Information on EC 1.11.1.9 - glutathione peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.9
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RECOMMENDED NAME
GeneOntology No.
glutathione peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 glutathione + H2O2 = glutathione disulfide + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arachidonic acid metabolism
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Arachidonic acid metabolism
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Glutathione metabolism
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glutathione-peroxide redox reactions
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reactive oxygen species degradation
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aloa barbadensis Miller
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-
Manually annotated by BRENDA team
ecotype Columbia
SwissProt
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IFO 0895
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-
Manually annotated by BRENDA team
zebra-seabream
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-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
RD
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Greasyback shrimp
UniProt
Manually annotated by BRENDA team
no activity in Bos taurus
-
-
-
Manually annotated by BRENDA team
no activity in Gallus gallus
-
-
-
Manually annotated by BRENDA team
no activity in Onchorhynchus mykiss
-
-
-
Manually annotated by BRENDA team
no activity in plants
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ridgetail white prawn
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain YPH499
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
organism exposed to Aroclor 1254
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
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
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
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
2-phenylpropan-2-ol + GSSG + H2O
show the reaction diagram
cumene hydroperoxide + GSH
?
show the reaction diagram
cumene hydroperoxide + H2O2
?
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 + cumene peroxide
?
show the reaction diagram
H2O2 + GSH
H2O + GSSG
show the reaction diagram
H2O2 + ROOH
H2O + ROH
show the reaction diagram
-
-
-
-
?
H2O2 + thioredoxin
H2O + ?
show the reaction diagram
-
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
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
phosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
in the absence of phospholipase A2
-
-
?
phosphatidylcholine hydroperoxide + H2O
?
show the reaction diagram
-
phosphatidylcholine hydroperoxide is a substrate after being previously incubated with 51 mU of phospholipase A2 for 10 min
-
-
?
phosphatidylcholine hydroperoxide + thioredoxin
?
show the reaction diagram
-
-
-
?
protamine + H2O2
?
show the reaction diagram
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
tert-butylhydroperoxide + 3-carboxy-4-nitrobenzenethiol
?
show the reaction diagram
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
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
cadmium
in liver, by 24 h, exposure to alow dose of Cd causes 13% loss of Gpx4a expression. At higher dose, Cd leads to 40% decrease in Gpx4a expression. Longer exposure periods cause about 20% loss of liver Gpx4a expression by low Cd dose; olfactory isoform Gpx4b mRNA expression is not extensively modulated by presence of cadmium ions. In liver, by 24 h, exposure to alow dose of Cd causes 18% loss of Gpx4b expression. At higher dose, Cd leads to 37% decrease in Gpx4b expression. Longer exposure periods cause about 22% loss of liver Gpx4b expression by low Cd dose, whereas at higher Cd exposures, a 33% loss in Gpx4b expression is observed
Mn2+
-
221% relative activity
Se
-
selenium-dependent enzyme
selenium
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-deoxyglucosone
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-
5,5'-dithiobis(2-nitrobenzoic acid)
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-
adenosine
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inhibition probably due to inhibition of glutathione reductase in coupled assay
Ag+
-
-
alpha-Mercaptopropionylglycine
-
-
Chloroacetate
-
-
CN-
-
no inhibition if simultaneously incubated with 2-mercaptoethanol, glutathione or dithiothreitol
cysteine
-
GPx-1 is inhibited by 0.5 mM cysteine
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
docosahexaenoic acid
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0.1 mM reduces the level of protein expression of GPx-4 by at least 50%
glutathione
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Glyoxal
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Gold(I)-thioglucose
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homocysteine
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GPx-1 is inhibited by 0.05-0.5 mM homocysteine, especially at low glutathione concentrations
iodoacetamide
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inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
Mercaptosuccinate
methylglyoxal
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Arg184 and Arg185, located in the glutathione binding site of the enzyme are irreversibly modified by treatment with methylglyoxal
NADPH
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inhibition probably due to inhibition of glutathione reductase in coupled assay
p-chloromercuribenzoate
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Penicillamine
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Phenylglyoxal
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Polyvalent anions
S-nitro-N-acetyl-DL-penicillamine
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tellurium
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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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
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cysteine increases activity at low glutathione concentrations
etoposide
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activates p53, wich induces the expression of glutathione peroxidase
genistein
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hyperglycemia
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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
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reduced glutathione
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activated by 2 to 6 mM
Selenite
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-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
