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1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
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5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
cumene hydroperoxide + GSH
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glutathione + H2O2
glutathione disulfide + H2O
glutathione + ROOH
glutathione disulfide + ROH + H2O
linolenic acid hydroperoxide + GSH
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
additional information
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1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
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1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
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5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
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5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
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cumene hydroperoxide + GSH
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cumene hydroperoxide + GSH
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cumene hydroperoxide + GSH
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cumene hydroperoxide + GSH
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cumene hydroperoxide + GSH
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cumene hydroperoxide + GSH
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + H2O2
glutathione disulfide + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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broad specificity for hydroperoxides
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cumene hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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ethyl hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cholesterol 7beta-hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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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
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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peroxidized DNA
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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pregnenolone 17alpha-hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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thymine hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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highly specific for glutathione
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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linoleic acid hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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gamma-glutamyl-L-cysteine-methylester has 26% of glutathione activity
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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broad specificity for hydroperoxides
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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tert-butylhydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cumene hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cumene hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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ethyl hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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ROOH can be: aliphatic or aromatic peroxide or H2O2
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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broad specificity for hydroperoxides
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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hydroperoxyarachidonate
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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peroxidized DNA
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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thymine hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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highly specific for glutathione
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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linoleic acid hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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tert-butylhydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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reduction of hydroperoxides increases with hydrophobicity of substrates
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cumene hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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ethyl hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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menthane hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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diisopropyl hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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linoleic acid hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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lauryl hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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cumene hydroperoxide
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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dithiothreitol has 10% of glutathione activity
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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highly specific for glutathione
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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broad specificity for hydroperoxides
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glutathione + ROOH
glutathione disulfide + ROH + H2O
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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the enzyme protects cells against oxidative damage
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H2O2 + GSH
H2O + GSSG
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H2O2 + GSH
H2O + GSSG
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linolenic acid hydroperoxide + GSH
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linolenic acid hydroperoxide + GSH
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linolenic acid hydroperoxide + GSH
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linolenic acid hydroperoxide + GSH
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
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tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
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additional information
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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
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additional information
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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
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additional information
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major antioxidant enzyme
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
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additional information
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the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
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additional information
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the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
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additional information
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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
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additional information
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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
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additional information
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upregulation of GPx-1 gene expression in prostate cancer cells bei genistein
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additional information
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adenosine may protect the cardiovascular system from ischemia/reperfusion injury, in part, by enhancing the expression of the central intracellular antioxidant enzyme, GPx-1
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additional information
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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
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additional information
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selenium containing glutathione transferase zeta1-1 does also possess glutathione peroxidase activity
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additional information
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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
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additional information
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Gpx2 affords resistance to gastrointestinal pathology in Se-depleted mice
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additional information
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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
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additional information
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involved in mainenance of the steady state levels of H2O2 in heart mitochondria matrix
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additional information
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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
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additional information
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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
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