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1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
1-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl)-L-3-phosphatidylcholine + 2 GSH
1-palmitoyl-2-(13-hydroxy-cis-9, trans-11-octadecadienoyl)-L-3-phosphatidylcholine + GSSG + H2O
-
-
-
?
2 glutathione + cumene hydroperoxide
glutathione disulfide + 2-phenylpropan-2-ol + H2O
2 glutathione + H2O2
glutathione disulfide + 2 H2O
2 glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + tert-butyl alcohol + H2O
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
arachidonic acid 15-hydroperoxide + GSH
15-hydroxyarachidonic acid + GSSG
-
-
-
-
?
cholesterol 5alpha-hydroperoxide + GSH
5alpha-hydroxycholesterol + GSSG
-
-
-
-
?
cholesterol 7alpha-hydroperoxide + GSH
7alpha-hydroxycholesterol + GSSG
-
-
-
-
?
cholesterol 7beta-hydroperoxide + GSH
7beta-hydroxycholesterol + GSSG
-
-
-
-
?
cumene hydroperoxide + 2 2-nitro-5-sulfanylbenzoic acid
2-phenylpropan-2-ol + 3,3'-disulfanediylbis(6-nitrobenzoic acid) + H2O
-
-
-
-
?
cumene hydroperoxide + 2 4-nitrobenzenethiol
2-phenylpropan-2-ol + 1,1'-disulfanediylbis(4-nitrobenzene) + H2O
-
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
cumene hydroperoxide + 2-nitro-5-sulfanylbenzoic acid
2-phenylpropan-2-ol + 3,3'-disulfanediylbis(6-nitrobenzoic acid) + H2O
-
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG + H2O
cumene hydroperoxide + GSH
?
cumene hydroperoxide + H2O2
?
-
-
-
-
?
glutathione + cumene hydroperoxide
?
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
glutathione + ROOH
glutathione disulfide + ROH + H2O
glutathione + tert-butyl hydroperoxide
?
-
-
-
?
glutathione disulfide + 2 H2O
2 glutathione + H2O2
-
-
-
-
r
H2O2 + 2 GSH
H2O + GSSG
-
-
-
-
?
H2O2 + ROOH
H2O + ROH
-
-
-
-
?
H2O2 + thioredoxin
H2O + ?
-
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
L-cysteine + + H2O2
cystin + 2 H2O
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
linolenic acid hydroperoxide + GSH
?
lipid peroxide + GSH
? + GSSG
phosphatidylcholine hydroperoxide + GSH
?
-
in the absence of phospholipase A2
-
-
?
phosphatidylcholine hydroperoxide + H2O
?
-
phosphatidylcholine hydroperoxide is a substrate after being previously incubated with 51 mU of phospholipase A2 for 10 min
-
-
?
phosphatidylcholine hydroperoxide + thioredoxin
?
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
tert-butylhydroperoxide + 3-carboxy-4-nitrobenzenethiol
?
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
additional information
?
-
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
?
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
?
2 glutathione + cumene hydroperoxide
glutathione disulfide + 2-phenylpropan-2-ol + H2O
-
83% of the activity with H2O2
-
-
?
2 glutathione + cumene hydroperoxide
glutathione disulfide + 2-phenylpropan-2-ol + H2O
-
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
-
r
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
-
r
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + tert-butyl alcohol + H2O
-
87% of the activity with H2O2
-
-
?
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + tert-butyl alcohol + H2O
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
?
cumene hydroperoxide + 2 GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
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
-
peroxidized DNA
-
-
?
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
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ROOH can be: aliphatic or aromatic peroxide or H2O2
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
hydroperoxyarachidonate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
peroxidized DNA
-
-
?
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
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
reduction of hydroperoxides increases with hydrophobicity of substrates
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
menthane hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
diisopropyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
lauryl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
dithiothreitol has 10% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
H2O2 + cumene peroxide
?
-
activity of seleno-glutathione transferase
-
-
?
H2O2 + cumene peroxide
?
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
activity of seleno-glutathione transferase
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
instead of tert-butyl hydroperoxide
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
396635, 396636, 396638, 396645, 685333, 686738, 686868, 688957, 695410, 695719, 701160 -
-
?
