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Literature summary extracted from

  • Joensson, T.J.; Johnson, L.C.; Lowther, W.T.
    Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace (2008), Nature, 451, 98-101.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 expressed in Escherichia coli C41(DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.98.2 vapour diffusion method, 2.6 A crystal structure of the sulphiredoxin–peroxiredoxin-I complex Homo sapiens
1.11.1.24 sulfredoxin in complex with PrxI, hanging-drop vapour diffusion method, in 20 mM HEPES pH 7.5 and 100 mM NaCl Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.98.2 Homo sapiens Q9BYN0
-
-
1.11.1.24 Homo sapiens Q06830
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.11.1.24 Prx can become inactivated through the hyperoxidation of an active site Cys residue to Cys sulphinic acid Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24 phenyl-Sepharose column chromatography, S-Sepharose column chromatography, hydroxyapatite column chromatography, and G25 gel filtration Homo sapiens

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.11.1.24 decamer hyperoxidized form of Prx, X-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 2-Cys peroxiredoxin
-
 Homo sapiens
1.11.1.24 Prx
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
 Homo sapiens