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Information on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin and Organism(s) Rattus norvegicus and UniProt Accession Q63716
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1.11.1.24 thioredoxin-dependent peroxiredoxinIUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
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Word Map
- 1.11.1.24
- catalase
- dismutase
- peroxidases
- s-transferase
- chloroplast
-
peroxidatic
-
hyperoxidation
- gsh
-
anti-oxidant
- glutaredoxins
-
detoxify
-
annexin
- ascorbate
-
thiol-dependent
-
neuroprotective
- leishmania
- cumene
-
sulfenic
-
redox-sensitive
- trx1
-
tert-butyl
-
redox-active
-
h2o2-induced
-
decameric
- mnsod
- trypanothione
-
t-butyl
-
nitrosative
- paraquat
-
glutathionylation
-
h2o2-mediated
- sod2
-
redox-dependent
- cyclophilin
-
2d-dige
- hepatica
- selenocysteine
-
thioredoxin-like
-
peroxide-mediated
-
peroxide-induced
-
peroxidase-like
-
redox-regulated
- ask1
- catalase-peroxidase
- auranofin
- fasciola
-
thiol-based
-
excretory-secretory
-
metal-catalyzed
- thioredoxin-1
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
peroxiredoxin, prdx2, prx i, peroxiredoxin 1, prx ii, prdx5, peroxiredoxin 2, alkyl hydroperoxide reductase, thioredoxin peroxidase, 2-cys prx, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
BCP
-
-
-
-
PrxQ
-
-
-
-
thioredoxin peroxidase
-
-
-
-
Tpx
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [4]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
additional information
?
-
enzyme is inactivated by hyperoxidation of the peroxidatic cysteine to a sulfinic acid in a catalytic cycle-dependent manner. The peroxidase activity of isoform Prx-4 is almost completely inhibited in the reaction with t-butyl hydroperoxide. When H2O2 is used as the substrate, the peroxidase activity significantly remains after oxidative damage. Both reactions result in the same oxidative damage, i.e. sulfinic acid formation at the peroxidatic cysteine
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
0.04
0.08
mutant enzyme C83S/R128K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.1
0.12
0.18
mutant enzyme C83S/R151E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.19
mutant enzyme C83S/R151K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.9
wild type enzyme, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
1
mutant enzyme C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
1.07
mutant enzyme C83S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
1.95
mutant enzyme C83S/C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
2.32
mutant enzyme C83S, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
2.74
wild type enzyme, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.03
mutant enzyme C83S/R128E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.03
mutant enzyme C83S/R128E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.04
mutant enzyme C83S/R128A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.04
mutant enzyme C83S/R128A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.04
mutant enzyme C83S/R128K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.1
mutant enzyme C83S/R151A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.1
mutant enzyme C83S/R151E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.12
mutant enzyme C83S/R151A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.12
mutant enzyme C83S/R151K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
less than 0.002 mg Prx I per mg of soluble protein Prx I, 0.002 mg Prx II per mg of soluble protein, less than 0.004 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and 0.0003 mg Prx VI per mg of soluble protein
-
0.0013 mg Prx I per mg of soluble protein Prx I, 0.0013 mg Prx II per mg of soluble protein, 0.0005 mg Prx III per mg of soluble protein, 0.001 mg Prx V per mg of soluble protein and 0.0017 mg Prx VI per mg of soluble protein
-
0.0013 mg Prx I per mg of soluble protein Prx I, 0.002 mg Prx II per mg of soluble protein, 0.0033 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0003 mg Prx VI per mg of soluble protein
-
0.0013 mg Prx I per mg of soluble protein Prx I, 0.0013 mg Prx II per mg of soluble protein, 0.0005 mg Prx III per mg of soluble protein, 0.0007 mg Prx V per mg of soluble protein and 0.0007 mg Prx VI per mg of soluble protein
-
0.002 mg Prx I per mg of soluble protein Prx I, 0.0007 mg Prx II per mg of soluble protein, 0.0007 mg Prx III per mg of soluble protein, 0.0013 mg Prx V per mg of soluble protein and 0.0003 mg Prx VI per mg of soluble protein
-
0.0007 mg Prx I per mg of soluble protein Prx I, 0.0005 mg Prx II per mg of soluble protein, 0.0007 mg Prx III per mg of soluble protein, 0.0007 mg Prx V per mg of soluble protein and 0.0003 mg Prx VI per mg of soluble protein
-
0.001 mg Prx I per mg of soluble protein Prx I, 0.0013 mg Prx II per mg of soluble protein, 0.0003 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and 0.0017 mg Prx VI per mg of soluble protein
-
0.0003 mg Prx III per mg of soluble protein, 0.0002 mg Prx V per mg of soluble protein and 0.00003 mg Prx VI per mg of soluble protein
-
0.002 mg Prx I per mg of soluble protein Prx I, 0.0033 mg Prx II per mg of soluble protein, 0.0007 mg Prx III per mg of soluble protein, 0.0002 mg Prx V per mg of soluble protein and 0.0002 mg Prx VI per mg of soluble protein
-
0.0002 mg Prx I per mg of soluble protein Prx I, 0.0007 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0007 mg Prx V per mg of soluble protein and 0.0002 mg Prx VI per mg of soluble protein
-
0.0007 mg Prx I per mg of soluble protein Prx I, 0.002 mg Prx II per mg of soluble protein, 0.0003 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and 0.00003 mg Prx VI per mg of soluble protein
-
0.0007 mg Prx I per mg of soluble protein Prx I, 0.001 mg Prx II per mg of soluble protein, 0.0003 mg Prx III per mg of soluble protein, 0.0002 mg Prx V per mg of soluble protein and 0.001 mg Prx VI per mg of soluble protein
-
0.0003 mg Prx I per mg of soluble protein Prx I, 0.0007 mg Prx II per mg of soluble protein, 0.0003 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and 0.00003 mg Prx VI per mg of soluble protein
-
0.0007 mg Prx I per mg of soluble protein Prx I, 0.0007 mg Prx II per mg of soluble protein, 0.0005 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and 0.0002 mg Prx VI per mg of soluble protein
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRDX1_RAT
199
0
22109
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C173S
decameric mutant enzyme, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions
C52S
decameric mutant enzyme, inactive, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions
C83S
dimeric mutant enzyme, mutant exhibits similar peroxidase activity compared to the wild type enzyme
C83S/C173S
increased specific activity with dithiothreitol compared to the wild type enzyme, shows no activity with thioredoxin
C83S/R128A
reduced specific activity compared to the wild type enzyme
C83S/R128E
reduced specific activity compared to the wild type enzyme
C83S/R128K
reduced specific activity compared to the wild type enzyme
C83S/R151A
reduced specific activity compared to the wild type enzyme
C83S/R151EA
reduced specific activity compared to the wild type enzyme
C83S/R151K
reduced specific activity compared to the wild type enzyme
C126S
very weak activity both with substrate H2O2 and t-butyl hydroperoxide
C247S
weak activity both with substrate H2O2 and t-butyl hydroperoxide
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DE-52 column chromatography and 2',5'-ADP-Sepharose affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rhee, S.G.; Kang, S.W.; Chang, T.S.; Jeong, W.; Kim, K.
Peroxiredoxin, a novel family of peroxidases
IUBMB Life
52
35-41
2001
Homo sapiens, Rattus norvegicus
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
J. Biol. Chem.
283
284-293
2008
Rattus norvegicus (Q63716)
EXTERNAL LINKS (specific for EC-Number 1.11.1.24)
Transporter Classification Database (TCDB): 8.A.147.1.1
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