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Literature summary for 1.11.1.27 extracted from

  • 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 (2009), Arch. Biochem. Biophys., 485, 139-149.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.27

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli cells Rattus norvegicus
expression in A-549 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C47S inactive Rattus norvegicus
D140A mutant shows decreased peroxidase activity Rattus norvegicus
H26A mutant shows decreased peroxidase activity Rattus norvegicus
S32A mutant shows decreased peroxidase activity with H2O2 and no activity with 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol treatment of A-549 cells with peroxides leads to translocation of Prdx6 from the cytosol to the cell membrane Rattus norvegicus 5829
-
membrane treatment of A-549 cells with peroxides leads to translocation of Prdx6 from the cytosol to the cell membrane Rattus norvegicus 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus O35244
-
-

Purification (Commentary)

Purification (Comment) Organism
column chromatography and YMC-10 gel filtration Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.28
-
 mutant enzyme H26A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4 Rattus norvegicus
5.25
-
 mutant enzyme D140A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4 Rattus norvegicus
5.6
-
 mutant enzyme H26A, using H2O2 as substrate, at pH 7.4 Rattus norvegicus
5.72
-
 mutant enzyme S32A, using H2O2 as substrate, at pH 7.4 Rattus norvegicus
6
-
 wild type enzyme, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4 Rattus norvegicus
6.15
-
 mutant enzyme D140A, using H2O2 as substrate, at pH 7.4 Rattus norvegicus
6.2
-
 wild type enzyme, using H2O2 as substrate, at pH 7.4 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH specific substrate for peroxiredoxin 6 Rattus norvegicus ?
-
 ?
H2O2 + 2 GSH
-
 Rattus norvegicus 2 H2O + GSSG
-
 ?
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 Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
peroxiredoxin 6
-
 Rattus norvegicus
Prdx6
-
 Rattus norvegicus