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Literature summary extracted from

  • Loo, G.H.; Schuller, K.A.
    Cloning and functional characterization of a peroxiredoxin 4 from yellowtail kingfish (Seriola lalandi) (2010), Comp. Biochem. Physiol. B, 156, 244-253.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 gene prx4, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression of enzyme versions PRX264, Prx231, and Prx197 in Escherichia coli strain BL21(DE3) Seriola lalandi

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.24 additional information construction of shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not Seriola lalandi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.24 additional information
-
 additional information both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics Seriola lalandi
1.11.1.24 0.00098
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 0.0032
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 0.152
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 0.18
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 0.191
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 0.193
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.24 2 thioredoxin + ROOH Seriola lalandi
-
 thioredoxin disulfide + H2O + ROH
-
 ?
1.11.1.24 additional information Seriola lalandi shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Seriola lalandi B9USM4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24 recombinant enzyme versions PRX264, Prx231, and Prx197 from Escherichia coli strain BL21(DE3) Seriola lalandi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 2 thioredoxin + cumene hydroperoxide
-
 Seriola lalandi thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
 ?
1.11.1.24 2 thioredoxin + H2O2
-
 Seriola lalandi thioredoxin disulfide + 2 H2O
-
 ?
1.11.1.24 2 thioredoxin + ROOH
-
 Seriola lalandi thioredoxin disulfide + H2O + ROH
-
 ?
1.11.1.24 2 thioredoxin + t-butyl hydroperoxide
-
 Seriola lalandi thioredoxin disulfide + H2O + t-butanol
-
 ?
1.11.1.24 additional information shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not Seriola lalandi ?
-
 ?
1.11.1.24 additional information both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics Seriola lalandi ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 2-Cys peroxiredoxin 4
-
 Seriola lalandi
1.11.1.24 peroxiredoxin 4
-
 Seriola lalandi
1.11.1.24 Prx 4
-
 Seriola lalandi
1.11.1.24 typical 2-Cys Prx
-
 Seriola lalandi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.24 3.2
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 7.3
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 10.4
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 15.2
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 22.3
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 24.6
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.11.1.24 50
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 160
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 380
-
 cumene hydroperoxide pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 580
-
 t-butyl hydroperoxide pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi
1.11.1.24 710
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx197 Seriola lalandi
1.11.1.24 2500
-
 H2O2 pH 7.0, temperature not specified in the publication, Prx231 Seriola lalandi