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1-palmitoyl-2-arichidonoyl-sn-glycero-3-phosphocholine + GSH
?
-
-
-
?
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 + ?
-
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
2 glutathione + H2O2
glutathione disulfide + H2O
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + H2O + tert-butyl alcohol
2 GSH + ROOH
GSSG + H2O + ROH
arachidonoyl hydroperoxide + GSH
?
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG
-
-
-
?
glutathione + H2O2
glutathione disulfide + 2 H2O
H2O2 + 2 GSH
2 H2O + GSSG
-
-
-
?
H2O2 + dithiothreitol
?
-
-
-
?
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
-
-
?
linolenoyl hydroperoxide + GSH
?
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
additional information
?
-
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 + H2O
ADV89163
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + H2O
ADV89163
-
-
-
?
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
-
-
-
?
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
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
-
-
-
?
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
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 glutathione + H2O2
glutathione disulfide + 2 H2O
-
-
-
?
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
2 GSH + ROOH
GSSG + H2O + ROH
additional information
?
-
2 glutathione + ROOH
glutathione disulfide + H2O + ROH
-
-
-
?
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
-
-
?
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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malfunction
ADV89163
the prx3 mutation impairs growth in the medium containing peroxides and reduced virulence in mice
malfunction
ADV89163
the prx3 mutation impairs growth in the medium containing peroxides and reduces virulence in mice
malfunction
Prdx6 null mice show increased lung or liver injury with exposure to hyperoxia, lipopolysaccharide (LPS), or paraquat. Prdx6 null mice as compared to wild type demonstrate increased age-related oxidative damage to their sperm chromatin
malfunction
-
enzyme haplodeficiency attenuates astro- and microglia activation around Abeta plaques promoting Abeta deposition and neuritic degeneration
malfunction
peroxiredoxin 6 down-regulation reduces cell proliferation. Enzyme silencing interferes with apoptotic signaling from CD95 but does not induce apoptosis in HepG2 cells
malfunction
-
the prx3 mutation impairs growth in the medium containing peroxides and reduced virulence in mice
-
malfunction
-
the prx3 mutation impairs growth in the medium containing peroxides and reduces virulence in mice
-
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
ADV89163
Prx3 is essential for survival under oxidative stress and pathogenesis of Vibrio vulnificus
physiological function
ADV89163
Prx3 is essential for survival under oxidative stress and virulence in mice
physiological function
cells over-expressing Prdx6 show an increase in survival compared to control when oxidatively challenged with hydroperoxides, paraquat, UVB radiation, or OH generated by Cu2+/ascorbate. Prx6 over-expression through adenoviral-mediated intratracheal delivery of a Prdx6 expression vector or in transgenic mice protected lungs from hyperoxic injury. Prdx6 has an important role in the repair of peroxidized cell membranes, at least in lungs, and that both its PHGPx and PLA2 activities play important roles
physiological function
function of PRDX6 in osteogenic differentiation, bone regeneration, and bone development. It is proposed that PRDX6 is a critical enzyme for cell fate determination of dental pulp stem cell into osteoblast lineages
physiological function
peroxiredoxins, the family of non-selenium glutathione peroxidases, are important antioxidant enzymes that defend a system from the toxic reactive oxygen species
physiological function
Prdx6 plays crucial roles in lung phospholipid metabolism, lipid peroxidation repair, and inflammatory signaling. Mice that over-express Prdx6 show a greater increase in the growth of lung tumors compared to wild-type animals. Both aiPLA2 and Prdx6 peroxidase activities are implicated in lung tumor development through the regulation of redox-sensitive pathways such as MAPK, JNK, JAK/STAT, and AP-1
physiological function
Prdx6 plays crucial roles in lung phospholipid metabolism, lipid peroxidation repair, and inflammatory signaling. Prdx6 prevents oxidative stress in human retinal pigment epithelial cells by activating the phosphoinositide 3-kinase/protein kinase B (PI3K/AKT) pathway. Prdx6 is necessary to prevent cataract formation and to limit aging-induced oxidative stress in the eye
physiological function
-
enzyme upregulation attenuates Abeta pathology
physiological function
-
Prx3 is essential for survival under oxidative stress and pathogenesis of Vibrio vulnificus
-
physiological function
-
Prx3 is essential for survival under oxidative stress and virulence in mice
