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Information on EC 1.11.1.27 - glutathione-dependent peroxiredoxin
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1.11.1.27 glutathione-dependent peroxiredoxinIUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutathione-dependent peroxiredoxins have been reported from bacteria and animals, and appear to be 1-Cys enzymes. The mechanism for the mammalian PRDX6 enzyme involves heterodimerization of the enzyme with pi-glutathione S-transferase, followed by glutathionylation of the oxidized cysteine residue. Subsequent dissociation of the heterodimer yields glutathionylated peroxiredoxin, which is restored to the active form via spontaneous reduction by a second glutathione molecule.
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Word Map
- 1.11.1.27
- peroxiredoxins
- plasmodium
- falciparum
-
malaria
- prxvi
-
intraerythrocytic
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pf1-cys-prx, peroxiredoxin vi, 1-cys prdx, hi0572, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-Cys peroxiredoxin
1-Cys Prdx
EC 1.11.1.15
-
-
formerly, part transferred
-
HI0572
peroxiredoxin 6
PGdx
Prdx6
Prx3
peroxiredoxin 6
bifunctional enzyme with glutathione peroxidase activity and Ca2+-independent phospholipase A2 activity
peroxiredoxin 6
bifunctional enzyme with glutathione peroxidase and calcium-independent phospholipase A2 activities
peroxiredoxin 6
-
dual function enzyme with independent glutathione peroxidase and phospholipase A2 activities
Prdx6
-
-
-
-
Prdx6
-
Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family
Prdx6
-
Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family
Prdx6
-
Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family
Prdx6
-
Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family
Prx3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + ROOH = glutathione disulfide + H2O + ROH
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glutathione:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [1]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutathione-dependent peroxiredoxins have been reported from bacteria and animals, and appear to be 1-Cys enzymes. The mechanism for the mammalian PRDX6 enzyme involves heterodimerization of the enzyme with pi-glutathione S-transferase, followed by glutathionylation of the oxidized cysteine residue. Subsequent dissociation of the heterodimer yields glutathionylated peroxiredoxin, which is restored to the active form via spontaneous reduction by a second glutathione molecule.
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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
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-
-
?
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
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-
?
additional information
?
-
the enzyme exhibits a low level of phospholipiase A2 activity at acidic pH
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-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
-
-
-
?
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
-
-
?
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
additional information
-
serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
-
additional information
-
serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
-
additional information
-
serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
-
additional information
-
serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
physiological mechanism for the glutathionylation of the oxidized cysteine in 1-cysPrx by its heterodimerization with glutathione-loaded glutathione S-transferase P (GST-pi) results in heterodimer formation, glutathionylation of the enzyme (1-cysPrx), and enzyme reactivation. Maximum activation of the enzyme (1-cysPrx) occurrs with a 1:1 molar ratio of glutathione-saturated glutathione S-transferase P and a 2:1 molar ratio of glutathione to enzyme (1-cysPrx)
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Proteomics-based approach identifying autoantibody against peroxiredoxin VI as a novel serum marker in esophageal squamous cell carcinoma.
Esophageal Squamous Cell Carcinoma
Proteomics-based approach identifying autoantibody against peroxiredoxin VI as a novel serum marker in esophageal squamous cell carcinoma.
Hypersensitivity
2-Cys peroxiredoxin of Plasmodium falciparum is involved in resistance to heat stress of the parasite.
Lymphoma, B-Cell
High intensity of cytoplasmic peroxiredoxin VI expression is associated with adverse outcome in diffuse large B-cell lymphoma independently of International Prognostic Index.
Lymphoma, Large B-Cell, Diffuse
High intensity of cytoplasmic peroxiredoxin VI expression is associated with adverse outcome in diffuse large B-cell lymphoma independently of International Prognostic Index.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.28
mutant enzyme H26A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
5.25
mutant enzyme D140A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
6
wild type enzyme, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
about 40% activity at pH 6.0, 100% activity at pH 7.0, about 90% activity at pH 8.0, about 70% activity at pH 9.0, about 60% activity at pH 10.0
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain
-
-
brenda
Populus tremula x Populus tremuloides
SwissProt
brenda
bifunctional protein with glutathione peroxidase activity and phospholipase A2 activity
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expressed at high levels during the haem-digesting stage
brenda
additional information