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
-
malaria
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prxvi
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intraerythrocytic
-
medicine
- 1.11.1.27
- peroxiredoxins
- plasmodium
- falciparum
-
malaria
- prxvi
-
intraerythrocytic
- medicine
Reaction
2 glutathione
+
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
ECTree
1.11.1.27 glutathione-dependent peroxiredoxinAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.11.1.27 - glutathione-dependent peroxiredoxin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
specific substrate for peroxiredoxin 6
-
-
?
2 glutathione + 1-palmitoyl-2-linolenoyl hydroperoxide-sn-glycero-3-phosphocholine
glutathione disulfide + H2O + ?
-
-
-
-
?
H2O2 + NADPH
H2O + NADP+
-
reaction is driven by glutathione which is maintained reduced via NADPH and glutathione reductase. Both the peroxiredoxin and glutaredoxin domains are biochemically active in the natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain. When expressed separately, the glutaredoxin domain is catalytically active and the peroxiredoxin domain posseses a weak activity when supplemented with expoenous glutaredoxin
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
-
-
-
?
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + H2O + tert-butyl alcohol
-
-
-
?
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + H2O + tert-butyl alcohol
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
glutathione + H2O2
glutathione disulfide + 2 H2O
ADV89163
the enzyme is only active when glutaredoxin 3, glutathione, and glutathione reductase are present together as a reducing system
-
-
?
glutathione + H2O2
glutathione disulfide + 2 H2O
ADV89163
the enzyme is only active when glutaredoxin 3, glutathione, and glutathione reductase are present together as a reducing system
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
-
-
-
?
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
?
additional information
?
-
the enzyme exhibits a low level of phospholipiase A2 activity at acidic pH
-
-
?
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
?
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
?
additional information
?
-
-
Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
-
-
?
additional information
?
-
-
Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
-
-
?
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
?