-
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
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oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
PRDX6 levels are decreased during osteogenic differentiation in human dental pulp stem cells
the Fe-S cluster regulator IscR activates prx3 expression by sensing reactive oxygen species and iron starvation. IscR controls the prx3 expression by directly binding to the type 2 IscR-binding site centered at positionx0244 from the transcription start site. Biochemical and molecular genetic evidence demonstrates that IscR senses iron starvation as well as ROS and shifts to the clusterless apo-form, which leads to the increase in its own levels in cells and accordingly, the activation of prx3
the Fe-S cluster regulator IscR senses iron starvation as well as reactive oxygen species and shifts to the Fe-S clusterless apo-form, which leads to the increase of cellular IscR and in turn prx3 expression, contributing to the survival and virulence of Vibrio vulnificus during pathogenesis
transcription of Prdx6 message in dermal epithelium is induced by treatment with keratinocyte growth factor, a response of presumed importance related to wound healing, requiring ARE and Nrf2. Dexamethasone induces Prdx6 expression in adult lung cells and regulates transcription through its interaction with a glucocorticoid response element in the promoter region of the Prdx6 gene. Oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
the Fe-S cluster regulator IscR activates prx3 expression by sensing reactive oxygen species and iron starvation. IscR controls the prx3 expression by directly binding to the type 2 IscR-binding site centered at positionx0244 from the transcription start site. Biochemical and molecular genetic evidence demonstrates that IscR senses iron starvation as well as ROS and shifts to the clusterless apo-form, which leads to the increase in its own levels in cells and accordingly, the activation of prx3
ADV89163
the Fe-S cluster regulator IscR activates prx3 expression by sensing reactive oxygen species and iron starvation. IscR controls the prx3 expression by directly binding to the type 2 IscR-binding site centered at positionx0244 from the transcription start site. Biochemical and molecular genetic evidence demonstrates that IscR senses iron starvation as well as ROS and shifts to the clusterless apo-form, which leads to the increase in its own levels in cells and accordingly, the activation of prx3
-
-
the Fe-S cluster regulator IscR senses iron starvation as well as reactive oxygen species and shifts to the Fe-S clusterless apo-form, which leads to the increase of cellular IscR and in turn prx3 expression, contributing to the survival and virulence of Vibrio vulnificus during pathogenesis
ADV89163
the Fe-S cluster regulator IscR senses iron starvation as well as reactive oxygen species and shifts to the Fe-S clusterless apo-form, which leads to the increase of cellular IscR and in turn prx3 expression, contributing to the survival and virulence of Vibrio vulnificus during pathogenesis
-
-
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Merkulova, M.I.; Shuvaeva, T.M.; Radchenko, V.V.; Yanin, B.A.; Bondar, A.A.; Sofin, A.D.; Lipkin, V.M.
Recombinant human peroxiredoxin VI: preparation and protective properties in vitro
Biochemistry
67
1235-1239
2002
Homo sapiens (P30041), Homo sapiens
brenda
Rouhier, N.; Jacquot, J.P.
Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis
FEBS Lett.
554
149-153
2003
Neisseria meningitidis
brenda
Kang, S.W.; Baines, I.C.; Rhee, S.G.
Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
J. Biol. Chem.
273
6303-6311
1998
Homo sapiens (P30041)
brenda
Rouhier, N.; Gama, F.; Wingsle, G.; Gelhaye, E.; Gans, P.; Jacquot, J.P.
Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin
Biochem. Biophys. Res. Commun.
341
1300-1308
2006
Populus tremula x Populus tremuloides (Q8S3L0)
brenda
Kawazu, S.; Ikenoue, N.; Takemae, H.; Komaki-Yasuda, K.; Kano, S.
Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum
FEBS J.
272
1784-1791
2005
Plasmodium falciparum
brenda
Manevich, Y.; Fisher, A.B.
Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
Free Radic. Biol. Med.
38
1422-1432
2005
Mus musculus (O08709), Rattus norvegicus (O35244), Bos taurus (O77834), Homo sapiens (P30041), Sus scrofa (Q9TSX9)
brenda
Yano, K.; Komaki-Yasuda, K.; Tsuboi, T.; Torii, M.; Kano, S.; Kawazu, S.
2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei
Mol. Biochem. Parasitol.
148
44-51
2006
Plasmodium berghei
brenda
Manevich, Y.; Shuvaeva, T.; Dodia, C.; Kazi, A.; Feinstein, S.I.; Fisher, A.B.
Binding of peroxiredoxin 6 to substrate determines differential phospholipid hydroperoxide peroxidase and phospholipase A(2) activities
Arch. Biochem. Biophys.
485
139-149
2009
Rattus norvegicus (O35244)
brenda
Roede, J.R.; Carbone, D.L.; Doorn, J.A.; Kirichenko, O.V.; Reigan, P.; Petersen, D.R.
