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Literature summary for 1.11.1.27 extracted from

  • Fisher, A.B.
    Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities (2010), Antioxid. Redox Signal., 15, 831-844.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination, analysis, and comparison Homo sapiens
DNA and amino acid sequence determination, analysis, and comparison Rattus norvegicus
DNA and amino acid sequence determination, analysis, and comparison Bos taurus
Prdx6 gene, DNA and amino acid sequence determination and analysis, comprises 5 exons and 4 introns and is located on chromosome 1, mapped to a 0.66 cM interval between D1Mit 159 and D1Mit 398, sequence comparison Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure determination and analysis at 2.0 A resolution Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Bos taurus
Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Homo sapiens
Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Mus musculus
Mercaptosuccinate a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected Rattus norvegicus
MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Bos taurus
MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Homo sapiens
MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Mus musculus
MJ33 a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity Rattus norvegicus
additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Bos taurus
additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Homo sapiens
additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Mus musculus
additional information serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Mus musculus 5829
-
cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Homo sapiens 5829
-
cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Rattus norvegicus 5829
-
cytosol cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment Bos taurus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25100
-
x * 25100, about, sequence calculation, x * 26000-29000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 GSH + ROOH Mus musculus glutathione is the primary native reductant GSSG + H2O + ROH
-
?
2 GSH + ROOH Homo sapiens glutathione is the primary native reductant GSSG + H2O + ROH
-
?
2 GSH + ROOH Rattus norvegicus glutathione is the primary native reductant GSSG + H2O + ROH
-
?
2 GSH + ROOH Bos taurus glutathione is the primary native reductant GSSG + H2O + ROH
-
?
additional information Mus musculus 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 Homo sapiens 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 Rattus norvegicus 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 Bos taurus 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Mus musculus
phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Homo sapiens
phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Rattus norvegicus
phosphoprotein MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain
-
Homo sapiens
-
brain
-
Rattus norvegicus
-
brain
-
Bos taurus
-
epidermis
-
Mus musculus
-
epidermis
-
Homo sapiens
-
epidermis
-
Rattus norvegicus
-
epidermis
-
Bos taurus
-
epithelium
-
Mus musculus
-
epithelium
-
Homo sapiens
-
epithelium
-
Rattus norvegicus
-
epithelium
-
Bos taurus
-
eye ciliary body Bos taurus
-
kidney
-
Mus musculus
-
kidney
-
Homo sapiens
-
kidney
-
Rattus norvegicus
-
kidney
-
Bos taurus
-
liver
-
Mus musculus
-
liver
-
Homo sapiens
-
liver
-
Rattus norvegicus
-
liver
-
Bos taurus
-
lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Mus musculus
-
lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Homo sapiens
-
lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Rattus norvegicus
-
lung especially in type II alveolar epithelial cells and bronchiolar Clara cells Bos taurus
-
additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Mus musculus
-
additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Homo sapiens
-
additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Rattus norvegicus
-
additional information within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview Bos taurus
-
olfactory mucosa
-
Rattus norvegicus
-
testis
-
Mus musculus
-
testis
-
Homo sapiens
-
testis
-
Rattus norvegicus
-
testis
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GSH + ROOH
-
Mus musculus GSSG + H2O + ROH
-
?
2 GSH + ROOH
-
Homo sapiens GSSG + H2O + ROH
-
?
2 GSH + ROOH
-
Rattus norvegicus GSSG + H2O + ROH
-
?
2 GSH + ROOH
-
Bos taurus GSSG + H2O + ROH
-
?
2 GSH + ROOH glutathione is the primary native reductant Mus musculus GSSG + H2O + ROH
-
?
2 GSH + ROOH glutathione is the primary native reductant Homo sapiens GSSG + H2O + ROH
-
?
2 GSH + ROOH glutathione is the primary native reductant Rattus norvegicus GSSG + H2O + ROH
-
?
2 GSH + ROOH glutathione is the primary native reductant Bos taurus GSSG + H2O + ROH
-
?
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 Mus musculus ?
-
?
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 Homo sapiens ?
-
?
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 Rattus norvegicus ?
-
?
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 Bos taurus ?
-
?
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 Mus musculus ?
-
?
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 Homo sapiens ?
-
?
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 Rattus norvegicus ?
-
?
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 Bos taurus ?
-
?

Subunits

Subunits Comment Organism
? x * 25100, about, sequence calculation, x * 26000-29000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
1-Cys Prdx
-
Mus musculus
1-Cys Prdx
-
Homo sapiens
1-Cys Prdx
-
Rattus norvegicus
1-Cys Prdx
-
Bos taurus
peroxiredoxin 6
-
Mus musculus
peroxiredoxin 6
-
Homo sapiens
peroxiredoxin 6
-
Rattus norvegicus
peroxiredoxin 6
-
Bos taurus
Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Mus musculus
Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Homo sapiens
Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Rattus norvegicus
Prdx6 Prdx6 is the prototype and the only mammalian 1-Cys member of the peroxiredoxin family Bos taurus

pI Value

Organism Comment pI Value Maximum pI Value
Homo sapiens
-
-
5.1

Expression

Organism Comment Expression
Mus musculus 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 up
Homo sapiens 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 up
Bos taurus 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 up
Rattus norvegicus 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 up

General Information

General Information Comment Organism
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 Mus musculus
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 Homo sapiens
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 Rattus norvegicus
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 Bos taurus
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 Mus musculus
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 Homo sapiens
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 Rattus norvegicus
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 Bos taurus