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Enzyme Nomenclature
Information on EC 1.11.1.15 - peroxiredoxin
for references in articles please use BRENDA:EC1.11.1.15
Word Map on EC 1.11.1.15
- 1.11.1.15
- superoxide
- peroxidases
- disulfide
- spot
- thiols
- catalase
- injury
- macrophage
- carcinoma
- inflammation
- chloroplast
-
peroxidatic
- gsh
-
anti-oxidant
-
detoxify
-
hyperoxidation
- glutaredoxins
-
annexins
-
redox-sensitive
-
sulfenic
-
thiol-dependent
- leishmania
-
h2o2-induced
- leishmaniasis
-
redox-dependent
- cumene
- trypanothione
-
h2o2-mediated
- cyclophilin
-
decameric
-
t-butyl
-
oxygenase-1
- selenocysteine
-
prohibitin
- infantum
-
2d-dige
-
metal-catalyzed
-
glutathionylation
-
redox-regulated
- fasciola
- mnsod
-
thioredoxin-like
- thioredoxin-1
-
2-related
-
peroxide-mediated
-
excretory-secretory
- tropomyosin
- crithidia
- auranofin
- medicine
-
thiol-based
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.11.1.15
-
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RECOMMENDED NAME
GeneOntology No.
peroxiredoxin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
-
-
-
-
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
the enzyme exhibits a saturable, single-displacement-like reaction mechanism rather than non-saturable double displacement (ping-pong) enzyme substitution mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
thiol-containing-reductant: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 [1]. 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 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 (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), 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 [1]. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor [3]. The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule [4].
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CAS REGISTRY NUMBER
COMMENTARY
207137-51-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
in conditions of oxidative stress, the peroxidatic cysteine can be overoxidized to sulfinic acid inactivating the Prx, the sulfinic 2-Cys Prx is reduced by sulfiredoxin, EC 1.8.98.2, overview
malfunction
-
in conditions of oxidative stress, the peroxidatic cysteine can be overoxidized to sulfinic acid inactivating the Prx, the sulfinic 2-Cys Prx is reduced by sulfiredoxin, EC 1.8.98.2, overview
-
metabolism
-
the enzyme plays an important role in the antioxidant defense system (peroxide-scavenging system) in an anaerobic archaeon Pyrococcus horikoshii
metabolism
-
the enzyme plays an important role in the antioxidant defense system (peroxide-scavenging system) in an anaerobic archaeon Pyrococcus horikoshii
-
physiological function
the enzyme plays a major role in the reponse of the bacterium to oxidative stress
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis
physiological function
-
peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress. Burkholderia BCP is not required for intracellular survival
physiological function
-
peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress
physiological function
peroxiredoxins are cysteine-dependent peroxidases that function as antioxidant enzymes and also in H2O2-mediated cell signaling
physiological function
to survive under oxidative stress imposed by the host, microorganisms express antioxidant proteins, including cysteine-based peroxidases named peroxiredoxins
physiological function
-
the enzyme may play an important role in the resistance against oxygen
physiological function
-
isoform Prx2 can prevent DNA from undergoing oxidative stress. Prx2 is also able to protect NIH/3T3 cells from UV-induced damage
physiological function
dsRNA suppression of isoform Prx IV expression increases anti-white spot syndrome virus replication in shrimp, whereas recombinant Prx IV injection into shrimp decreases anti-white spot syndrome virus replication
physiological function
E8VQ78, E8VUX3
isoform Prx2 effectively scavenges low levels of peroxides because of its high affinity to H2O2, whereas Prx1 quickly degrades higher levels of peroxides because of its high turnover rate and more efficient reactivation; isoform Prx2 effectively scavenges low levels of peroxides because of its high affinity to H2O2, whereas Prx1 quickly degrades higher levels of peroxides because of its high turnover rate and more efficient reactivation
physiological function
-
neither overexpression in bloodstream cells nor the deletion of both alleles of isoform Px IV in bloodstream or procyclic parasites affects the in vitro proliferation
physiological function
-
peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress. Burkholderia BCP is not required for intracellular survival
-
physiological function
