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Literature summary for 1.11.1.24 extracted from

  • Sutton, D.L.; Loo, G.H.; Menz, R.I.; Schuller, K.A.
    Cloning and functional characterization of a typical 2-Cys peroxiredoxin from southern bluefin tuna (Thunnus maccoyii) (2010), Comp. Biochem. Physiol. B, 156, 97-106.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Prx 2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression in Escherichia coli Thunnus maccoyii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH Thunnus maccoyii
0.012
-
thioredoxin pH 7.5, 25°C, recombinant enzyme Thunnus maccoyii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21800
-
x * 21800, SDS-PAGE and sequence calculation Thunnus maccoyii
250000
-
recombinant enzyme, peak 1, gel filtration Thunnus maccoyii
400000
-
recombinant enzyme, peak 2, gel filtration Thunnus maccoyii

Organism

Organism UniProt Comment Textmining
Thunnus maccoyii A9QKS0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Prx 2 from Escherichia coli by nickel affinity chromatography and gel filtration Thunnus maccoyii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 thioredoxin + cumene hydroperoxide
-
Thunnus maccoyii thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
?
2 thioredoxin + H2O2
-
Thunnus maccoyii thioredoxin disulfide + 2 H2O
-
?
2 thioredoxin + t-butyl hydroperoxide
-
Thunnus maccoyii thioredoxin disulfide + H2O + t-butanol
-
?

Subunits

Subunits Comment Organism
? x * 21800, SDS-PAGE and sequence calculation Thunnus maccoyii
More the native SBT Prx enzyme exists as a mixture of dimers, tetramers, decamers and a higher order aggregate Thunnus maccoyii

Synonyms

Synonyms Comment Organism
Prx 2
-
Thunnus maccoyii
typical 2-Cys peroxiredoxin
-
Thunnus maccoyii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Thunnus maccoyii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7
-
Thunnus maccoyii

General Information

General Information Comment Organism
additional information the fish Prx 2 contains the GGLG motif associated with the sensitivity of eukaryotic typical 2-Cys Prx proteins to overoxidation and consequent inactivation by H2O2 Thunnus maccoyii
physiological function peroxiredoxins are cysteine-dependent peroxidases that function as antioxidant enzymes and also in H2O2-mediated cell signaling Thunnus maccoyii