cholesterol 5alpha-hydroperoxide
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0.011
cholesterol 7alpha-hydroperoxide
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-
0.003
cholesterol 7beta-hydroperoxide
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-
0.006 - 7.8
cumene hydroperoxide
0.09 - 0.42
cumene peroxide
1.33
glutathione
-
-
0.033 - 11.1
GSH
0.00229 - 19.08
H2O2
0.026 - 9.7
L-alpha-phosphatidylcholine hydroperoxide
0.007 - 3.8
linolenic acid hydroperoxide
0.059 - 7.9
tert-butyl hydroperoxide
0.024
tert-butylhydroperoxide
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 35.78
cumene peroxide
14.48 - 408.3
GSH
5.7 - 670
H2O2
25.3
tert-butyl hydroperoxide
Lucilia cuprina
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27C, pH 7.0, activity of seleno-glutathione transferase
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.013
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crude enzyme, at 25C
0.07
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cholesterol 5alpha-hydroperoxide
0.1
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cholesterol 7beta-hydroperoxide
0.13
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linolenic acid hydroperoxide
0.16
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L-alpha-phosphatidylcholine hydroperoxide
0.18
-
cholesterol 7alpha-hydroperoxide
0.24
mutant enzyme N136A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
0.4
mutant enzyme N136H, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
1.462
-
after 112.46fold purification, at 25C
4.29
mutant enzyme N40A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
5
-
Saos-2
5.5
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Saos-2 treated with etoposide
5.81
mutant enzyme C74A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
6.7
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U2-OS
11.9
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U2-OS treated with etoposide
14.38
wild type enzyme, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
120
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subcellular fractionation
281
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outer mitochondrial membrane
337
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inner mitochondrial membrane
350
-
-
402
-
linolenic acid hydroperoxide
408
-
linoleic acid hydroperoxide
472
-
cumene hydroperoxide
511
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arachidonic acid 15-hydroperoxide
1300
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plasma membrane
1407
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
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8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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less than 20% of maximal activity below
7.2 - 7.6
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7.5 - 9
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pH 7.5: about 45% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
reaction with cumene hydroperoxide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
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25C: about 40% of maximal activity, 45C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
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calculated from amino acid sequence
7.6
isoelectric focusing
7.7
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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pGPx is expressed during bovine adipocyte differentiation, transcriptional control of pGPx in cattle might be carried out by C/EBPdelta
Manually annotated by BRENDA team
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intraperitoneal fat, high expression of pGPx
Manually annotated by BRENDA team
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GPx1 is highly expressed in adrenal glands
Manually annotated by BRENDA team
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GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
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GPx is detected on the membranes of vacuoles situated in the gland's epithelial cells
Manually annotated by BRENDA team
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human endothelial cell line Ea.hy926
Manually annotated by BRENDA team
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extremely highly expressed in early embryos
Manually annotated by BRENDA team
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GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
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human primary pulmonary artery endothelial cells
Manually annotated by BRENDA team
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a non-transformed lung epithelial cell line
Manually annotated by BRENDA team
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GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
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low expression
Manually annotated by BRENDA team
highly expressed in pre-vitellogenic and mid-vitellogenic oocytes, while no expression is detected in late-vitellogenic oocytes
Manually annotated by BRENDA team
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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
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intraperitoneal fat, high expression of pGPx
Manually annotated by BRENDA team
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GPx3 is widely inactivated in prostate cancer cells
Manually annotated by BRENDA team
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain; highest mRNA expression in pyloric ceca, followed by brain, heart and liver
Manually annotated by BRENDA team
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GPx is detected in the tubulo-alveolar structures of the gland's parenchyma, in the apical part of secreting epithelial cells of the gland's alveoli, and in the vascular endothelium of blood vessels found in interstitial connective tissue
Manually annotated by BRENDA team
isozyme n-GPx-4 is specifically expressed in late spermatocytes
Manually annotated by BRENDA team
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GPx3 is exclusively expressed in thyrocytes
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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-
Manually annotated by BRENDA team
full-length fusion protein with enhanced green fluorescent protein is localised to the trans-Golgi.The secretion of the enzyme into the culture medium requires an amino-terminal signal peptide
Manually annotated by BRENDA team
additional information