-
the enzyme plays a major role in the reponse of the bacterium to oxidative stress
-
physiological function
-
isoform Prx2 effectively scavenges low levels of peroxides because of its high affinity to H2O2, whereas Prx1 quickly degrades higher levels of peroxides because of its high turnover rate and more efficient reactivation; isoform Prx2 effectively scavenges low levels of peroxides because of its high affinity to H2O2, whereas Prx1 quickly degrades higher levels of peroxides because of its high turnover rate and more efficient reactivation
-
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of Prdx6 gene regulation, overview. Transcription is activated by binding of the transcription factor Nrf2 to the ARE whereas transcription is inhibited by the binding of Nrf3. Prdx6 expression also is responsive to hormonal regulation
additional information
-
regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body; regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body
additional information
regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body; regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body
additional information
regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body; regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body
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
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
additional information
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfenic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx by sulfiredoxin, catalytic cycle of 2-Cys Prx, overview. The knockout mutant plants without Srx or 2-Cys Prx exhibit phenotypical differences under growth conditions of 16 h light, probably due to the signalling role of the sulfinic form of Prx
additional information
although this Tp peroxiredoxin closely resembles AhpC-like peroxidoxins, Treponema pallidum lacks AhpF, the typical reductant for such enzymes. Functionally, TpAhpC resembles largely eukaryotic, nonAhpC typical 2-Cys Prx proteins in using thioredoxin as an efficient electron donor and exhibiting broad specificity toward hydroperoxide substrates
additional information
-
although this Tp peroxiredoxin closely resembles AhpC-like peroxidoxins, Treponema pallidum lacks AhpF, the typical reductant for such enzymes. Functionally, TpAhpC resembles largely eukaryotic, nonAhpC typical 2-Cys Prx proteins in using thioredoxin as an efficient electron donor and exhibiting broad specificity toward hydroperoxide substrates
additional information
-
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfenic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx by sulfiredoxin, catalytic cycle of 2-Cys Prx, overview. The knockout mutant plants without Srx or 2-Cys Prx exhibit phenotypical differences under growth conditions of 16 h light, probably due to the signalling role of the sulfinic form of Prx
-
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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
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
-
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
-
specific substrate for peroxiredoxin 6
-
-
?
arachidonic acid hydroperoxide + tryparedoxin
arachidonic acid + oxidized tryparedoxin
-
-
-
-
?
cumene hydroperoxide + reduced dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
low activity
-
-
?
cumene hydroperoxide + reduced glutaredoxin
2-phenylpropan-2-ol + oxidized glutaredoxin
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
cumene hydroperoxide + tryparedoxin 2
2-phenylpropan-2-ol + oxidized tryparedoxin 2
-
57% of the activity with H2O2
-
-
?
ethyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
-
-
-
?
H2O2 + NADPH
H2O + NADP+
-
reaction is driven by glutathione which is maintained reduced via NADPH and glutathione reductase. Both the peroxiredoxin and glutaredoxin domains are biochemically active in the natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain. When expressed separately, the glutaredoxin domain is catalytically active and the peroxiredoxin domain posseses a weak activity when supplemented with expoenous glutaredoxin
-
-
?
H2O2 + S128WNTD
H2O + ?
S128WNTD is the S128W mutant of the N-terminal domain of AhpF (a flavoprotein disulfide reductase)
-
-
?
H2O2 + thioredoxin
?
1-Cys peroxiredoxin is less active than 2-Cys peroxiredoxin
-
-
?
iodoacetamide + reduced thioredoxin
?
-
Prx 3 reacts very slowly with iodoacetamide
-
-
?
linoleic acid hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
-
-
-
?
linoleic acid hydroperoxide + tryparedoxin 2
?
-
7.8% of the activity with H2O2
-
-
?
N-ethylmaleimide + reduced thioredoxin
?
-
Prx 3 reacts very slowly with N-ethylmaleimide
-
-
?
peroxynitrite + H2O2
nitrite + ?
