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Literature summary for 1.11.1.24 extracted from

  • Matsumura, T.; Okamoto, K.; Iwahara, S.; Hori, H.; Takahashi, Y.; Nishino, T.; Abe, Y.
    Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization (2008), J. Biol. Chem., 283, 284-293.
    View publication on PubMed
Search for more literature for 1.11.1.24

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain JM109 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C173S decameric mutant enzyme, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions Rattus norvegicus
C52S decameric mutant enzyme, inactive, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions Rattus norvegicus
C83S dimeric mutant enzyme, mutant exhibits similar peroxidase activity compared to the wild type enzyme Rattus norvegicus
C83S/C173S increased specific activity with dithiothreitol compared to the wild type enzyme, shows no activity with thioredoxin Rattus norvegicus
C83S/R128A reduced specific activity compared to the wild type enzyme Rattus norvegicus
C83S/R128E reduced specific activity compared to the wild type enzyme Rattus norvegicus
C83S/R128K reduced specific activity compared to the wild type enzyme Rattus norvegicus
C83S/R151A reduced specific activity compared to the wild type enzyme Rattus norvegicus
C83S/R151EA reduced specific activity compared to the wild type enzyme Rattus norvegicus
C83S/R151K reduced specific activity compared to the wild type enzyme Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
 2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms Rattus norvegicus
23000
-
 10 * 23000, SDS-PAGE, the wild type enzyme exists as a mixture of various forms, favoring the homodecamer at higher protein concentration and lower ionic salt concentration and in the presence of dithiothreitol Rattus norvegicus
44000
-
 dimer, SDS-PAGE Rattus norvegicus
230000
-
 decamer, SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q63716
-
-

Purification (Commentary)

Purification (Comment) Organism
DE-52 column chromatography and 2',5'-ADP-Sepharose affinity column chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.03
-
 mutant enzyme C83S/R128E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.03
-
 mutant enzyme C83S/R128E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.04
-
 mutant enzyme C83S/R128A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.04
-
 mutant enzyme C83S/R128A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.04
-
 mutant enzyme C83S/R128K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.08
-
 mutant enzyme C83S/R128K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.1
-
 mutant enzyme C83S/R151A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.1
-
 mutant enzyme C83S/R151E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.12
-
 mutant enzyme C83S/R151A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.12
-
 mutant enzyme C83S/R151K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
0.18
-
 mutant enzyme C83S/R151E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.19
-
 mutant enzyme C83S/R151K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
0.9
-
 wild type enzyme, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
1
-
 mutant enzyme C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
1.07
-
 mutant enzyme C83S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
1.95
-
 mutant enzyme C83S/C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C Rattus norvegicus
2.32
-
 mutant enzyme C83S, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus
2.74
-
 wild type enzyme, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 + reduced thioredoxin
-
 Rattus norvegicus H2O + oxidized thioredoxin
-
 ?
tert-butyl hydroperoxide + reduced dithiothreitol
-
 Rattus norvegicus tert-butanol + oxidized dithiothreitol
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms Rattus norvegicus
homodecamer 10 * 23000, SDS-PAGE, the wild type enzyme exists as a mixture of various forms, favoring the homodecamer at higher protein concentration and lower ionic salt concentration and in the presence of dithiothreitol Rattus norvegicus

Synonyms

Synonyms Comment Organism
2-Cys peroxiredoxin
-
 Rattus norvegicus
HBP23/Prx I
-
 Rattus norvegicus
heme-binding protein 23/peroxiredoxin belongs to the 2-Cys peroxiredoxin type I family and exhibits peroxidase activity coupled with reduced thioredoxin as an electron donor Rattus norvegicus
Prx I
-
 Rattus norvegicus