H2O2 + GSH
H2O + GSSG
-
the enzyme protects cells against oxidative damage
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
-
not hydrogen peroxide
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
r
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
lipid peroxide + GSH
? + GSSG
-
-
-
-
?
lipid peroxide + GSH
? + GSSG
-
-
-
-
?
protamine + H2O2
?
-
snGPx acts as a protamine cysteine thiol peroxidase
-
-
?
protamine + H2O2
?
-
snGPx acts as a protamine cysteine thiol peroxidase
-
-
?
protamine + H2O2
?
-
snGPx acts as a protamine cysteine thiol peroxidase
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
activity of seleno-glutathione transferase
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
-
-
-
?
additional information
?
-
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
?
additional information
?
-
-
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
?
additional information
?
-
-
major antioxidant enzyme
-
-
?
additional information
?
-
enzyme shows substrate preference against organic hydroperoxides, such as cumene-OOH and t-butyl-OOH, and low activity against H2O2
-
-
?
additional information
?
-
-
enzyme shows substrate preference against organic hydroperoxides, such as cumene-OOH and t-butyl-OOH, and low activity against H2O2
-
-
?
additional information
?
-
enzyme shows substrate preference against organic hydroperoxides, such as cumene-OOH and t-butyl-OOH, and low activity against H2O2
-
-
?
additional information
?
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
the enzyme does not metabolise H2O2
-
-
?
additional information
?
-
the enzyme does not metabolise H2O2
-
-
?
additional information
?
-
-
the enzyme does not metabolise H2O2
-
-
?
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate. Coupling of GSH with a monosaccharide such as ribose might contribute to the decreased cell GSH and glutathione peroxidase activity observed in diabetics
-
-
?
additional information
?
-
-
the enzyme is uniquely involved in the detoxification of oxidative damage to membrane lipids. It plays a role in vivo in the mechanism of apoptosis induced by oxidative stress that most likely occurs through oxidative damage to mitochondrial phospholipids such as cardiolipin
-
-
?
additional information
?
-
-
upregulation of GPx-1 gene expression in prostate cancer cells bei genistein
-
-
?
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate
-
-
?
additional information
?
-
-
adenosine may protect the cardiovascular system from ischemia/reperfusion injury, in part, by enhancing the expression of the central intracellular antioxidant enzyme, GPx-1
-
-
?
additional information
?
-
-
increased GPx-1 expression in immature cortical neurons of transgenic mice with 200 copies of the human GPx-1 gene confers protection from oxidative stress
-
-
?
additional information
?
-
-
selenium containing glutathione transferase zeta1-1 does also possess glutathione peroxidase activity
-
-
?
additional information
?
-
-
substrate H2O2 is preferred over cumene hydroperoxide and t-butyl hydroperoxide, both isoform Gpx1 and Gpx2
-
-
?
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
-
-
?
additional information
?
-
-
involved in mainenance of the steady state levels of H2O2 in heart mitochondria matrix
-
-
?
additional information
?
-
-
the enzyme plays a critical role in antioxidant defense system by catalyzing detoxification of H2O2 and organic hydroperoxides. Significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
-
-
?
additional information
?
-
-
glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way
-
-
?
additional information
?
-
-
Gpx3 protects glutamine synthetase from non-enzymatic proteolysis
-
-
?
additional information
?
-
-
Gpx3 protects glutamine synthetase from non-enzymatic proteolysis
-
-
?
additional information
?
-
-
compounds N-hydroxy-4-((3-oxobenzo[d][1,2]selenazol-2(3H)-yl)methyl)benzamide and N-hydroxy-4-(1-(3-oxobenzo[d][1,2]selenazol-2(3H)-yl)ethyl)benzamide demonstrate good catalytic peroxidase-like activity, with rate values that are similar to ebselen's value. Compound N-hydroxy-4-((3-oxobenzo[d][1,2]selenazol-2(3H)-yl)methyl)benzamide is a histone deacetylase inhibitor, possessing rapid hydrogen peroxide scavenging activity and good free oxygen radical absorbance capacity
-
-
-
additional information
?