-
CPX and MPX catalytically reduce peroxynitrite to nitrite through a fast-reacting thiol group located at the peroxidatic cysteine residue (Cys52 and Cys81 in CPX and MPX respectively), thus acting as tryparedoxin/peroxynitrite oxidoreductases
-
-
?
peroxynitrite + reduced thioredoxin
?
-
AhpE reduces peroxynitrite 2 orders of magnitude faster than H2O2
-
-
?
phosphatidyl choline hydroperoxide + tryparedoxin 2
?
-
3.8% of the activity with H2O2
-
-
?
phosphatidylcholine hydroperoxide + reduced glutaredoxin
? + oxidized glutaredoxin
-
-
-
-
?
tert-butyl hydroperoxide + reduced glutaredoxin
tert-butanol + oxidized glutaredoxin
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
-
-
-
-
?
tert-butyl hydroperoxide + tryparedoxin 2
tert-butanol + oxidized tryparedoxin 2
-
95% of the activity with H2O2
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
-
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
40% of the activity with H2O2
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
about 10% of the activity with H2O2
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
-
?
H2O2 + NADPH + H+
2 H2O + 2 NADP+
E8VQ78, E8VUX3
isoform Prx2 is able to reduce H2O2 in vitro in the presence of thioredoxin A/thioredoxin reductase as electron donors
-
-
?
H2O2 + NADPH + H+
2 H2O + 2 NADP+
E8VQ78, E8VUX3
isoform Prx2 is able to reduce H2O2 in vitro in the presence of thioredoxin A/thioredoxin reductase as electron donors
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
acts as a catalyst in ferrithiocyanate system and protects supercoiled form of plasmid DNA from damage in metal-catalyzed oxidation system in vitro
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
reduced Prx2 is exceptionally reactive withH2O2 and other peroxides but shows very low reactivity with other thiol oxidants and alkylating agents
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
reaction is dependent on thioredoxin
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
Prx 3 displays strong reactivity with H2O2
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
thioredoxin from Escherichia coli and thioredoxin f and m from spinach
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
ping-pong kinetics
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
A1KXR1
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
ping-pong mechanism
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
the enzyme works on the basis of a monothiol mechanism
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
E8VQ78, E8VUX3
-
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
E8VQ78, E8VUX3
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
50% of the activity with H2O2
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
low activity
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
about 60% of the activity with H2O2
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
9.5% of the activity with tert-butyl hydroperoxide and tryparedoxin 2
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
additional information
?
-
-
the photosynthetic machinery needs high levels of enzyme during leaf development to protect it from oxidative damage. The damage is reduced by the accumulation of 2-CP protein, by the de novo synthesis and replacement of damaged proteins, and by the induction of other antioxidant defenses in 2-CP mutants
-
-
-
additional information
?
-
-
Prx Q attaches to photosystem II and has a specific function distinct from 2-Cys peroxiredoxin in protecting photosynthesis. Its absence causes metabolic changes that are sensed and trigger appropriate compensatory responses
-
-
-
additional information
?
-
-
the enzyme is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
-
-
-
additional information
?
-
-
insignificant affinity towards complex phospholipid hydroperoxide
-
-
-
additional information
?
-
-
enzyme reduces hydrogen peroxide and peroxynitrite with rate constants of 11000 and 2000 mM/s, respectively, at pH 7.4 and 25°C. Reduction of tert-butyl hydroperoxide is slower
-
-
-
additional information
?
-
enzyme reduces hydrogen peroxide and peroxynitrite with rate constants of 11000 and 2000 mM/s, respectively, at pH 7.4 and 25°C. Reduction of tert-butyl hydroperoxide is slower
-
-
-
additional information
?
-
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
additional information
?
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
-
additional information
?
-
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
-
additional information
?
-
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
-
additional information
?
-
-
Burkholderia cenocepacia BCP homologue functions through a 1-Cys catalytic pathway. During catalysis, BcBCP can utilize thioredoxin as a reductant for the sulfenic acid intermediate. However, significantly higher peroxidase activity is observed utilizing glutathione as a resolving cysteine and glutaredoxin as a redox partner, substrate specificity, overview
-
-
-
additional information
?
