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Literature summary extracted from

  • Low, F.M.; Hampton, M.B.; Winterbourn, C.C.
    Peroxiredoxin 2 and peroxide metabolism in the erythrocyte (2008), Antioxid. Redox Signal., 10, 1621-1630.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.24 cytosol the enzyme is mostly cytosolic Homo sapiens 5829
-
1.11.1.24 membrane 0.05% of cellular Prx2 is bound to the membrane Homo sapiens 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.24 erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 Gardos channel + ? activates the Gardos channel Homo sapiens ?
-
 ?
1.11.1.24 H2O2 + dithiothreitol
-
 Homo sapiens H2O + oxidized dithiothreitol
-
 ?
1.11.1.24 H2O2 + reduced thioredoxin
-
 Homo sapiens H2O + oxidized thioredoxin
-
 ?
1.11.1.24 peroxinitrite + reduced thioredoxin
-
 Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.24 decamer pentamer of dimers Homo sapiens
1.11.1.24 homodimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 calpromotin
-
 Homo sapiens
1.11.1.24 natural killer enhancing factor-B
-
 Homo sapiens
1.11.1.24 peroxiredoxin 2
-
 Homo sapiens
1.11.1.24 Prx2
-
 Homo sapiens
1.11.1.24 thiol-specific antioxidant/protector protein
-
 Homo sapiens
1.11.1.24 thioredoxin peroxidase II
-
 Homo sapiens
1.11.1.24 torin
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
 Homo sapiens