-
-
the enzyme can reduce fatty acid, phospholipid, and short chain organic hydroperoxides utilizing a novel redox cycle in which enzyme activity is linked to the reduction of trypanothione, by glutathione. The activity of TcGPXI can also be linked to trypanothione reduction by an alternative pathway involving thioredoxin-like protein tryparedoxin. Overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
cumene hydroperoxide + GSH
?
glutathione + H2O2
glutathione disulfide + H2O
glutathione + ROOH
glutathione disulfide + ROH + H2O
linolenic acid hydroperoxide + GSH
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
additional information
?
-
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
?
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
cumene hydroperoxide + GSH
?
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
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
-
peroxidized DNA
-
-
?
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
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ROOH can be: aliphatic or aromatic peroxide or H2O2
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
hydroperoxyarachidonate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
peroxidized DNA
-
-
?
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
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
reduction of hydroperoxides increases with hydrophobicity of substrates
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
menthane hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
diisopropyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
lauryl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
dithiothreitol has 10% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
the enzyme protects cells against oxidative damage
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
-
-
-
?
additional information
?
-
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
?
additional information
?
-
-
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
?
additional information
?
-
-
major antioxidant enzyme
-
-
?
additional information
?
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
-
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
?
additional information
?
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
-
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
?
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate. Coupling of GSH with a monosaccharide such as ribose might contribute to the decreased cell GSH and glutathione peroxidase activity observed in diabetics
-
-
?
additional information
?
-
-
the enzyme is uniquely involved in the detoxification of oxidative damage to membrane lipids. It plays a role in vivo in the mechanism of apoptosis induced by oxidative stress that most likely occurs through oxidative damage to mitochondrial phospholipids such as cardiolipin
-
-
?
additional information
?
-
-
upregulation of GPx-1 gene expression in prostate cancer cells bei genistein
-
-
?
additional information
?
-
-
adenosine may protect the cardiovascular system from ischemia/reperfusion injury, in part, by enhancing the expression of the central intracellular antioxidant enzyme, GPx-1
-
-
?
additional information
?
-
-
increased GPx-1 expression in immature cortical neurons of transgenic mice with 200 copies of the human GPx-1 gene confers protection from oxidative stress
-
-
?
additional information
?
-
-
selenium containing glutathione transferase zeta1-1 does also possess glutathione peroxidase activity
-
-
?
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
-
-
?
additional information
?
-
-
involved in mainenance of the steady state levels of H2O2 in heart mitochondria matrix
-
-
?
additional information
?
-
-
the enzyme plays a critical role in antioxidant defense system by catalyzing detoxification of H2O2 and organic hydroperoxides. Significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
-
-
?
additional information
?
-
-
the enzyme can reduce fatty acid, phospholipid, and short chain organic hydroperoxides utilizing a novel redox cycle in which enzyme activity is linked to the reduction of trypanothione, by glutathione. The activity of TcGPXI can also be linked to trypanothione reduction by an alternative pathway involving thioredoxin-like protein tryparedoxin. Overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