-
-
Burkholderia cenocepacia BCP homologue functions through a 1-Cys catalytic pathway. During catalysis, BcBCP can utilize thioredoxin as a reductant for the sulfenic acid intermediate. However, significantly higher peroxidase activity is observed utilizing glutathione as a resolving cysteine and glutaredoxin as a redox partner, substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q5W9B5
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
-
Escherichia coli BCP catalyzes the reduction of hydroperoxides and is an atypical 2-Cys peroxiredoxin that functions through the formation of an intramolecular disulfide bond between the active and resolving cysteine. An engineered Escherichia coli BCP, which lacks the resolving cysteine, retains enzyme activity through a different catalytic pathway, substrate specificity, overview
-
-
-
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
-
additional information
?
-
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
-
additional information
?
-
-
the enzyme promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue
-
-
-
additional information
?
-
-
together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2
-
-
-
additional information
?
-
-
the enzyme exhibits a low level of phospholipiase A2 activity at acidic pH
-
-
-
additional information
?
-
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
Prx1 shows a androgen receptor-stimulating function in response to hypoxia/reoxygenation
-
-
-
additional information
?
-
-
thioredoxin 2 directly associates with Prx3 in vivo and functions in protection against cell death
-
-
-
additional information
?
-
-
peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
-
additional information
?
-
-
isoform Prx2 is able to prevent supercoiled pUC18 plasmid DNA from oxidative cleavage by reactive oxygen species. Prx2 treatment inhibits the UV-mediated apoptosis. Prx2 treatment decreases reactive oxygen species production in NIH/3T3 cells induced by UV exposure
-
-
-
additional information
?
-
-
the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane
-
-
-
additional information
?
-
-
tryparedoxin peroxidase activity. The enzyme does not follow a classic ping-pong mechanism
-
-
-
additional information
?
-
-
the enzyme is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
-
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
-
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
Prx I can be used as an indicator of microglial activation
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
-
additional information
?
-
-
antioxidant activity may be the primary function of the enzyme
-
-
-
additional information
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
-
-
-
additional information
?
-
-
Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
-
-
-
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
-
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
-
additional information
?
-
-
after subjection to exogenous and endogenous oxidative stress, the Plasmodium falciparum blood stage form shows a marked elevation of PfTrx-Px1 mRNA and protein levels consistent with the structure of related proteins
-
-
-
additional information
?
-
-
Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
-
-
-
additional information
?
-
-
the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
-
-
-
additional information
?
-
-
cumene hydroperoxide is not accepted as a substrate
-
-
-
additional information
?
-
-
PfTPx1 also possesses peroxynitrite reductase activity
-
-
-
additional information
?
-
-
Prx IV is a secretable protein and may exert its protective function against oxidative damage by scavenging reactive oxygen species in the extracellular space
-
-
-
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
peroxiredoxin 6 differs from other mammalian peroxiredoxins both in its ability to reduce phospholipid hydroperoxides at neutral pH and in having phospholipase A2 activity that is maximal at acidic pH
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
DTT is not a physiological reductant and thioredoxin, the reductant that is active in the catalytic cycle for the 2-Cys peroxiredoxins, is not effective as a reductant for 1-Cys Prdx6. Prdx6 binds and reduces phospholipid hydroperoxides. Prdx6 reduces H2O2 and other short chain hydroperoxides. The conserved Cys in Prdx6 is buried at the base of a narrow pocket. This location renders it unable to dimerize through disulfide formation in the native configuration but homodimers (and multimers) can arise through hydrophobic interactions. Disulfide formation may occur with denatured proteins and heterodimerization also occurs normally as part of the catalytic cycle. The protein also contains a surface expressed catalytic triad, S-D-H, that is important for phospholipid binding and enzymatic activities
-
-
-
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
-
-
-
additional information
?
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
-
additional information
?
-
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
-
additional information
?
-
-
cPrx I and cPrx II function both as peroxidases and as molecular chaperones. The peroxidase function predominates in the lower molecular weight forms, whereas the chaperone function predominates in the higher molecular weight complexes. Oxidative stress and heat shock exposure of yeasts cause the protein structures of cPrxl and cPrx II to shift from low MW species to high molecular weight complexes. This triggers a peroxidase-to-chaperone functional switch
-
-
-
additional information
?
