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Literature summary for 1.11.1.24 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
Search for more literature for 1.11.1.24

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
sulfredoxin in complex with PrxI, hanging-drop vapour diffusion method, in 20 mM HEPES pH 7.5 and 100 mM NaCl Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q06830
-
-

Oxidation Stability

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
2-Cys peroxiredoxin
-
 Homo sapiens
Prx
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thioredoxin
-
 Homo sapiens