2 mM, 23% residual activity
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
6-diazo-5-oxo-L-norleucine
-
20 mM, 60% residual activity
adenosine
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
AlCl3
-
10 mM, 67% residual activity
alpha-Mercaptopropionylglycine
-
-
BaCl2
-
10 mM, 52% residual activity
CaCl2
-
10 mM, 81% residual activity
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
DL-dithiothreitol
-
2 mM, no residual activity
docosahexaenoic acid
-
0.1 mM reduces the level of protein expression of GPx-4 by at least 50%
DTNB
-
20 mM, 46% residual activity
EDTA
-
1 mM, about 40% residual activity, activity is completely restored upon addition of Se+ cations, followed by Na+
Fe2+
-
2 mM, 21% of initial activity
FeCl3
-
10 mM, 68% residual activity
HgCl2
-
10 mM, 61% residual activity
homocysteine
-
GPx-1 is inhibited by 0.05-0.5 mM homocysteine, especially at low glutathione concentrations
hydroxylamine
-
20 mM, 25% residual activity
KCl
-
10 mM, 45% residual activity
MBTH
-
20 mM, 59% residual activity
methylglyoxal
-
Arg184 and Arg185, located in the glutathione binding site of the enzyme are irreversibly modified by treatment with methylglyoxal
MgSO4
-
10 mM, 58% residual activity
NADPH
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
p-chloromercuribenzoate
-
-
Phenanthroline
-
competitive
PMSF
-
20 mM, 59% residual activity
S-nitro-N-acetyl-DL-penicillamine
-
-
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
iodoacetamide
-
competitive
iodoacetamide
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
-
-
iodoacetate
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
-
20 mM, 57% residual activity
Mercaptosuccinate
-
-
O2-
-
-
Polyvalent anions
-
e.g. phosphate, sulfate, maleate
-
Polyvalent anions
-
e.g. phosphate, sulfate, maleate
-
Polyvalent anions
-
e.g. phosphate, sulfate, maleate
-
Polyvalent anions
-
e.g. phosphate, sulfate, maleate
-
Zn2+
-
-
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
-
not: ophthalmic acid
-
additional information
-
dicarbonyl compounds directly inactivate the enzyme, resulting in an increase in intracellular peroxides, which are responsible for oxidative cellular damage
-
additional information
-
not: ophthalmic acid
-
additional information
not inhibitory: potassium cyanide or sodium azide
-
additional information
-
not inhibitory: potassium cyanide or sodium azide
-
additional information
-
for each 1 year increase in age, GPx activity decreases by 0.0029 mmol/min
-
additional information
-
aging decreases expression and activity of glutathione peroxidase-1 in human endothelial progenitor cells, increasing selenium concentration in the cell culture does not affect the protein levels of GPX1, suggesting the reduced GPX1 in old subject's endothelial progenitor cells is selenium independent
-
additional information
-
reduced plasma glutathione peroxidase 3 levels are found in patients with type 2 diabetes mellitus
-
additional information
-
not: ophthalmic acid
-
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
-
additional information
-
not: ophthalmic acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.004
cholesterol 5alpha-hydroperoxide
-
-
0.011
cholesterol 7alpha-hydroperoxide
-
-
0.003
cholesterol 7beta-hydroperoxide
-
-
0.006 - 7.8
cumene hydroperoxide
0.09 - 0.42
cumene peroxide
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
-
-
0.006
cumene hydroperoxide
-
-
0.111
cumene hydroperoxide
-
-
0.144
cumene hydroperoxide
-
-
0.145
cumene hydroperoxide
-
pH 8.0, 30°C
0.26
cumene hydroperoxide
-
-
7.8
cumene hydroperoxide
-
pH 7.5, 25°C
0.09
cumene peroxide
-
25°C, pH 8
0.42
cumene peroxide
-
27°C, pH 7.0, activity of seleno-glutathione transferase
0.022
glutathione
mutant C2S/C78S/C115S/C156S/C202S, presence of 0.03 mM H2O2, pH 7.4, 37°C
0.31
glutathione
mutant C2S/C78S/C115S/C156S/C202S, presence of 0.10 mM H2O2, pH 7.4, 37°C
1.73
glutathione
pH 9.0, 30°C
0.033
GSH
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25°C
0.15
GSH
-