-
-
Gpx2 is likely to play an important role in the protection of cells from oxidative stress in the presence of Ca2+
-
-
-
additional information
?
-
-
Prx1 is particularly required to protect against mitochondrial oxidation, Prx1 requires thioredoxin reductase 2 and the glutathione system, but not thioredoxin 3, to promote oxidant resistance
-
-
-
additional information
?
-
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
-
additional information
?
-
-
Tpx1 is an upstream activator of Pap1. At low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations
-
-
-
additional information
?
-
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
-
-
-
additional information
?
-
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
-
-
-
additional information
?
-
-
Bcp2 plays an important role in the peroxide-scavaging system in Sulfolobus solfataricus. The enzyme protects plasmid DNA from nicking by the metal-catalysed oxidation system
-
-
-
additional information
?
-
-
Bcp2 plays an important role in the peroxide-scavaging system in Sulfolobus solfataricus. The enzyme protects plasmid DNA from nicking by the metal-catalysed oxidation system
-
-
-
additional information
?
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
additional information
?
-
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
additional information
?
-
-
peroxidases belonging to the class of 1-Cys and 2-Cys peroxiredoxins play crucial roles in maintaining redox balance. TgTrx-Px1 is an extremely potent antioxidant
-
-
-
additional information
?
-
-
TgPrx2 has general antioxidant properties as indicated by its ability to protect glutamine synthetase against a dithiothreitol Fe3+-catalyzed system. TgPrx2 does not reduce H2O2 or tert-butyl hydroperoxide at the expense of glutaredoxin, thioredoxin or glutathione
-
-
-
additional information
?
-
TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
-
-
-
additional information
?
-
-
TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
-
-
-
additional information
?
-
-
catalyzes the trypanothione/tryparedoxin-dependent reduction of hydrogen peroxide and, even more efficiently, of arachidonic acid hydroperoxide
-
-
-
additional information
?
-
E8VQ78
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
E8VUX3
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
E8VQ78
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
E8VUX3
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
Cys83 is the resolving cysteine of XfPrxQ
-
-
-
additional information
?
-
-
Cys83 is the resolving cysteine of XfPrxQ
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
-
glutathione is the primary native reductant
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
-
-
-
-
?
additional information
?
-
-
the photosynthetic machinery needs high levels of enzyme during leaf development to protect it from oxidative damage. The damage is reduced by the accumulation of 2-CP protein, by the de novo synthesis and replacement of damaged proteins, and by the induction of other antioxidant defenses in 2-CP mutants
-
-
-
additional information
?
-
-
Prx Q attaches to photosystem II and has a specific function distinct from 2-Cys peroxiredoxin in protecting photosynthesis. Its absence causes metabolic changes that are sensed and trigger appropriate compensatory responses
-
-
-
additional information
?
-
-
the enzyme is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
-
-
-
additional information
?
-
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
additional information
?
-
Q9NL98
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
additional information
?
-
O77834
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
Burkholderia cenocepacia BCP homologue functions through a 1-Cys catalytic pathway. During catalysis, BcBCP can utilize thioredoxin as a reductant for the sulfenic acid intermediate. However, significantly higher peroxidase activity is observed utilizing glutathione as a resolving cysteine and glutaredoxin as a redox partner, substrate specificity, overview
-
-
-
additional information
?
-
-
Burkholderia cenocepacia BCP homologue functions through a 1-Cys catalytic pathway. During catalysis, BcBCP can utilize thioredoxin as a reductant for the sulfenic acid intermediate. However, significantly higher peroxidase activity is observed utilizing glutathione as a resolving cysteine and glutaredoxin as a redox partner, substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q5W9B5
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q5W9B6
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q5W9B7
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
-
Escherichia coli BCP catalyzes the reduction of hydroperoxides and is an atypical 2-Cys peroxiredoxin that functions through the formation of an intramolecular disulfide bond between the active and resolving cysteine. An engineered Escherichia coli BCP, which lacks the resolving cysteine, retains enzyme activity through a different catalytic pathway, substrate specificity, overview
-
-
-
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
-
additional information
?