In vitro and in silico characterization of peroxiredoxin 6 modified by 4-hydroxynonenal and 4-oxononenal
Chem. Res. Toxicol.
21
2289-2299
2008
Rattus norvegicus
brenda
Greetham, D.; Grant, C.M.
Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
Mol. Cell. Biol.
29
3229-3240
2009
Saccharomyces cerevisiae
brenda
Fisher, A.B.
Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
Antioxid. Redox Signal.
15
831-844
2010
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Pauwels, F.; Vergauwen, B.; Vanrobaeys, F.; Devreese, B.; Van Beeumen, J.J.
Purification and characterization of a chimeric enzyme from Haemophilus influenzae Rd that exhibits glutathione-dependent peroxidase activity
J. Biol. Chem.
278
16658-16666
2003
Haemophilus influenzae (P44758), Haemophilus influenzae ATCC 51907 (P44758)
brenda
Lim, J.G.; Bang, Y.J.; Choi, S.H.
Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation
J. Biol. Chem.
289
36263-36274
2014
Vibrio vulnificus (ADV89163), Vibrio vulnificus MO6-24/O (ADV89163)
brenda
Manevich, Y.; Feinstein, S.I.; Fisher, A.B.
Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST
Proc. Natl. Acad. Sci. USA
101
3780-3785
2004
Bos taurus
brenda
Park, K.R.; Yun, H.M.; Yeo, I.J.; Cho, S.; Hong, J.T.; Jeong, Y.S.
Peroxiredoxin 6 inhibits osteogenic differentiation and bone formation through human dental pulp stem cells and induces delayed bone development
Antioxid. Redox Signal.
30
1969-1982
2019
Homo sapiens (P30041)
brenda
Arevalo, J.A.; Vazquez-Medina, J.P.
The role of peroxiredoxin 6 in cell signaling
Antioxidants (Basel)
7
172
2018
Mus musculus (O08709), Homo sapiens (P30041)
brenda
Shahnaj, S.; Chowhan, R.K.; Meetei, P.A.; Kakchingtabam, P.; Herojit Singh, K.; Rajendrakumar Singh, L.; Nongdam, P.; Fisher, A.B.; Rahaman, H.
Hyperoxidation of peroxiredoxin 6 induces alteration from dimeric to oligomeric state
Antioxidants (Basel)
8
33
2019
Rattus norvegicus (O35244)
brenda
Fisher, A.B.
Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling
Arch. Biochem. Biophys.
617
68-83
2017
Mus musculus (O08709)
brenda
Wang, L.L.; Lu, S.Y.; Hu, P.; Fu, B.Q.; Li, Y.S.; Zhai, F.F.; Ju, D.D.; Zhang, S.J.; Su, B.; Zhou, Y.; Liu, Z.S.; Ren, H.L.
Construction and activity analyses of single functional mouse peroxiredoxin 6 (Prdx6)
J. Vet. Res.
63
99-105
2019
Mus musculus (O08709)
brenda
Lopez Grueso, M.J.; Tarradas Valero, R.M.; Carmona-Hidalgo, B.; Lagal Ruiz, D.J.; Peinado, J.; McDonagh, B.; Requejo Aguilar, R.; Barcena Ruiz, J.A.; Padilla Pena, C.A.
Peroxiredoxin 6 down-regulation induces metabolic remodeling and cell cycle arrest in HepG2 cells
Antioxidants (Basel)
8
505
2019
Homo sapiens (P30041)
brenda
Pankiewicz, J.E.; Diaz, J.R.; Marta-Ariza, M.; Lizi?czyk, A.M.; Franco, L.A.; Sadowski, M.J.
Peroxiredoxin 6 mediates protective function of astrocytes in Abeta proteostasis
Mol. Neurodegener.
15
50
2020
Mus musculus
brenda
Chen, C.; Gong, L.; Liu, X.; Zhu, T.; Zhou, W.; Kong, L.; Luo, J.
Identification of peroxiredoxin 6 as a direct target of withangulatin A by quantitative chemical proteomics in non-small cell lung cancer
Redox Biol.
46
102130
2021
Homo sapiens (P30041)
brenda
Chowhan, R.K.; Rahaman, H.; Singh, L.R.
Structural basis of peroxidase catalytic cycle of human Prdx6
Sci. Rep.
10
17416
2020
Homo sapiens (P30041)
brenda
Chowhan, R.K.; Hotumalani, S.; Rahaman, H.; Singh, L.R.
pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
Sci. Rep.
11
9657
2021
Homo sapiens (P30041)
brenda