27°C, pH 7.0, reaction with tert-butyl hydroperoxide, activity of seleno-glutathione transferase
0.2
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
0.22
GSH
-
27°C, pH 7.0, reaction with cumene peroxide, activity of seleno-glutathione transferase
0.26
GSH
-
27°C, pH 7.0, reaction with H2O2, activity of seleno-glutathione transferase
0.3
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
0.4
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
2.1
GSH
-
pH 7.5, 25°C, reaction with H2O2
2.6
GSH
-
pH 7.5, 25°C, reaction with cumene hydroperoxide
5.5
GSH
-
pH 7.5, 25°C, reaction with tert-butyl hydroperoxide
5.93
GSH
-
wild type enzyme, in the presence of 0.1 mM H2O2, at 37°C and pH 7.0
7.96
GSH
-
wild type enzyme, in the presence of 0.2 mM H2O2, at 37°C and pH 7.0
9.87
GSH
-
wild type enzyme, in the presence of 0.5 mM H2O2, at 37°C and pH 7.0
11.1
GSH
-
wild type enzyme, in the presence of 1 mM H2O2, at 37°C and pH 7.0
0.00229
H2O2
-
-
0.02
H2O2
mutant C2S/C78S/C115S/C156S/C202S, presence of 3 mM GSH, pH 7.4, 37°C
0.024
H2O2
-
isoform Gpx1, pH 7.0, 25°C
0.049
H2O2
-
isoform Gpx2, pH 7.0, 25°C
0.204
H2O2
-
pH 8.0, 30°C
0.208
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25°C
0.26
H2O2
-
27°C, pH 7.0, activity of seleno-glutathione transferase
0.31
H2O2
mutant C2S/C78S/C115S/C156S/C202S, presence of 10 mM GSH, pH 7.4, 37°C
0.45
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
0.62
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
0.77
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
8.99
H2O2
-
wild type enzyme, in the presence of 0.25 mM GSH, at 37°C and pH 7.0
12.6
H2O2
-
wild type enzyme, in the presence of 0.5 mM GSH, at 37°C and pH 7.0
15.88
H2O2
-
wild type enzyme, in the presence of 1 mM GSH, at 37°C and pH 7.0
19.08
H2O2
-
wild type enzyme, in the presence of 2 mM GSH, at 37°C and pH 7.0
0.026
L-alpha-phosphatidylcholine hydroperoxide
-
-
-
9.7
L-alpha-phosphatidylcholine hydroperoxide
-
-
-
0.007
linolenic acid hydroperoxide
-
-
3.8
linolenic acid hydroperoxide
-
-
0.059
tert-butyl hydroperoxide
-
-
0.09
tert-butyl hydroperoxide
-
25°C, pH 8
0.2088
tert-butyl hydroperoxide
-
-
0.32
tert-butyl hydroperoxide
-
pH 8.0, 30°C
0.91
tert-butyl hydroperoxide
-
27°C, pH 7.0, activity of seleno-glutathione transferase
7.9
tert-butyl hydroperoxide
-
pH 7.5, 25°C
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0.8 - 35.78
cumene peroxide
25.3
tert-butyl hydroperoxide
-
27°C, pH 7.0, activity of seleno-glutathione transferase
0.8
cumene peroxide
-
27°C, pH 7.0, activity of seleno-glutathione transferase
35.78
cumene peroxide
-
27°C, pH 7.0, activity of seleno-glutathione transferase
4.8
glutathione
mutant C2S/C78S/C115S/C156S/C202S, presence of 0.03 mM H2O2, pH 7.4, 37°C
683
glutathione
mutant C2S/C78S/C115S/C156S/C202S, presence of 0.10 mM H2O2, pH 7.4, 37°C
14.48
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
19.5
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
24.5
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C
221.7
GSH
-
wild type enzyme, in the presence of 0.1 mM H2O2, at 37°C and pH 7.0
293.3
GSH
-
wild type enzyme, in the presence of 0.2 mM H2O2, at 37°C and pH 7.0
361.7
GSH
-
wild type enzyme, in the presence of 0.5 mM H2O2, at 37°C and pH 7.0
408.3
GSH
-
wild type enzyme, in the presence of 1 mM H2O2, at 37°C and pH 7.0
4.7
H2O2
mutant C2S/C78S/C115S/C156S/C202S, presence of 3 mM GSH, pH 7.4, 37°C
5.7
H2O2
-
27°C, pH 7.0, activity of seleno-glutathione transferase
10.55
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
16.02
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
20.83
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C
44.03
H2O2
-
27°C, pH 7.0, activity of seleno-glutathione transferase
316.7
H2O2
-
wild type enzyme, in the presence of 0.25 mM GSH, at 37°C and pH 7.0
445
H2O2
-
wild type enzyme, in the presence of 0.5 mM GSH, at 37°C and pH 7.0
560
H2O2
-
wild type enzyme, in the presence of 1 mM GSH, at 37°C and pH 7.0
670
H2O2
-
wild type enzyme, in the presence of 2 mM GSH, at 37°C and pH 7.0
727.8
H2O2
mutant C2S/C78S/C115S/C156S/C202S, presence of 10 mM GSH, pH 7.4, 37°C
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-
-
brenda
-
-
brenda
-