-
P21762
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
-
additional information
?
-
-
the enzyme promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue
-
-
-
additional information
?
-
-
together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2
-
-
-
additional information
?
-
-
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane
-
-
-
additional information
?
-
-
the enzyme is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
-
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
-
additional information
?
-
O08709
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
Prx I can be used as an indicator of microglial activation
-
-
-
additional information
?
-
-
the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
-
-
-
additional information
?
-
-
antioxidant activity may be the primary function of the enzyme
-
-
-
additional information
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
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additional information
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Q9GSV3
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
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-
-
additional information
?
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Q9N699
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
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additional information
?
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after subjection to exogenous and endogenous oxidative stress, the Plasmodium falciparum blood stage form shows a marked elevation of PfTrx-Px1 mRNA and protein levels consistent with the structure of related proteins
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additional information
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Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
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additional information
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the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
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additional information
?
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Prx IV is a secretable protein and may exert its protective function against oxidative damage by scavenging reactive oxygen species in the extracellular space
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-
-
additional information
?
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O35244
the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
?
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peroxiredoxin 6 differs from other mammalian peroxiredoxins both in its ability to reduce phospholipid hydroperoxides at neutral pH and in having phospholipase A2 activity that is maximal at acidic pH
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additional information
?
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the 1-Cys Prdx type Prdx6, possessing a single conserved cysteine residue, shows heterodimerization with piGSH S-transferase as part of the catalytic cycle, and the ability to either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (PLA2 activity), thus exhiting peroxidase and phospholipase activities, overview. The bifunctional protein has separate active sites for both activities, namely a Cys 47-dependent peroxidase activity site and a Ser32-dependent PLA2 activity site. Substrate specificity, overview
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additional information
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O69777
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
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additional information
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constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
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additional information
?
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Gpx2 is likely to play an important role in the protection of cells from oxidative stress in the presence of Ca2+
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additional information
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Prx1 is particularly required to protect against mitochondrial oxidation, Prx1 requires thioredoxin reductase 2 and the glutathione system, but not thioredoxin 3, to promote oxidant resistance
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additional information
?
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isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
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additional information
?
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isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
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additional information
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peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
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additional information
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Tpx1 is an upstream activator of Pap1. At low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations
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additional information
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B9USM4
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
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additional information
?
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Bcp2 plays an important role in the peroxide-scavaging system in Sulfolobus solfataricus. The enzyme protects plasmid DNA from nicking by the metal-catalysed oxidation system
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additional information
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Bcp2 plays an important role in the peroxide-scavaging system in Sulfolobus solfataricus. The enzyme protects plasmid DNA from nicking by the metal-catalysed oxidation system
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additional information
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Q9TSX9
the enzyme functions in antioxidant defense and lung phospholipid metabolism
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additional information
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peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
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additional information
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peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
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additional information
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peroxidases belonging to the class of 1-Cys and 2-Cys peroxiredoxins play crucial roles in maintaining redox balance. TgTrx-Px1 is an extremely potent antioxidant
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
thioredoxin
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Benzoate
-
in orthorhombic 1 form, the benzoate ion is present close to the Cp residue in both fully folded subunits the benzoate ion is not observed in the six oxidized subunits in which the disulfide bond is formed
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
3 mM ATP in concert with Mg2+, Ca2+, Mn2+, or Zn2+ lowers the peroxidase activity in a dose-dependent manner
