
Swiss-Prot
Mitochondrion (Reliability: 3)
GPX3_BOVIN
226
0
25663
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21510
75000 - 85500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol restores about 50% of the S-nitro-N-acetyl-DL-penicillamine inhibited enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity in the serum of late-lactation cows is 2fold higher compared to dry cows and 4fold higher than in first-calving heifers and multiparous cows in early lactation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wendel, A.
Glutathione peroxidase
Methods Enzymol.
77
325-333
1981
Bos taurus, Mammalia, no activity in plants
Ladenstein, R.; Epp, O.; Bartels, K.; Jones, A.; Huber, R.
Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 A resolution
J. Mol. Biol.
134
199-218
1979
Bos taurus
Gunzler, W.A.; Steffens, G.J.; Grossmann, A.; Kim, S.M.A.; tting, F.; Wendel, A.; Flohe, L.
The amino-acid sequence of bovine glutathione peroxidase
Hoppe-Seyler's Z. Physiol. Chem.
365
195-212
1984
Bos taurus
Epp, O.; Ladenstein, R.; Wendel, A.
The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
Eur. J. Biochem.
133
51-69
1983
Bos taurus
Flohe, L.; Eisele, B.; Wendel, A.
Glutathione peroxidase. I. Isolation and determinations of molecular weight
Hoppe-Seyler's Z. Physiol. Chem.
352
151-158
1971
Bos taurus
Flohe, L.; Gunzler, W.; Jung, G.; Schaich, E.; Schneider, F.
Glutathione peroxidase. II. Substrate specificity and inhibitory effects of substrate analogues
Hoppe-Seyler's Z. Physiol. Chem.
352
159-169
1971
Bos taurus
Asahi, M.; Fujii, J.; Suzuki, K.; Seo, H.G.; Kuzuya, T.; Hori, M.; Tada, M.; Fujii, S.; Taniguchi, N.
Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity
J. Biol. Chem.
270
21035-21039
1995
Bos taurus
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
Park, Y.S.; Koh, Y.H.; Takahashi, M.; Miyamoto, Y.; Suzuki, K.; Dohmae, N.; Takio, K.; Honke, K.; Taniguchi, N.
Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185
Free Radic. Res.
37
205-211
2003
Bos taurus
Yamasaki, T.; Tahara, K.; Takano, S.; Inoue-Murayama, M.; Rose, M.T.; Minashima, T.; Aso, H.; Ito, S.
Mechanism of plasma glutathione peroxidase production in bovine adipocytes
Cell Tissue Res.
326
139-147
2006
Bos taurus
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
Vaisberg, C.N.; Jelezarsky, L.V.; Dishlianova, B.; Chaushev, T.A.
Activity, substrate detection and immunolocalization of glutathione peroxidase (GPx) in bovine reproductive organs and semen
Theriogenology
64
416-428
2005
Bos taurus
Ballihaut, G.; Mounicou, S.; Lobinski, R.
Multitechnique mass-spectrometric approach for the detection of bovine glutathione peroxidase selenoprotein: focus on the selenopeptide
Anal. Bioanal. Chem.
388
585-591
2007
Bos taurus (P00435), Bos taurus
Durmaz, A.; Dikmen, N.
Homocysteine effects on cellular glutathione peroxidase (GPx-1) activity under in vitro conditions
J. Enzyme Inhib. Med. Chem.
22
733-738
2007
Bos taurus
Pilarczyk, B.; Jankowiak, D.; Tomza-Marciniak, A.; Pilarczyk, R.; Sablik, P.; Drozd, R.; Tylkowska, A.; Skolmowska, M.
Selenium concentration and glutathione peroxidase (GSH-Px) activity in serum of cows at different stages of lactation
Biol. Trace Elem. Res.
147
91-96
2012
Bos taurus
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