low expression
brenda
-
pGPx is expressed during bovine adipocyte differentiation, transcriptional control of pGPx in cattle might be carried out by C/EBPdelta
brenda
-
intraperitoneal fat, high expression of pGPx
brenda
GPx1 is highly expressed in adrenal glands
brenda
-
almost undetectable
brenda
GPx-3 is detected at very low levels under basal conditions
brenda
-
-
brenda
-
-
brenda
-
brenda
-
GPx is detected on the membranes of vacuoles situated in the gland's epithelial cells
brenda
-
-
brenda
-
-
brenda
-
moderate mRNA level
brenda
-
-
brenda
-
moderate mRNA level
brenda
-
-
brenda
-
-
brenda
-
brenda
-
human endothelial cell line Ea.hy926
brenda
-
primary
brenda
-
-
brenda
-
-
brenda
GPx-2
brenda
-
brenda
GPx-3 is detected at very low levels under basal conditions
brenda
-
-
brenda
-
-
brenda
-
human primary pulmonary artery endothelial cells
brenda
-
a non-transformed lung epithelial cell line
brenda
GPx-3 is detected at very low levels under basal conditions
brenda
restricted to
brenda
-
brenda
-
very high mRNA level
brenda
-
flag leaf, very high mRNA level
brenda
-
brenda
-
-
brenda
-
low expression
brenda
-
-
brenda
-
-
brenda
-
L6 myoblast
brenda
-
very high mRNA level
brenda
GPx-6
brenda
highly expressed in pre-vitellogenic and mid-vitellogenic oocytes, while no expression is detected in late-vitellogenic oocytes
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
intraperitoneal fat, high expression of pGPx
brenda
-
-
brenda
GPx3 is widely inactivated in prostate cancer cells
brenda
-
LNCAP and PC-3
brenda
-
-
brenda
-
moderate mRNA level in immature seed
brenda
-
-
brenda
-
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
brenda
-
-
brenda
-
very high mRNA level
brenda
-
-
brenda
-
-
brenda
isozyme n-GPx-4 is specifically expressed in late spermatocytes
brenda
GPx3 is exclusively expressed in thyrocytes
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
GPX activity was significantly higher in HIV-positive than in HIV-negative subjects. When GPX activity is compared by HIV status and ARTuse, HIV-negative subjects have the lowest median, HIV-positive subjects not taking ART have an intermediate median (11% greater than that of HIV-negative subjects), and HIV-positive subjects taking ART have the highest median (21% higher than that of the HIV-positive subjects not taking ART)
brenda
-
-
brenda
-
highest expression
brenda
-
-
brenda
-
-
brenda
-
activity in brain is much lower than in liver
brenda
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
potential for Gpx1 and Gpx2 redundancy in lymphatic tissue, but not in epithelial cells of the colon crypt or in the lamina propria, sub-mucosa, muscularis or serosa
brenda
-
-
brenda
-
extremely highly expressed in early embryos
brenda
-
GPX5
brenda
-
GPX5
brenda
-
-
brenda
-
-
brenda
-
GPX5
brenda
Gpx-5
brenda
-
GPX5
brenda
-
-
brenda
-
GPX5
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
activity in erythrocytes from patients with non-small-cell lung cancer and small-cell lung cancer is slightly increased compared to healthy control group
brenda
-
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
-
low expression
brenda
-
weak expression of pGPx
brenda
-
overexpression of glutathione peroxidase attenuates myocardial remodeling and preserves diastolic function in diabetic heart
brenda
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
brenda
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
highest expression
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
low expression
brenda
-
-
brenda
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
-
most abundantly expressed in hepatopancreas
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
GPX2
brenda
-
GPX2
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
GPX2
brenda
-
GPX1
brenda
-
GPX3
brenda
-
high expression of pGPx
brenda
-
-
brenda
-
brenda
-
GPX1
brenda
-
GPX3
brenda
-
GPX1
brenda
-
GPX3
brenda
-
GPX1
brenda
-
-
brenda
-
significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
brenda
-
GPX1
brenda
-
GPX3
brenda
-
weak expression of pGPx
brenda
-
-
brenda
-
-
brenda
highest expression
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
activity in brain is much lower than in liver
brenda
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
brenda
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
brenda
-
-
brenda
-
-
brenda
-
-
396610, 396612, 396614, 396615, 396617, 396618, 396635, 396636, 396638, 396641, 396645, 685480, 688957, 695410, 695719, 726472 brenda
-
-
brenda
-
GPX1
brenda
-
GPX3
brenda
-
weak expression of pGPx
brenda
-
GPX1
brenda
-
GPX3
brenda
-
GPX1
brenda
-
GPX3
brenda
-
-
brenda
-
GPX1
brenda
-
-
brenda
-
GPX1
brenda
-
GPX3
brenda
-
brenda
lowest expression
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
vascular smooth muscles cell
brenda
-
upregulated Gpx-1 activity is associated with neuroprotection in vitro
brenda
-
brenda
-
upregulated Gpx-1 activity is associated with neuroprotection in vitro
brenda
specifically expressed in shrimp ovaries, but not in other tissues
brenda
highest mRNA expression in ovary, followed by pyloric caeca, heart, liver and brain
brenda
-
brenda
-
extremely highly expressed in ovary
brenda
-
-
brenda
-
-
brenda
-
brenda
-
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
brenda
-
-
brenda
GPx-3
brenda
GPx-3 is secreted into the plasma
brenda
-
-
brenda
-
brenda
-
expression is observed in the membranes of vacuoles contained in prostate secretions as well as in the endothelium of arterioles and venules
brenda
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
brenda
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
brenda
-
-
brenda
main expression
brenda
-
moderate low mRNA level
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
weak expression of pGPx
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
GPX5
brenda
-
GPX5
brenda
-
GPX4
brenda
-
GPX5
brenda
-
GPX4
brenda
-
GPX5
brenda
-
GPX4
brenda
-
GPX5
brenda
-
-
brenda
-
GPX4
brenda
-
weak expression of pGPx
brenda
-
brenda
-
-
brenda
-
GPX2
brenda
-
GPX2
brenda
-
brenda
-
GPX2
brenda
-
GPX4
brenda
GPx4 is highly expressed in testis
brenda
-
GPX4
brenda
-
brenda
-
GPX4
brenda
-
GPX4
brenda
additional information
-
not detected at all in muscle, brain or liver
brenda
additional information
-
GPX transcript is absent from both immature and mature oocytes
brenda
additional information
the mRNA is present throughout the nematode second stage juvenile and is particularly abundant in metabolically active tissues including the genital primordia
brenda
additional information
the mRNA is present throughout the nematode second stage juvenile and is particularly abundant in metabolically active tissues including the genital primordia
brenda
additional information
-
the mRNA is present throughout the nematode second stage juvenile and is particularly abundant in metabolically active tissues including the genital primordia
brenda
additional information
in general, isoform Gpx4b mRNA expression exceeds that of isoform Gpx4a in all tissues with the exception of the pyloric caeca. The ratio of gpx4b/gpx4a is highest in ovary, and lowest in pyloric caeca
brenda
additional information
in general, isoform Gpx4b mRNA expression exceeds that of isoform Gpx4a in all tissues with the exception of the pyloric caeca. The ratio of gpx4b/gpx4a is highest in ovary, and lowest in pyloric caeca
brenda
additional information
-
in general, isoform Gpx4b mRNA expression exceeds that of isoform Gpx4a in all tissues with the exception of the pyloric caeca. The ratio of gpx4b/gpx4a is highest in ovary, and lowest in pyloric caeca
brenda
additional information
-
not detected in heart, brain, gut, muscle, epidermis, and testis
brenda
additional information
-
glial cells are devoid of GPx4
brenda
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a selenium deficient diet decreases glutathione reductase activity
-
adult male Swiss mice treated with 40 mg/ml methylmercury for 21 days show about 50% decrease in GPx activity in the brain
-
after Vibrio anguillarum and white spot syndrome virus challenge, glutathione peroxidase transcripts both in hemocytes and hepatopancreas increases about 3fold in the first 6 h and 3 h, respectively
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
-
expression is increased after treatment with copper ions
expression is not induced by heat stress
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
GPx-3 is induced by MG132 in HUVEC cells with an exponential increase in GPx-3 mRNA up to 120fold of control levels within 48 h. GPx-3 is still upregulated by a factor of 3-4 even after 72 and 96 h of proteasome inhibition. HAEC cells upregulate GPx-3 by more than 40fold in response to MG132. Proteasome inhibition clearly induces GPx-3 in HAoSMCs by a factor of 18
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
in Portunus trituberculatus challenged with the Hematodinium parasite, transcripts in hemocytes are initially suppressed at 3 h, and then induced significantly at all the other time points except for 96 h
in the brain, enzyme activity is significantly inhibited (51% after 28 days) during methylmercury exposure. In the case of co-exposure to methylmercury and selenium, inhibition of enzyme activity is less pronounced (25% at day 28)
-
no variation of enzyme expression is observed after a 1-day exposure to polychlorinated biphenyl 77
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
selenium treatment (0.01-0.03 mg/ml) significantly increases glutathione peroxidases activity in young barley seedlings
-
the enzyme (OsGPX5) is upregulated in response to hormone treatment. The OsGPX5 transcript is strongly induced by gibberellin or salicylic acid following a 3-h treatment and reaches maximum levels at 12 and 6 h, respectively. For abscisic acid treatment, OsGPX5 is activated and peaked within 3 h, approximately fourfold of the original level, and then declines to a normal level after 6 h. When rice seedlings are exposed to indole-3-acetic acid or 6-benzylaminopurine, a weak induction of the OsGPX5 transcript is observed within 1-h treatment and its expression sustaines at this level for 12 h. OsGPX5 mRNA level is weakly upregulated in response to heat
-
the enzyme expression level shows a 4 and a 2.6fold decrease after 3 and 7 days of exposure to polychlorinated biphenyl 77, respectively
the GPx gene contains a standard UGU codon for cysteine instead of a UGA opal codon for seleno-cysteine at the active site, and no selenoocysteine insertion sequence motif is identified within the 3'-untranslated region
the level of mRNA significantly increases 6 h after challenge with Vibrio harveyi, Staphyloccocus aureus or white spot syndrome virus
-
the seasonal gpx4 mRNA transcript is significantly lower in lizard brain during mating as compared with stasis. In testis the gpx4 mRNA transcript level is significantly higher in the mating phase
the transcript levels of antioxidant enzyme genes Gpx3, superoxide dismutase and catalase are induced after acute nitrite exposure. In the gill, the expression level of Gpx3 mRNA increases significantly from 6 to 12 h after nitrite exposure but returns to its original level after 24h
treatment with 7alpha,17beta-[9-[(4,4,5,5,5-pentafluoropentyl)sulfinyl]nonyl]estra-1,3,5(10)-triene-3,17-diol, i.e. ICI 182,780, increases expression during mating
treatment with human chorionic gonadotropin decreases expression in stasis
Vibrio challenge can significantly upregulate the mRNA expression of the enzyme, and the highest expression level (6.5fold) is detected at 24 h post infection with 6.5fold increase compared with that in the control group. Enzyme expression is significantly induced by 0.02 and 0.04 mg l-1 Cd (both 2.9fold after 24 h) and 0.01 and 0.02 mg l-1 Cu (2.7fold after 24 h and 1.6fold at 96 h, respectively). The mRNA expression is maximally induced (6.29fold) at 96 h post challenge with 0.05 mg l-1 benzo[a]pyrene
-
expression is increased after treatment with copper ions
expression is increased after treatment with copper ions
-
-
the GPx gene contains a standard UGU codon for cysteine instead of a UGA opal codon for seleno-cysteine at the active site, and no selenoocysteine insertion sequence motif is identified within the 3'-untranslated region
the GPx gene contains a standard UGU codon for cysteine instead of a UGA opal codon for seleno-cysteine at the active site, and no selenoocysteine insertion sequence motif is identified within the 3'-untranslated region
-
-
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