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Literature summary extracted from

  • Tavender, T.J.; Sheppard, A.M.; Bulleid, N.J.
    Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells (2008), Biochem. J., 411, 191-199.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 expressed in HT-1080 cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.24 endoplasmic reticulum
-
 Homo sapiens 5783
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.24 27000
-
 SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Homo sapiens Q13162
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 H2O2 + reduced thioredoxin
-
 Homo sapiens H2O + oxidized thioredoxin
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.24 oligomer Prx IV oligomers contain two prevalent species with apparent molecular masses of 27 and 54 kDa corresponding to Prx IV monomers and disulfide-linked homodimers Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 peroxiredoxin IV
-
 Homo sapiens
1.11.1.24 PRx IV
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
 Homo sapiens