1.11.1.27: glutathione-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about glutathione-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.27
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1.11.1.27
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peroxiredoxins
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plasmodium
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falciparum
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malaria
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prxvi
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intraerythrocytic
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medicine
- 1.11.1.27
- peroxiredoxins
- plasmodium
- falciparum
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malaria
- prxvi
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intraerythrocytic
- medicine
Reaction
Synonyms
1-Cys peroxiredoxin, 1-Cys Prdx, 1-Cys Prx, 1-CysPrx, 2-Cys peroxiredoxin, 2-Cys peroxiredoxin TPx-1, EC 1.11.1.15, glutathione peroxidase, GPX, HI0572, peroxiredoxin 6, peroxiredoxin II, peroxiredoxin VI, Pf1-Cys-Prx, PGdx, Prdx6, Prx1, Prx3, Prx6, TPx-1
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Natural Substrates Products
Natural Substrates Products on EC 1.11.1.27 - glutathione-dependent peroxiredoxin
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REACTION DIAGRAM
glutathione disulfide + H2O + ROH
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2 GSH + ROOH
GSSG + H2O + ROH
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glutathione is the primary native reductant
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2 GSH + ROOH
GSSG + H2O + ROH
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glutathione is the primary native reductant
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2 GSH + ROOH
GSSG + H2O + ROH
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glutathione is the primary native reductant
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the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
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the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
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additional information
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the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
?
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the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
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additional information
?
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the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
?
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the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
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additional information
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Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
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additional information
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Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
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additional information
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the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
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peroxiredoxin 6 differs from other mammalian peroxiredoxins both in its ability to reduce phospholipid hydroperoxides at neutral pH and in having phospholipase A2 activity that is maximal at acidic pH
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additional information
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the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
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additional information
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Prx1 is particularly required to protect against mitochondrial oxidation, Prx1 requires thioredoxin reductase 2 and the glutathione system, but not thioredoxin 3, to promote oxidant resistance
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additional information
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the enzyme functions in antioxidant defense and lung phospholipid metabolism
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