Mg2+
in the presence of 2 mM Mg2+, the rate of H2O2 removal is inhibited by 60%, 5% and 5% when it is assayed with 2 mM ADP, AMP or phosphate, respectively, total inactivation of 2-Cys Prx is caused by incubation with 3 mM ATP and 3 mM Mg2+
peptidoglycan
downregulates Prx expression in lymphoid tissue and heart, but not in hemocytes
H2O2
-
highly susceptible to inactivation by H2O2; highly susceptible to inactivation by H2O2
H2O2
-
significant reductions in Prx II is detected at H2O2 concentrations above 0.6 mM; significant reductions in Prx I is detected at H2O2 concentrations above 0.6 mM
H2O2
high concentrations of H2O2 temporarily inactivate Tpx1
H2O2
E8VQ78, E8VUX3
1 mM H2O2 overoxidizes isoform Prx2 at the peroxidatic cysteine and results in the loss of the peroxidase activity
imidazole
approximately 70% of the Prx activity is lost in the presence of 0.4 M imidazole or higher. The presence of 1.6 M imidazole seems to promote protein degradation
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mercaptosuccinate
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a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
MJ33
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a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
SDS
activity is lost completely in the presence of 1% SDS or higher
additional information
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serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
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additional information
during exposure to haemorrhagic septicaemia virus, HdPrxVI mRNA transcription is downregulated in the gill
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additional information
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during exposure to haemorrhagic septicaemia virus, HdPrxVI mRNA transcription is downregulated in the gill
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additional information
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H2O2 does not cause dose-dependent reduction in expression of isoform Prx IV; H2O2 does not cause dose-dependent reduction in expression of isoform Prx V
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additional information
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serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
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additional information
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serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
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additional information
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serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
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additional information
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insensitive to hygromycin, paromomycin, and cycloheximide
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additional information
neither tert-butyl hydroperoxide nor cumene hydroperoxide demonstrate any observable inactivation of the enzyme, even when present at concentrations as high as 60 mM
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additional information
TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates
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additional information
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TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
forkhead box transcription factor 3A
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depletion of forkhead box transcription factor 3A leads to a dramatic reduction of Prx III mRNA showing that endogenous FOXO3A is necessary for base-line expression of Prx
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dithiothreitol
in the H2O2 reduction assay, AbTPx1 shows the ability to remove H2O2 without the presence of dithiothreitol. However, removal of H2O2 is promoted with the presence of dithiothreitol; in the H2O2 reduction assay, AbTPx2 shows the ability to remove H2O2 without the presence of dithiothreitol. However, removal of H2O2 is promoted with the presence of dithiothreitol
dithiothreitol
A1KXR1
dithiothreitol is capable of reducing the oxidised form of the Prx1 to regenerate its activity
H2O2
-
treatment of with H2O2 results in the dose-dependent expressions of Prx I at protein and mRNA levels; treatment of with H2O2 results in the dose-dependent expressions of Prx II at protein and mRNA levels
H2O2
the total expression of Prx I is increased in response to H2O2; the total expression of Prx VI is increased in response to H2O2
additional information
AbTPx1 gene expression is induced by oxidative stress; AbTPx2 gene expressions is induced by oxidative stress
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additional information
AbTPx1 gene expression is induced by oxidative stress; AbTPx2 gene expressions is induced by oxidative stress
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additional information
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Prx I expression is upregulated in microglia after lipopolysaccharide stimulation (0.001 mg/ml)
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additional information
A1KXR1
Prx1's ability to remove H2O2 is not supported by the presence of 1 mM GSH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
Ethyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.00665
cumene hydroperoxide
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
0.00848
cumene hydroperoxide
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PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
0.107
cumene hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.152
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
0.191
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
0.00098
H2O2
pH 7.0, temperature not specified in the publication, Prx231
0.0014
H2O2
-
pH 7.0, 25°C, wild-type enzyme
0.0014
H2O2
in 50 mM potassium phosphate pH 7.0, at 25°C
0.0016
H2O2
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pH 7.0, 25°C, mutant enzyme T77V
0.0032
H2O2
pH 7.0, temperature not specified in the publication, Prx197
0.062
H2O2
-
pH 7.0, 25°C, mutant enzyme T77D
0.0934
H2O2
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pH 7.0, 25°C, mutant enzyme T77I
0.18
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
0.193
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
0.13
tert-butyl hydroperoxide
-
in 7 mM phosphate buffer, pH 7.3, 150 mM NaCl, at 25°C
0.238
tert-butyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
additional information
additional information
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the Km-value for H2O2 is below 0.02 mM
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additional information
additional information
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
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additional information
additional information
SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH
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additional information
additional information
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SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE