Information on EC 1.11.1.15 - peroxiredoxin

New: Word Map on EC 1.11.1.15
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.11.1.15
-
RECOMMENDED NAME
GeneOntology No.
peroxiredoxin
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
show the reaction diagram
-
-
-
-
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
show the reaction diagram
the enzyme exhibits a saturable, single-displacement-like reaction mechanism rather than non-saturable double displacement (ping-pong) enzyme substitution mechanism
P91883
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
-
-
glutathione metabolism
-
-
Metabolic pathways
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY
207137-51-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
strain K1
UniProt
Manually annotated by BRENDA team
Aeropyrum pernix DSM 11879
-
UniProt
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia
-
UniProt
Manually annotated by BRENDA team
isoform peroxiredoxin 6
UniProt
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
BiPrx1; gene BiPrx1 encoding a 1-Cys type Prx
UniProt
Manually annotated by BRENDA team
BiTPrx1; gene BiTPx1 encoding a 2-Cys type Prx
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
subsp. pekinensis
SwissProt
Manually annotated by BRENDA team
Burkholderia cenocepacia K56-2
-
-
-
Manually annotated by BRENDA team
Zhikong scallop
UniProt
Manually annotated by BRENDA team
Chinese mitten crab
UniProt
Manually annotated by BRENDA team
var. Gerbel
-
-
Manually annotated by BRENDA team
tammar wallaby
UniProt
Manually annotated by BRENDA team
kuruma shrimp
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain
-
-
Manually annotated by BRENDA team
L. cv. Dong-jin
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
BKM-F-1767
-
-
Manually annotated by BRENDA team
1-Cys peroxiredoxin
SwissProt
Manually annotated by BRENDA team
2-Cys peroxiredoxin
SwissProt
Manually annotated by BRENDA team
isoform peroxiredoxin 1
UniProt
Manually annotated by BRENDA team
Populus tremula x Populus tremuloides
SwissProt
Manually annotated by BRENDA team
sheep scab mite
UniProt
Manually annotated by BRENDA team
isozyme Gpx1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YPH250
isozyme Gpx1
-
-
Manually annotated by BRENDA team
Staphylococcus aureus NCTC 8325
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
i.e. Taiwanofungus camphoratus
SwissProt
Manually annotated by BRENDA team
Thermus aquaticus YT-1
YT-1
-
-
Manually annotated by BRENDA team
gene TP0509
UniProt
Manually annotated by BRENDA team
gene prxq or bcp
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
Q96291
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
physiological function
A9QKS0
peroxiredoxins are cysteine-dependent peroxidases that function as antioxidant enzymes and also in H2O2-mediated cell signaling
physiological function
-
peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress
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
-
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
Q2FXL3
the enzyme plays a major role in the reponse of the bacterium to oxidative stress
physiological function
Q9PER7
to survive under oxidative stress imposed by the host, microorganisms express antioxidant proteins, including cysteine-based peroxidases named peroxiredoxins
physiological function
O58966
the enzyme may play an important role in the resistance against oxygen
physiological function
A8R072
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
-
isoform Prx2 can prevent DNA from undergoing oxidative stress. Prx2 is also able to protect NIH/3T3 cells from UV-induced damage
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
physiological function
Staphylococcus aureus NCTC 8325
-
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
-
physiological function
Burkholderia cenocepacia K56-2
-
peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress. Burkholderia BCP is not required for intracellular survival
-
malfunction
Arabidopsis thaliana Columbia
-
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
-
additional information
O83522
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
-
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 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
Q96291
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
A9QKS0
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
Arabidopsis thaliana Columbia
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-arichidonoyl-sn-glycero-3-phosphocholine + GSH
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
show the reaction diagram
-
specific substrate for peroxiredoxin 6
-
-
?
2 GSH + H2O2
GSSG + 2 H2O
show the reaction diagram
Burkholderia cenocepacia, Burkholderia cenocepacia K56-2
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
Burkholderia cenocepacia K56-2
-
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
show the reaction diagram
B9USM4
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
show the reaction diagram
A9QKS0
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
show the reaction diagram
Q9PER7
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
show the reaction diagram
O83522
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
-
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
B9USM4
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
A9QKS0
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
Q9PER7
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
O83522
-
-
-
?
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
Aeropyrum pernix DSM 11879
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
B9USM4
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
C3VVL4, C3VVL6
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
Burkholderia cenocepacia K56-2
-
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
show the reaction diagram
B9USM4
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
show the reaction diagram
A9QKS0
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
show the reaction diagram
Q9PER7
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
show the reaction diagram
O83522
-
-
-
?
arachidonoyl hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
-
40% of the activity with H2O2
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
P32119
low activity
-
-
?
cumene hydroperoxide + reduced glutaredoxin
2-phenylpropan-2-ol + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
Q1AN22
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
P0A251
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
B6RB12
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
-
about 10% of the activity with H2O2
-
-
?
cumene hydroperoxide + reduced thioredoxin
?
show the reaction diagram
P91883
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + tryparedoxin 2
2-phenylpropan-2-ol + oxidized tryparedoxin 2
show the reaction diagram
-
57% of the activity with H2O2
-
-
?
dithiothreitol + H2O2
oxidized dithiothreitol + H2O
show the reaction diagram
Q9U5A1
-
-
-
?
ethyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
P0A251
-
-
-
?
Gardos channel + ?
?
show the reaction diagram
-
activates the Gardos channel
-
-
?
glycine chloramine + dithiothreitol
?
show the reaction diagram
P32119
slow reaction
-
-
?
H2O2 + 2 GSH
2 H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
Q5W9B5, Q5W9B6, Q5W9B7
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
O69777
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
A1KXU3
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + ferrithiocyanate
?
show the reaction diagram
Phanerochaete chrysosporium, Phanerochaete chrysosporium BKM-F-1767
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
O08709
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
O35244
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
O77834
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Q9TSX9
-
-
-
?
H2O2 + NADPH
H2O + NADP+
show the reaction diagram
-
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 + NADPH + H+
2 H2O + 2 NADP+
show the reaction diagram
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+
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
Q74887
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
A8D0B7
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
show the reaction diagram
P32119
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
show the reaction diagram
Q97VL0
-
-
-
?
H2O2 + reduced glutaredoxin
H2O + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced plasmoredoxin
H2O + oxidized plasmoredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q13162
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
P91883
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
P21762
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
P35704, Q63716, Q9R063, Q9Z0V6
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
O69777
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q9FUC5
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q74887
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
B3SP74
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
A0ZXY5
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
P0A251
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
B1N693, B1N694
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
B6RB12
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
A1KXR1
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
B6V3F6
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q21824, Q8IG31
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
ping-pong mechanism
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
ping-pong kinetics
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
reaction is dependent on thioredoxin
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
thioredoxin from Escherichia coli and thioredoxin f and m from spinach
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
the enzyme works on the basis of a monothiol mechanism
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q97VL0, Q97WG5, Q97WP9
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
-
Prx 3 displays strong reactivity with H2O2
-
-
?
H2O2 + reduced thioredoxin 2
H2O + oxidized thioredoxin 2
show the reaction diagram
-
-
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
show the reaction diagram
E8VQ78, E8VUX3
-
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
show the reaction diagram
E8VQ78, E8VUX3
-
-
-
?
H2O2 + S128WNTD
H2O + ?
show the reaction diagram
P0AE08
S128WNTD is the S128W mutant of the N-terminal domain of AhpF (a flavoprotein disulfide reductase)
-
-
?
H2O2 + thioredoxin
?
show the reaction diagram
Q9GSV3, Q9N699
1-Cys peroxiredoxin is less active than 2-Cys peroxiredoxin
-
-
?
H2O2 + tryparedoxin 2
H2O + oxidized tryparedoxin 2
show the reaction diagram
-
-
-
-
?
histamine chloramine + dithiothreitol
?
show the reaction diagram
P32119
slow reaction
-
-
?
HOCl + dithiothreitol
?
show the reaction diagram
P32119
low activity
-
-
?
iodoacetamide + reduced thioredoxin
?
show the reaction diagram
-
Prx 3 reacts very slowly with iodoacetamide
-
-
?
linoleic acid hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
P0A251
-
-
-
?
linoleic acid hydroperoxide + tryparedoxin 2
?
show the reaction diagram
-
7.8% of the activity with H2O2
-
-
?
linolenoyl hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linoleoyl hydroperoxide + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
N-ethylmaleimide + reduced thioredoxin
?
show the reaction diagram
-
Prx 3 reacts very slowly with N-ethylmaleimide
-
-
?
NADPH + H2O2
NADP+ + H2O
show the reaction diagram
Q9SQJ4
-
-
-
?
paraquat + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
peroxinitrite + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
peroxinitrite + thioredoxin
?
show the reaction diagram
-
-
-
-
?
peroxynitrite + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
peroxynitrite + H2O2
nitrite + ?
show the reaction diagram
-
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
?
show the reaction diagram
-
AhpE reduces peroxynitrite 2 orders of magnitude faster than H2O2
-
-
?
phosphatidyl choline hydroperoxide + tryparedoxin 2
?
show the reaction diagram
-
3.8% of the activity with H2O2
-
-
?
phosphatidylcholine hydroperoxide + reduced glutaredoxin
? + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
taurine chloramine + dithiothreitol
?
show the reaction diagram
P32119
slow reaction
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
50% of the activity with H2O2
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
t-butanol + GSSG
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
show the reaction diagram
Q8S3L0
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
A1KZ88
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
Q1AN22
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
P32119
low activity
-
-
?
tert-butyl hydroperoxide + reduced glutaredoxin
tert-butanol + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
P0A251
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
B1N693, B1N694
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
9.5% of the activity with tert-butyl hydroperoxide and tryparedoxin 2
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
about 60% of the activity with H2O2
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
Q97VL0, Q97WG5, Q97WP9
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
?
show the reaction diagram
P91883
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + tryparedoxin 2
tert-butanol + oxidized tryparedoxin 2
show the reaction diagram
-
95% of the activity with H2O2
-
-
?
monochloramine + dithiothreitol
?
show the reaction diagram
P32119
slow reaction
-
-
?
additional information
?
-
Q9GSV3, Q9N699
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
?
-
-
antioxidant activity may be the primary function of the enzyme
-
-
-
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
?
-
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
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 is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
-
additional information
?
-
Q5W9B5, Q5W9B6, Q5W9B7
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q9NL98
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
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
?
-
-
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 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
?
-
-
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
?
-
-
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
?
-
-
no activity with glutaredoxin or glutathione
-
-
-
additional information
?
-
-
the enzyme exhibits a low level of phospholipiase A2 activity at acidic pH
-
-
-
additional information
?
-
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
-
-
-
additional information
?
-
-
tryparedoxin peroxidase activity. The enzyme does not follow a classic ping-pong mechanism
-
-
-
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
?
-
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
-
-
-
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
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
-
-
-
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
-
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 functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O08709
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O35244
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O77834
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
Q9TSX9
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
the enzyme is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
-
-
-
additional information
?
-
-
the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
-
-
-
additional information
?
-
-
Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
-
-
-
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
?
-
-
cumene hydroperoxide is not accepted as a substrate
-
-
-
additional information
?
-
-
insignificant affinity towards complex phospholipid hydroperoxide
-
-
-
additional information
?
-
-
PfTPx1 also possesses peroxynitrite reductase activity
-
-
-
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
?
-
Q06830
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
?
-
-
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
?
-
-
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
?
-
-
Prx I can be used as an indicator of microglial activation
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
B9USM4
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
-
-
-
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
?
-
B9USM4
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
-
-
-
additional information
?
-
Q9PER7
Cys83 is the resolving cysteine of XfPrxQ
-
-
-
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
?
-
O83522
TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
-
-
-
additional information
?
-
E8VQ78, E8VUX3
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
Q8GZT7
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
-
additional information
?
-
Q9SQJ4
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
-
additional information
?
-
Q9Z0V5
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
?
-
Q1AN22
enzyme reduces hydrogen peroxide and peroxynitrite with rate constants of 11000 and 2000 mM/s, respectively, at pH 7.4 and 25C. Reduction of tert-butyl hydroperoxide is slower
-
-
-
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
?
-
Thermus aquaticus YT-1
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
additional information
?
-
Saccharomyces cerevisiae YPH250
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
E8VQ78, E8VUX3
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
-
additional information
?
-
Burkholderia cenocepacia K56-2
-
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
?
-
-
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
?
-
Phanerochaete chrysosporium BKM-F-1767
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
-
glutathione is the primary native reductant
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
Burkholderia cenocepacia K56-2
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
B9USM4
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
Saccharomyces cerevisiae YPH250
-
-
-
-
?
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
Burkholderia cenocepacia K56-2
-
-
-
-
?
additional information
?
-
Q9GSV3, Q9N699
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
?
-
-
antioxidant activity may be the primary function of the enzyme
-
-
-
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
?
-
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
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 is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
-
additional information
?
-
Q5W9B5, Q5W9B6, Q5W9B7
the enzyme is important for protection against endogenously generated H2O2
-
-
-
additional information
?
-
Q9NL98
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
-
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
?
-
-
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 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
?
-
-
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
?
-
-
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
?
-
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
-
-
-
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
?
-
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
additional information
?
-
-
Pf1-Cys-Prx protects the parasite against oxidative stress by binding to ferriprotoporphyrin
-
-
-
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
-
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 functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O08709
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O35244
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
O77834
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
Q9TSX9
the enzyme functions in antioxidant defense and lung phospholipid metabolism
-
-
-
additional information
?
-
-
the enzyme is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
-
-
-
additional information
?
-
-
the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
-
-
-
additional information
?
-
-
Tpx-1 is required for normal gametocyte development but does not affect the male/female gametocyte ratio or male gametogenesis
-
-
-
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
?
-
-
peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream
-
-
-
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
?
-
-
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
?
-
-
Prx I can be used as an indicator of microglial activation
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
B9USM4
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
-
-
-
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
?
-
Thermus aquaticus YT-1
-
peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2
-
-
-
additional information
?
-
Saccharomyces cerevisiae YPH250
-
isozyme Gpx1 is an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally
-
-
-
additional information
?
-
Burkholderia cenocepacia K56-2
-
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
?
-
-
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
?
-
Phanerochaete chrysosporium BKM-F-1767
-
PcPrx-1 may play a protective role against oxidative stress
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
reaction is dependent on
thioredoxin
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
thioredoxin
-
-
thioredoxin
-
-
thioredoxin
P35704, Q9R063, Q9Z0V6
-
thioredoxin
Q9FUC5
-
thioredoxin
Q97WG5
-
thioredoxin
-
-
thioredoxin
-
;
thioredoxin
-
dependent
thioredoxin
A0ZXY5
-
thioredoxin
Q1AN22
-
thioredoxin
-
-
thioredoxin
B1N693, B1N694
;
thioredoxin
B6RB12
-
thioredoxin
A1KXR1
-
thioredoxin
-
-
thioredoxin
-
-
thioredoxin
B6V3F6
-
thioredoxin
Q21824, Q8IG31
;
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
Q9FUC5
inhibitory at 2 mM
AMP
Q9FUC5
inhibitory at 2 mM
ATP
Q9FUC5
3 mM ATP in concert with Mg2+, Ca2+, Mn2+, or Zn2+ lowers the peroxidase activity in a dose-dependent manner
Ca2+
Q9FUC5
92% inhibition at 2 mM, in the presence of 3 mM ATP
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
Q74887
high concentrations of H2O2 temporarily inactivate Tpx1
H2O2
-
excess of H2O2 inactivates the enzyme by overoxidation
H2O2
E8VQ78, E8VUX3
1 mM H2O2 overoxidizes isoform Prx2 at the peroxidatic cysteine and results in the loss of the peroxidase activity
H2O2
-
-
imidazole
A1KZ88
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
imidazole
A1KXU3
0.1 M, 50% inhibition
Mercaptosuccinate
-
a thiol-active agent that inhibits the peroxidase activity of Prdx6 while the PLA2 activity is unaffected
Mg2+
Q9FUC5
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+
MJ33
-
a phospholipid substrate intermediate analogue, inhibits the PLA2 activity of Prdx6 but has no effect on peroxidase activity
peptidoglycan
A8R072
downregulates Prx expression in lymphoid tissue and heart, but not in hemocytes
peroxynitrite
-
-
peroxynitrite
-
excess of peroxynitrite inactivates the enzyme by overoxidation
phosphate
Q9FUC5
inhibitory at 2 mM
SDS
A1KZ88
activity is lost completely in the presence of 1% SDS or higher
SDS
A1KXU3
1%, slight decrease in activity
tert-butyl hydroperoxide
-
substrate inhibition
Zn2+
Q9FUC5
65% inhibition at 2 mM, in the presence of 3 mM ATP
Mn2+
Q9FUC5
85% 92% inhibition at 2 mM, in the presence of 3 mM ATP
additional information
-
insensitive to hygromycin, paromomycin, and cycloheximide
-
additional information
-
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
-
additional information
P0A251
neither tert-butyl hydroperoxide nor cumene hydroperoxide demonstrate any observable inactivation of the enzyme, even when present at concentrations as high as 60 mM
-
additional information
B6RB12
during exposure to haemorrhagic septicaemia virus, HdPrxVI mRNA transcription is downregulated in the gill
-
additional information
-
serine protease inhibitors inhibit the PLA2 activity of Prdx6 but have no effect on peroxidase activity
-
additional information
O83522
TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates
-
additional information
E8VQ78, E8VUX3
isoform Prx1 is not overoxidized by H2O2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
A0ZXY5
stimulates enzyme expression
dithiothreitol
B1N693, B1N694
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
dithiothreitol
-
required for full activity
forkhead box transcription factor 3A
-
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
-
H2O2
P35704, Q9R063, Q9Z0V6
the total expression of Prx I is increased in response to H2O2; the total expression of Prx VI is increased in response to H2O2
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
lipopolysaccharide
B4XEM9
stimulates enzyme expression
Na+
A0ZXY5
Na+ at 25 mM stimulates expression of PrxII F
thiol
A8D0B7
dependent
lipoteichoic acid
B4XEM9
stimulates enzyme expression
-
additional information
-
Prx I expression is upregulated in microglia after lipopolysaccharide stimulation (0.001 mg/ml)
-
additional information
B1N693, B1N694
AbTPx1 gene expression is induced by oxidative stress; AbTPx2 gene expressions is induced by oxidative stress
-
additional information
A1KXR1
Prx1's ability to remove H2O2 is not supported by the presence of 1 mM GSH
-
additional information
-
oxidative stress does not regulate Prx5 expression
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.129
1-palmitoyl-2-arichidonoyl-sn-glycero-3-phosphocholine
-
-
0.12
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide
-
-
0.135
arachidonoyl hydroperoxide
-
-
0.00665
cumene hydroperoxide
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.00848
cumene hydroperoxide
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.0096
cumene hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
0.0127
cumene hydroperoxide
P91883
22C, pH 7.0
0.037
cumene hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
0.107
cumene hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.12
cumene hydroperoxide
-
-
0.152
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
0.191
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
0.0045
Ethyl hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.00038
H2O2
-
-
0.0007
H2O2
-
Km below 0.0007 mM, at 25C and pH 7.4
0.00078
H2O2
-
pH 7.6, 30C
0.00098
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
0.0011
H2O2
E8VQ78, E8VUX3
pH 7.0, 25C
0.0014
H2O2
-
pH 7.0, 25C, wild-type enzyme
0.0014
H2O2
P0AE08
wild type enzyme
0.0014
H2O2
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.0016
H2O2
-
pH 7.0, 25C, mutant enzyme T77V
0.002
H2O2
P0AE08
mutant enzyme P161S
0.0032
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
0.00475
H2O2
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.00856
H2O2
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.012
H2O2
O83522
pH 7.0, 25C, TpAhpC
0.0186
H2O2
A0ZXY5
wild type enzyme, in 25 mM Tris-HCl (pH 8)
0.02
H2O2
-
pH 7.0, reaction with thioredoxin
0.0276
H2O2
-
-
0.03
H2O2
P91883
22C, pH 7.0
0.0326
H2O2
E8VQ78, E8VUX3
pH 7.0, 25C
0.033
H2O2
Q9PER7
pH 7.4, 37C, recombinant enzyme
0.035
H2O2
-
pH 7.0, 37C
0.036
H2O2
Q5W9B5, Q5W9B6, Q5W9B7
pH 7.0, 37C
0.0425
H2O2
P0AE08
mutant enzyme P166L
0.062
H2O2
-
pH 7.0, 25C, mutant enzyme T77D
0.062
H2O2
O69777
-
0.072
H2O2
-
pH 7.0, 80C, wild-type enzyme
0.0934
H2O2
-
pH 7.0, 25C, mutant enzyme T77I
0.165
H2O2
-
in 7 mM phosphate buffer, pH 7.3, 150 mM NaCl, at 25C
0.17
H2O2
-
pH 7.0, reaction with GSH
0.18
H2O2
-
-
0.189
H2O2
P0AE08
mutant enzyme A167T
0.209
H2O2
-
pH 7.0, 80C, C207S mutant enzyme
0.711
H2O2
P0AE08
mutant enzyme S159P
16.28
H2O2
Q9U5A1
-
0.023
phosphatidylcholine hydroperoxide
-
pH 8.0, 30C
0.0024
reduced thioredoxin
-
human thioredoxin, at 25C
0.004
reduced thioredoxin
-
Escherichia coli thioredoxin, at 25C
0.0079
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
-
0.0087
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
-
0.003
S128W NTD
P0AE08
mutant enzyme S159P
0.0035
S128W NTD
P0AE08
mutant enzyme A167T; mutant enzyme P161S
0.0058
S128W NTD
P0AE08
wild type enzyme
0.0113
S128W NTD
P0AE08
mutant enzyme P166L
0.072
t-butyl hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
0.104
t-butyl hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
0.18
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
0.193
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
0.00004
tert-butyl hydroperoxide
-
-
0.0091
tert-butyl hydroperoxide
-
pH 7.6, 25C
0.0186
tert-butyl hydroperoxide
P91883
22C, pH 7.0
0.0625
tert-butyl hydroperoxide
-
pH 7.0, reaction with thioredoxin
0.13
tert-butyl hydroperoxide
-
in 7 mM phosphate buffer, pH 7.3, 150 mM NaCl, at 25C
0.142
tert-butyl hydroperoxide
-
-
0.238
tert-butyl hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.313
tert-butyl hydroperoxide
-
pH 7.0, reaction with GSH
0.001
thioredoxin
-
pH 7.0, 37C
0.0042
thioredoxin
-
-
0.012
thioredoxin
A9QKS0
pH 7.5, 25C, recombinant enzyme
0.0189
thioredoxin
-
pH 7.6, 30C
0.0388
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with cumene hydroperoxide
0.062
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with H2O2
0.0794
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with t-butyl hydroperoxide
0.0319
tryparedoxin 2
-
pH 7.6, 25C
-
0.141
linolenoyl hydroperoxide
-
-
additional information
additional information
-
the Km-value for H2O2 is below 0.02 mM
-
additional information
additional information
-
-
-
additional information
additional information
B9USM4
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
-
additional information
additional information
A9QKS0
SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.274
cumene hydroperoxide
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.281
cumene hydroperoxide
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.41
cumene hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
0.9
cumene hydroperoxide
-
-
6.3
cumene hydroperoxide
P91883
22C, pH 7.0
7.3
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
9.8
cumene hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
15.2
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
52
cumene hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
52.7
Ethyl hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.285
H2O2
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25C; PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25C
0.69
H2O2
-
-
0.83
H2O2
-
-
1
H2O2
-
pH 7.0, 25C, wild-type enzyme
1.1
H2O2
Q9PER7
pH 7.4, 37C, recombinant enzyme
1.4
H2O2
-
pH 7.0, reaction with GSH
1.67
H2O2
-
pH 7.6, 30C
10.6
H2O2
A0ZXY5
wild type enzyme, in 25 mM Tris-HCl (pH 8)
15.8
H2O2
P91883
22C, pH 7.0
17
H2O2
O83522
pH 7.0, 25C, TpAhpC
22.3
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
24.6
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
25
H2O2
-
pH 7.0, 25C, mutant enzyme T77I
31.5
H2O2
-
pH 7.0, 25C, mutant enzyme T77D
52.4
H2O2
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
55.1
H2O2
-
pH 7.0, 25C, wild-type enzyme
75.8
H2O2
-
pH 7.0, 25C, mutant enzyme T77V
99.4
H2O2
-
pH 7.0, reaction with GSH
957
H2O2
-
pH 7.0, reaction with thioredoxin
2.1
phosphatidylcholine hydroperoxide
-
-
0.098
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
-
2.9
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
-
33.8
S128W NTD
P0AE08
mutant enzyme A167T
44.5
S128W NTD
P0AE08
mutant enzyme S159P
52.2
S128W NTD
P0AE08
wild type enzyme
70.3
S128W NTD
P0AE08
mutant enzyme P161S
109
S128W NTD
P0AE08
mutant enzyme P166L
2
t-butyl hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
3.2
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
10.4
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
20.9
t-butyl hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
1.5
tert-butyl hydroperoxide
-
-
2.79
tert-butyl hydroperoxide
-
-
7.6
tert-butyl hydroperoxide
P91883
22C, pH 7.0
54.7
tert-butyl hydroperoxide
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
109
tert-butyl hydroperoxide
-
pH 7.0, reaction with GSH
368
tert-butyl hydroperoxide
-
pH 7.0, reaction with thioredoxin
9.65
thioredoxin
-
pH 7.6, 30C
9.8
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with cumene hydroperoxide
17
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with H2O2
20.9
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with t-butyl hydroperoxide
37
tryparedoxin 2
-
pH 7.6, 25C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.49
cumene hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
814
50
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
814
380
cumene hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
814
1000
cumene hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
814
33.5
H2O2
Q9PER7
pH 7.4, 37C, recombinant enzyme
22
88
H2O2
E8VQ78, E8VUX3
pH 7.0, 25C; pH 7.0, 25C
22
710
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
22
1400
H2O2
O83522
pH 7.0, 25C, TpAhpC
22
2500
H2O2
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
22
12
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
0
330
reduced thioredoxin A
E8VQ78, E8VUX3
pH 7.0, 25C
0
53.4
t-butyl hydroperoxide
Q9PER7
pH 7.4, 37C, recombinant enzyme
5218
160
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx197
5218
200
t-butyl hydroperoxide
O83522
pH 7.0, 25C, TpAhpC
5218
580
t-butyl hydroperoxide
B9USM4
pH 7.0, temperature not specified in the publication, Prx231
5218
250
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with cumene hydroperoxide
121
260
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with t-butyl hydroperoxide
121
270
thioredoxin
O83522
pH 7.0, 25C, TpAhpC with H2O2
121
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.294
H2O2
-
MPX, at 28C
0.3
H2O2
-
CPX, at 28C
0.4
peroxynitrite
-
MPX, at 28C
0.48
peroxynitrite
-
CPX, at 28C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
-
mutant enzyme C83S/R128E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C; mutant enzyme C83S/R128E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
0.04
-
mutant enzyme C83S/R128A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C; mutant enzyme C83S/R128A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C; mutant enzyme C83S/R128K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
0.08
-
mutant enzyme C83S/R128K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
0.1
-
mutant enzyme C83S/R151A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C; mutant enzyme C83S/R151E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
0.12
-
mutant enzyme C83S/R151A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C; mutant enzyme C83S/R151K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
0.18
-
mutant enzyme C83S/R151E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
0.19
-
mutant enzyme C83S/R151K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
0.28
-
mutant enzyme H26A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
0.67
Q9PER7
pH 7.4, 37C, recombinant enzyme, substarte t-butyl hydroperoxide
0.9
-
wild type enzyme, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
1
-
mutant enzyme C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
1.07
-
mutant enzyme C83S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
1.49
Q9PER7
pH 7.4, 37C, recombinant enzyme, substrate cumene hydroperoxide
1.76
Q9PER7
pH 7.4, 37C, recombinant enzyme, substrate H2O2
1.95
-
mutant enzyme C83S/C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25C
2.32
-
mutant enzyme C83S, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
2.74
-
wild type enzyme, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25C
5.25
-
mutant enzyme D140A, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
5.6
-
mutant enzyme H26A, using H2O2 as substrate, at pH 7.4
5.72
-
mutant enzyme S32A, using H2O2 as substrate, at pH 7.4
6
-
wild type enzyme, using 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate, at pH 7.4
6.15
-
mutant enzyme D140A, using H2O2 as substrate, at pH 7.4
6.2
-
wild type enzyme, using H2O2 as substrate, at pH 7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
A9QKS0
-
7
-
assay at, with glutathione or thioredoxin and peroxides
7
C3VVL4, C3VVL6
assay at; assay at
7
O83522
assay at
7
-
assay at
7
-
assay at
7.2
-
assay at, with glutathione and H2O2
7.4
Q9PER7
assay at
8
B1N693, B1N694
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
B1N693, B1N694
;
5.4 - 9
A1KZ88
no activity at or below pH 5.4, optimal activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
25
A9QKS0
assay at
25
O83522
assay at
25
-
assay at
37
-
around 37C
37
B1N693, B1N694
;
37
Q9PER7
assay at
80
-
assay at
85
Q97WG5
; Bcp1 and Bcp3
95 - 100
Q97WG5
; Bcp4
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
-
the enzyme retains no less than 50% of activity over a temperature range of 10-50C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
calculation from nucleotide sequence
4.9
E8VQ78, E8VUX3
calculated
5.18
A8R072
isoelectric focusing
5.3
O69777
calculated from sequence
5.3
A8D0B7
isoelectric focusing
5.34
P35704, Q9R063, Q9Z0V6
isoelectric focusing
5.6
A8R072
calculated
5.64
P35704, Q9R063, Q9Z0V6
isoelectric focusing
5.7
B1N693, B1N694
calculated from amino acid sequence
5.9
A1KXU3
calculated from sequence
5.92
A0ZXY5
estimated from amino acid sequence
6
Q9NL98
calculation from nucleotide sequence
6
B1N693, B1N694
calculated from amino acid sequence
6.18
P35704, Q9R063, Q9Z0V6
isoelectric focusing
6.2
C5H3W2
calculated from amino acid sequence
6.4
-
calculated from sequence
6.85
-
calculated from sequence
7.14
P35704, Q9R063, Q9Z0V6
isoelectric focusing
7.3
B6RB12
calculated from amino acid sequence
7.65
Q97WG5
Bcp4, calculated from amino acid sequence
7.73
Q97WG5
Bcp1, calculated from amino acid sequence
8.2
B3SP74
calculated from amino acid sequence; estimated from amino acid sequence
8.27
P35704, Q9R063, Q9Z0V6
isoelectric focusing
8.84
Q97WG5
Bcp3, calculated from amino acid sequence
8.9
-
calculated from sequence
8.94
P35704, Q9R063, Q9Z0V6
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
0.003 mg Prx I per mg of soluble protein Prx I, 0.0027 mg Prx II per mg of soluble protein, 0.001 mg Prx III per mg of soluble protein, 0.00003 mg Prx V per mg of soluble protein and 0.0002 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
O69777
the enzyme is strongly expressed under microaerobic conditions and during the sambiotic interaction with Phaseolus vulgaris
Manually annotated by BRENDA team
-
expressed at high levels during the haem-digesting stage
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
PRDX I is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body, PRDX II is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body, PRDX III is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body
Manually annotated by BRENDA team
-
tegumentary and muscle cells
Manually annotated by BRENDA team
-
ciliary body
Manually annotated by BRENDA team
-
cardiac fibroblast
Manually annotated by BRENDA team
-
containing green sepals
Manually annotated by BRENDA team
C5H3W2
the expression of Prx6 in gill is 4.9fold of that in haemocytes
Manually annotated by BRENDA team
A8R072
upregulation after anti-white spot syndrome virus challenge
Manually annotated by BRENDA team
C5H3W2
trace transcript is detectable in the gonad
Manually annotated by BRENDA team
A8R072
upregulation after anti-white spot syndrome virus challenge
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
C5H3W2
the Prx6 expression in heart is slightly lower than in haemocytes
Manually annotated by BRENDA team
-
more than 0.004 mg Prx I per mg of soluble protein Prx I, 0.0033 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and above 0.003 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
B3SP74
stimulation of Listonella anguillarum significantly enhances the mRNA expression of PRX in hemocytes
Manually annotated by BRENDA team
C5H3W2
temporal expression in hemocytes of crabs challenged with Listonella anguillarum
Manually annotated by BRENDA team
A8R072
upregulation after anti-white spot syndrome virus challenge
Manually annotated by BRENDA team
-
0.0033 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, 0.0005 mg Prx V per mg of soluble protein and 0.0017 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
C5H3W2
highest expression level in hepatopancreas which is 17.4 fold of that in haemocytes
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
0.0027 mg Prx I per mg of soluble protein Prx I, 0.001 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0001 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
0.0033 mg Prx I per mg of soluble protein Prx I, 0.002 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and more than 0.005 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q9U5A1
lateral hypodermal chords of both male and female worms
Manually annotated by BRENDA team
Q9SQJ4
the gene is predominantly expressed in leaf tissue of seedlings
Manually annotated by BRENDA team
-
about equal acttivity in young and mature leaves. The amount of Prx Q is decreased in senescent leaves
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
especially in type II alveolar epithelial cells and bronchiolar Clara cells
Manually annotated by BRENDA team
-
immunohistochemical reactivity for Prx I is detected rarely in microglia, whereas strong and specific immunoreactivity for Prx I is observed exclusively in microglia of primary neural cell culture
Manually annotated by BRENDA team
Q9U5A1
afibrillar muscle cells in male worms
Manually annotated by BRENDA team
C5H3W2
the expression of Prx6 in muscle is 5.3fold of that in haemocytes
Manually annotated by BRENDA team
-
of cysticercus
Manually annotated by BRENDA team
-
immunohistochemical reactivity for Prx I is detected dominantly in oligodendrocytes
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
transcript liver rapidly decreases after imbibition of seeds, but the protein is detected for 15 days after imbibition
Manually annotated by BRENDA team
-
isoform Per1a is expressed in developing seeds and transiently in germinating seeds. Per1 protein is synthesized in developing seeds, and was degraded during germination and growth. In addition, two forms of GmPer1 protein exist in both submerged and normally grown seedlings, and the amount of both forms is higher in the submerged seedlings
Manually annotated by BRENDA team
Q9SQJ4
transcript is not detected in the seeds, but its expression level increases at germination and is maintained thereafter
Manually annotated by BRENDA team
Q8GZT7
transcript level is abundant at the seed stage, but rapidly decreases after imbibitions
Manually annotated by BRENDA team
Q9XF72
transcript level is low at the seed stage, rapidly increases for 10 days after imbibitions, and gradually disappears thereafter
Manually annotated by BRENDA team
-
expressed in the postacrosomal sheath region
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
B6V3F6
stomach lining
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
B4XEM9
cervical thymus
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q5W9B5, Q5W9B6, Q5W9B7
-
Manually annotated by BRENDA team
-
0.0027 mg Prx I per mg of soluble protein Prx I, 0.0005 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0013 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
Q9U5A1
uterine wall in female worms
Manually annotated by BRENDA team
additional information
-
no activity in root
Manually annotated by BRENDA team
additional information
Q9SQJ4
the mRNA is generally expressed in most tissues of mature plant, except root
Manually annotated by BRENDA team
additional information
-
no activity is detected in muscles, coelomic fluid, and other internal structures
Manually annotated by BRENDA team
additional information
B6RB12
PrxVI mRNA is constitutively expressed in all tissues in a tissue-specific manner
Manually annotated by BRENDA team
additional information
B4Y9T5
TPx is also detected in bile fluid and bile duct epithelial cells surrounding the flukes 2 weeks after infection of hamsters with Opisthorchis viverrini
Manually annotated by BRENDA team
additional information
-
not in the hemolymph
Manually annotated by BRENDA team
additional information
-
within organs, expression of Prdx is greatest in epithelium such as apical regions of respiratory epithelium and skin epidermis, tissue distribution, overview
Manually annotated by BRENDA team
additional information
E8VQ78, E8VUX3
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
Manually annotated by BRENDA team
additional information
-
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
peroxiredoxin Q represents about 0.3% of chloroplast proteins. It attaches to the thylakoid membrane and is detected in preparations enriched in photosystem II complexes
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia
-
-
-
Manually annotated by BRENDA team
Q5W9B5, Q5W9B6, Q5W9B7
-
Manually annotated by BRENDA team
-
Prx1, Prx5 resides in the cytoplasm of peroxiredoxin 1-negative MEF cells
Manually annotated by BRENDA team
-
Prx I and Prx II
Manually annotated by BRENDA team
-
the enzyme is mostly cytosolic
Manually annotated by BRENDA team
-
treatment of A-549 cells with peroxides leads to translocation of Prdx6 from the cytosol to the cell membrane
Manually annotated by BRENDA team
-
cytosolic Prdx6 could bind to and reduce peroxidized membrane phospholipids followed by its dissociation from the membrane and return to the cytosolic compartment
Manually annotated by BRENDA team
-
associated with erythrocyte membrane
Manually annotated by BRENDA team
-
0.05% of cellular Prx2 is bound to the membrane
Manually annotated by BRENDA team
-
treatment of A-549 cells with peroxides leads to translocation of Prdx6 from the cytosol to the cell membrane
Manually annotated by BRENDA team
-
after spermiation, PRDX2 localization becomes confined to the mitochondrial sheath of the sperm tail midpiece
Manually annotated by BRENDA team
-
localized to the mitochondrial matrix
Manually annotated by BRENDA team
Q5W9B5, Q5W9B6, Q5W9B7
-
Manually annotated by BRENDA team
-
Prx5 is primarily nuclear
Manually annotated by BRENDA team
-
when expressed in Escherichia coli
-
Manually annotated by BRENDA team
-
reversible binding of the oligomeric form of the enzyme to the thylakoid membrane
Manually annotated by BRENDA team
-
residual body
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain J99 / ATCC 700824)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
Xylella fastidiosa (strain 9a5c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16980
Q97WG5
Bcp3, calculated from amino acid sequence
686695
17400
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
17460
Q97WG5
Bcp1, calculated from amino acid sequence; Bcp4, calculated from amino acid sequence
686695
18000
Q97WG5
Bcp1, SDS-PAGE
686695
18040
Q97WG5
Bcp3, MALDI-TOF mass spectrometry
686695
18530
Q97WG5
Bcp1, MALDI-TOF mass spectrometry; Bcp4, MALDI-TOF mass spectrometry
686695
18570
A0ZXY5
estimated from amino acid sequence
689642
18750
A0ZXY5
mature enzyme, gel filtration
689642
19320
-
electrospray ionization mass spectrometry
696360
20000
-
SDS-PAGE
696569
20000
Q21824, Q8IG31
reduced PRDX-2, SDS-PAGE; reduced PRDX-3, SDS-PAGE
700970
20100
B3SP74
calculated from amino acid sequence; estimated from amino acid sequence
700109
21800
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
21810
-
electrospray ionization mass spectrometry
687541
22000
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
23000
A1KXR1
Prx1 monomer, SDS-PAGE
698042
23000
B6V3F6
SDS-PAGE
700568
23400
B6V3F6
calculated from amino acid sequence
700568
23570
B4Y9T5
monomer, calculated from amino acid sequence
700080
24000
C5H3W2
calculated from amino acid sequence
698023
24000
B6RB12
estimated from amino acid sequence
698025
24400
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
25000
-
TgTrx-Px2 monomer, gel filtration
656291
25000
A8D0B7
calculated molecular mass
686216
26000
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
27000
-
SDS-PAGE
684998
28900
P35704, Q9R063, Q9Z0V6
SDS-PAGE
685356
30000
A8D0B7
recombinant enzyme, SDS-PAGE
686216
34000
-
gel filtration
655981
40000
A0ZXY5
SDS-PAGE
689642
43630
-
Prx2, Q-TOF mass spectrometry
687581
44000
-
dimer, SDS-PAGE
687764
47070
Q7RSE5
mass spectroscopy, oxidized dimer
724677
47460
-
mass spectroscopy, oxidized dimer
724677
49000
-
dimer, gel filtration
656408
50000
B4Y9T5
non-reducing and non-denaturing SDS-PAGE
700080
52000
-
TgTrx-Px2 dimer, gel filtration
656291
60000
-
SDS-PAGE
700171
64500
B1N693, B1N694
recombinant protein, SDS-PAGE
698018
70500
B1N693, B1N694
recombinant protein, SDS-PAGE
698018
150000
-
TgTrx-Px2 hexamer, gel filtration
656291
219700
-
Prx1, Q-TOF mass spectrometry
687581
230000
-
decamer, SDS-PAGE
687764
235000
-
gel filtration
655986
250000
-
TgTrx-Px1 decamer, gel filtration
656291
250000
A9QKS0
recombinant enzyme, peak 1, gel filtration
711785
260000
Q9FUC5
gel filtration
686691
388000
-
decamer, gel filtration
656408
400000
-
gel filtration
656749
400000
A9QKS0
recombinant enzyme, peak 2, gel filtration
711785
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 18000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
Q9U5A1
x * 26000, SDS-PAGE
?
A1KZ88
x * 25000, SDS-PAGE
?
Q9NL98
x * 21589, calculation from nucleotide sequence
?
Q9GSV3, Q9N699
x * 21800, 2-Cys peroxiredoxin, calculation from nucleotide sequence
?
-
x * 21913, calculation from nucleotide sequence
?
Q9GSV3, Q9N699
x * 24700, 1-Cys peroxiredoxin, calculation from nucleotide sequence
?
-
x * 25034, calculation from nucleotide sequence
?
-
x * 18000, calculated from sequence
?
O69777
x * 20080, calculated from sequence
?
-
x * 22100, calculated from sequence
?
-
x * 24745, calculated from sequence
?
A1KZ88
x * 25081, calculated from sequence
?
Q9PER7
x * 17813, sequence calculation
?
A9QKS0
x * 21800, SDS-PAGE and sequence calculation
?
C3VVL4, C3VVL6
x * 25000, BiTPx1, SDS-PAGE
?
-
x * 25100, about, sequence calculation, x * 26000-29000, SDS-PAGE
?
C3VVL4, C3VVL6
x * 27000, BiPrx1, SDS-PAGE
?
-
x * 18525, calculated from sequence
?
A8R072
x * 27500, calculated, x * 28000, SDS-PAGE
?
E8VQ78, E8VUX3
x * 22168, calculated
?
-
x * 31000, SDs-PAGe, x * 25900, calculated, His-tagged recombinant protein
?
-
x * 22168, calculated
-
?
-
x * 24745, calculated from sequence
-
?
Phanerochaete chrysosporium BKM-F-1767
-
x * 22100, calculated from sequence
-
decamer
-
10 * 24600, TgTrx-Px1, SDS-PAGE
decamer
-
10 * 27345, the enzyme exists as a homodecameric ring structure composed of five dimers, MALDI-TOF spectrometry
decamer
-
a stable decamer forms in vivo under conditions of oxidative stress
decamer
-
consisting of pentamers of homodimers that have a doughnut-like shape
decamer
Q9FUC5
10 * 26000, gel filtration
decamer
-
hyperoxidized form of Prx, X-ray crystallography
decamer
-
pentamer of dimers
decamer
-
Prx1, X-ray crystallography
decamer
P0AE08
wild type enzyme
decamer
-
the enzyme exists as a decamer in vivo, the reduced protein is also a decamer composed of the association of non-covalently linked dimers
dimer
A1KXU3
2 * 21000, SDS-PAGE
dimer
A0ZXY5
2 * 20000, SDS-PAGE
dimer
-
2 * 17000, SDS-PAGE
dimer
-
1 * 26500, TgTrx-Px2, SDS-PAGE
dimer
-
2 * 17030, calculation from nucleotide sequence
dimer
Q9SQJ4
2 * 22000, mutant enzyme DELTA66-273 migrates as a dimer under non-reducing SDS-PAGE
dimer
A1KXU3
2 * 20965, calculated from sequence
dimer
-
2 * 22000, the homodimeric oxidized enzyme form is reduced to a monomeric form by thioredoxin and by dithiothreitol and is converted to a homodimeric oxidized form by H2O2, SDS-PAGE
dimer
-
2 * 25650, the dimeric TgPrx2 is able to form tetramers and hexamers which are non-covalently associated, calculated from sequence
dimer
-
the crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution
dimer
-
2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms
dimer
Q97WG5
Bcp1, gel filtration, Bcp3, gel filtration
dimer
-
Bcp3, gel filtration
dimer
-
Prx2, X-ray crystallography
dimer
Q7RSE5
2 * 23534, mass spectroscopy, reduced monomer
dimer
-
2 * 23702, mass spectroscopy, reduced monomer
dimer
-
2 * 23702, mass spectroscopy, reduced monomer
-
hexadecamer
-
composed of two identical octamers, 2-fold toroid-shaped structure with outer and inner diameters of 14 and 6 nm, respectively. Although oligomerization of individual subunits does not take place through an intersubunit-disulfide linkage involving Cys50 and Cys213, Cys50 is essential for the formation of the hexadecamer
hexadecamer
Aeropyrum pernix DSM 11879
-
composed of two identical octamers, 2-fold toroid-shaped structure with outer and inner diameters of 14 and 6 nm, respectively. Although oligomerization of individual subunits does not take place through an intersubunit-disulfide linkage involving Cys50 and Cys213, Cys50 is essential for the formation of the hexadecamer
-
hexamer
-
1 * 26500, TgTrx-Px2, SDS-PAGE
hexamer
-
trimer of homodimers , X-ray crystallography
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
homodimer
-
-
homodimer
B4Y9T5
2 * 25000, SDS-PAGE
homodimer
-
2 * 50000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer
homodimer
-
mutant enzyme C45S, X-ray crystallography
monomer
Q9SQJ4
1 * 22000, mutant enzyme DELTA66-273 migrates as a monomer under reducing conditions
monomer
-
1 * 26500, TgTrx-Px2, SDS-PAGE
monomer
-
1 * 21805, electrospray ionization mass spectrometry
monomer
-
1 * 22000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer, 1 * 25000, SDS-PAGE, after reduction with 10 mM dithiothreitol the protein appears as a reduced monomer
multimer
-
x * 21000, SDS-PAGE
multimer
Thermus aquaticus YT-1
-
x * 21000, SDS-PAGE
-
oligomer
-
Prx IV oligomers contain two prevalent species with apparent molecular masses of 27 and 54 kDa corresponding to Prx IV monomers and disulfide-linked homodimers
monomer
Q97WG5
Bcp4, gel filtration
additional information
-
MW of open reading frame HI0572 determined by SDS-PAGE is 20000 Da
additional information
-
no dimeric form detectable
additional information
-
recombinant cPrx I produces in Escherichia coli forms differently sized high molecular weight protein structures. 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
-
the crystal structure shows that peroxiredoxin 5 does not form a dimer
additional information
-
the transition dimer-decamer produced in vitro between pH 7.5 and 8.0 suggests that a great change in the enzyme quarternary structure of the enzyme may take place in the chloroplast during the dark-light transition. The dimer-decamer equilibrium depends on NaCl concentration and concentration of dithiothreitol
additional information
-
Prx is a toroid-shaped pentamer of homodimers, or an (alpha2)5 decamer
additional information
-
the enzyme occurs in both dimeric and decameric forms when purified under non-reducing conditions
additional information
Q9PER7
primary structure and peptide mapping for detection of the disulfide-containing peptide, using chemical modification and tryptic digestion with HPLC-ESI-MS analyses, overview. Conformational analysis of XfPrxQ, modelling, overview
additional information
O83522
reduced TpAhpC forms stable octamers or decamers in solution whereas oxidation generates a heterogeneous mixture of oligomeric species. TpAhpC undergoes redox-sensitive oligomer formation
additional information
A9QKS0
the native SBT Prx enzyme exists as a mixture of dimers, tetramers, decamers and a higher order aggregate
additional information
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6
phosphoprotein
-
MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6
phosphoprotein
Q9FUC5
ATP facilitates the autophosphorylation of 2-Cys Prx when the protein is successively reduced with thiol-bearing compounds and oxidized with hydroperoxides or quinones
additional information
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.3 A resolution, microbatch method at 18C, using a crystallization robot, TERA
-
crystals of SeC207S are obtained by the hanging-drop vapor-diffusion method
-
in complex with H2O2, hanging drop vapour diffusion method, at 20C, using either acetate-containing or acetate-free reservoir conditions. The former consists of 0.1 M imidazole-HCl, pH 6.5, and 1 M sodium acetate, and the latter consists of 0.1 M HEPES-NaOH, pH 7.5, and 0.8 M potassium sodium tartrate
Q9Y9L0
oxidation by hydrogen peroxide converts the active site peroxidatic Cys-50 of ApTPx to a cysteine sulfenic acid derivative, followed by further oxidation to cysteine sulfinic and sulfonic acids. The crystal structure of the cysteine sulfenic acid derivative is refined to 1.77 A resolution
-
the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method using potassium sodium tartrate as the precipitant at 298 K. Diffraction data were collected and processed to 2.7 A resolution. The crystal belongs to space group P1, with unit-cell parameters a = 126.2, b = 126.3, c = 213.7 A, alpha = 80.4, beta = 80.3, gamma = 70.7
-
mutant C45S is crystallized by hanging drop vapour diffusion method, at 18C, in 0.1 M Bis-tris pH 5.5, 25% (w/v) PEG3350, 0.001 M dithiothreitol, and 0.02% (w/v) sodium azide
-
hanging-drop vapor-diffusion method, structure determined at 2.2 A resolution
-
1.5 A resolution crystal structure of peroxiredoxin 5 in the reduced form
-
crystal form of human peroxiredoxin 5 is described at 2.0 A resolution
-
hanging drop vapour diffusion method with 100 mM citrate (pH 4.6) and 10% polyethylene glycol; hanging drop vapour diffusion method with 100 mM citrate (pH 4.6) and 10% polyethylene glycol
-
structure of decameric 2-Cys peroxiredoxin at 1.7 A resolution
-
sulfredoxin in complex with PrxI, hanging-drop vapour diffusion method, in 20 mM HEPES pH 7.5 and 100 mM NaCl
-
the C72S mutant is crystallized by hanging drop vapour diffusion method with sodium cacodylate 0.1 M pH 6.5, PEG8000 20% (w/v), sodium acetate 0.1 M, and 6-aminocaproic acid 3% (w/v), at 18C
-
X-ray diffraction structure determination and analysis at 2.0 A resolution
-
hanging-drop vapour-diffusion technique, resolution of 2.8 A, the protein crystallizes in space group P1, with unit-cell parameters a = 61.88 A, b = 66.40 A, c = 77.23 A, alpha = 102.90, beta = 104.40, gamma = 99.07
-
hanging-drop vapor-diffusion method, 1.8 A resolution crystal structure
-
sitting-drop vapour diffusion
-
isoform PvTrx-Px1, in reduced and oxidized form, to 2.45 and 2.5 A resolution. The structures contain the typical thioredoxin-fold found in known peroxiredoxins. There is a central 7-stranded beta-sheet sandwiched by alpha1 and alpha4 on one side and alpha2, alpha3, and alpha5 on the other side. Isoform Trx-Px1 is a H2O2-sensitive peroxiredoxin
-
isoform Trx-Px1, in oxidized form, to 2.2 A resolution. The structure contains the typical thioredoxin-fold found in known peroxiredoxins. There is a central 7-stranded beta-sheet sandwiched by alpha1 and alpha4 on one side and alpha2, alpha3, and alpha5 on the other side. Isoform Trx-Px1 is a H2O2-sensitive peroxiredoxin
Q7RSE5
hanging drop method, wild-type enzyme and mutant enzymes T77V, T77I and T77D
-
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of 60 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 50 mM NaCl, 2 mM DTT, are mixed with 0.002 ml of 2 M ammonium sulfate, 0.1 M Na HEPES, pH 7.0, 2% v/v PEG 400, 25C, 2 days, X-ray diffraction structur determination and analysis at 2.3 A resolution
Q2FXL3
hanging-drop vapor-diffusion method, C45S/C50S double mutant crystallizes in the space group P2(1) with four molecules per asymmetric unit
-
hanging-drop vapor-diffusion method, crystal structure at 2.15 A, resolution of the C45S/C50S double mutant
-
sitting drop vapour diffusion method with 1.8 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 7.5% (v/v) ethylene glycol
-
purified recombinant PrxQ C47S, sitting drop vapor diffusion method, 5-15 mg/ml protein in 5 mM sodium citrate, pH 5.0, and 10 mM DTT, are mixed with reservoir solution containing 0.1 M HEPES-HCl, pH 7.5, and 20% PEG 8000 at 20C, X-ray diffraction structure determination and analysis
Q9PER7
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
AhpE is unstable and precipitates under low pH conditions (below pH 4.5)
696360
5 - 11
A1KXU3
37C, 30 min, stable
671558
5 - 11
A1KXR1
the enzyme is stable under a broad pH range from 5.0 to 11.0
698042
7.8 - 10.2
A1KZ88
37C, 30 min, stable
671545
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 90
B1N693, B1N694
H2O2 reduction activity increases from 30 to 37C and gradually decreases from 37 to 90C; H2O2 reduction activity increases from 30 to 37C and gradually decreases from 37 to 90C
698018
60
A1KZ88
half-life: 15.5 min
671545
60
A1KXU3
2 min, Prx retains 68% activity
671558
60
A1KXR1
the enzyme retains 60% activity at 60C for 2.5 min
698042
80 - 100
Q97WG5
Bcp1 shows no loss of activity after 2 h incubation at 80C, displays a half-life of 2 h at 95C but after a 60 min incubation at 100C its relative activity drops to 20% of the starting value; Bcp3 shows no loss of activity after 2 h incubation at 80C, after 2 h at 95C relative activity drops to 60%; Bcp4 shows no loss of activity after 2 h incubation at 80C, after 2 h at 95C relative activity drops to 92%
686695
80
-
6 h, the 63% of the activity is retained
673577
90
-
half-life: 3 h
673577
95
-
30 min, 70% loss of activity
673577
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 1 mM N-acetylcysteine to AhpE treated with equimolar H2O2 results in a destabilization of the dimer, leading to lower molecular weight species
-
PRX6 is resistant to inactivation via aldehyde modification
-
1.6 M imidazole seems to promote protein degradation
A1KZ88
sensitive to trypsin and chymotrypsin treatment. Very little or no activity detected after 40 min incubation with either protease
A1KZ88
susceptible to chymotrypsin treatment but resistant to digestion by trypsin. The enzyme retains approximately 65%, 50%, and 40% activity after treating with chymotrypsin for 1, 2, and 3 h, respectively
A1KXU3
the enzyme shows 57% activity after 40 min of incubation at 37C with trypsin, the enzyme shows 46% activity after 20 min of incubation at 37C with one-tenth its weight of chymotrypsin, the enzyme retains about 45% activity in 0.2 M imidazole
A1KXR1
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SDS
A1KXR1
the enzyme retains 40.5% activity in 2% (w/v) SDS
urea
Q97WG5
Bcp4 retains 50% of its activity after a 30 min incubation in 6 M urea
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation by hydrogen peroxide converts the active site peroxidatic Cys-50 of ApTPx to a cysteine sulfenic acid derivative, followed by further oxidation to cysteine sulfinic and sulfonic acids
-
728656
PRDX-2 is sensitive to hydrogen peroxide-induced oxidation, after treatment with 5.0 mM H2O2, reduced PRDX-2 is replaced with a hyperoxidized monomeric form and an additional peroxide-induced PRDX-2 disulfide
Q21824, Q8IG31
700970
Prx can become inactivated through the hyperoxidation of an active site Cys residue to Cys sulphinic acid
-
689157
the enzyme seems to be sensitive to oxygen but forms a thioredoxin-dependent system to eliminate reactive oxygen species in Pyrococcus horikoshii
O58966
722563
inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid is always preceded by a sulfinic acid form in a covalently linked dimer
Q74887
688901
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged 2-Cys Prx from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Q96291
Ni2+ column chromatography
-
glutathione-Sepharose column chromatography, gel filtration
-
Ni2+-NTA binding resin chromatography
A8D0B7
Ni2+-iminodiacetate-Sepharose column chromatography
Q9FUC5
recombinant His-tagged wild-type and mutant BCP homologues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
nickel-chelate affinity column chromatography
-
recombinant enzyme
P91883
recombinant protein
-
recombinant open reading frame HI0572
-
amylose resin column chromatography; amylose resin column chromatography
B1N693, B1N694
DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Superdex 200 gel filtration; DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Superdex 200 gel filtration
-
DEAE-Sepharose column chromatography, Superdex 75 gel filtration, and Superdex 200 gel filtration
-
HiPrep 16/10 DEAE column chromatography
-
phenyl-Sepharose column chromatography, S-Sepharose column chromatography, hydroxyapatite column chromatography, and G25 gel filtration
-
recombinant protein
-
TALON metal affinity resin column chromatography
B4Y9T5
recombinant
Q8S3L0
column chromatography and YMC-10 gel filtration
-
DE-52 column chromatography and 2',5'-ADP-Sepharose affinity column chromatography
-
with chitin beads
-
Ni-NTA His bind resin column chromatography, gel filtration
-
recombinant His6-tagged wild-type and mutant Gpx1 from Escherichia coli
-
nickel-chelate affinity column chromatography
-
GSH-Sepharose 4B bead chromatography
Q74887
recombinant enzyme versions PRX264, Prx231, and Prx197 from Escherichia coli strain BL21(DE3)
B9USM4
recombinant His-tagged enzyme from Escherichia coli by nickle affinity chromatography and gel filtration
Q2FXL3
HisTrap HP column chromatography, Resource S column chromatography, and Resource Q column chromatography; HisTrap HP column chromatography, Resource S column chromatography, and Resource Q column chromatography; HisTrap HP column chromatography, Resource S column chromatography, and Resource Q column chromatography
Q97WG5
Ni-NTA Sepharose column chromatography
A1KXR1
recombinant
A1KXU3
ammonium sulfate precipitation, ACA44 gel filtration, and DEAE Sephacel column chromatography
-
recombinant Prx 2 from Escherichia coli by nickel affinity chromatography and gel filtration
A9QKS0
Ni-NTA agarose column chromatography, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression of mutant enzyme C207S in Escherichia coli
-
expression of His-tagged 2-Cys Prx in Escherichia coli strain BL21(DE3)
Q96291
expressed in Escherichia coli
-
-
Q9NL98
expressed in Escherichia coli BL21 cells
-
gene BiPrx1, encoding a 1-Cys type Prx, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, determination of the transcriptional expression profile of BiPrx1, expression in Spodoptera frugiperda Sf9 cells using baculovirus transfection system; gene BiTPx1, encoding a 2-Cys type Prx, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, transcriptional expression profile of BiTPx1, expression in Spodoptera frugiperda Sf9 cells using baculovirus transfection system
C3VVL4, C3VVL6
expressed in Escherichia coli BL21 (DE3) cells
A8D0B7
DNA and amino acid sequence determination, analysis, and comparison
-
expressed in Escherichia coli JM109 cells
Q9FUC5
expression of N-terminally truncated enzyme in Escherichia coli, DELTA66-273
Q9SQJ4
gene bcp, the Burkholderia bcp gene shows unique linkage and coexpression with the arn locus, subcloning and expression as N-terminally His6-tagged proteins of wild-type and mutant BCP homologue in Escherichia coli strains DH5R and BL21(DE3)
-
expressed in Escherichia coli JM109 cells
B3SP74
expression in Escherichia coli as a polyhistidine fusion protein
Q9U5A1
expression in Escherichia coli
Q5W9B5, Q5W9B6, Q5W9B7
expressed in Escherichia coli Top10F' cells
C5H3W2
expressed in Escherichia coli
-
expression of open reading frame HI0572 in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells
B1N693, B1N694
expressed in Escherichia coli BL21(DE3) cells
B6RB12
expression in Escherichia coli
P21762
DNA and amino acid sequence determination, analysis, and comparison
-
expressed in Escherichia coli C41(DE3) cells
-
expressed in HT-1080 cells
-
expressed in LnCaP cells, LN3, C4-2, and C4-2B prostate cancer cells
-
expression in COS-7 cells
-
expression in Escherichia coli
-
expression in Escherichia coli or in NIH 3T3 cells
-
expression of Prx I, Prx II and Prx III in Escherichia coli
-
expression in Escherichia coli as an N-terminally His-tagged protein
-
expression of mature enzyme in Escherichia coli
A8R072
expressed in K-562 cells and CD34+ cells
-
Prdx6 gene, DNA and amino acid sequence determination and analysis, comprises 5 exons and 4 introns and is located on chromosome 1, mapped to a 0.66 cM interval between D1Mit 159 and D1Mit 398, sequence comparison
-
expressed in Escherichia coli BL21(DE3) cells
-
1. full-length protein with 345 amino acids, 2. a construction which stretches from the N-terminus to the end of the peroxiredoxin domain, contains 165 amino acids, 3. the grx module, that starts with MAQESVA and ends with the C-terminus of the fusion with 77 amino acids overall, expression in Escherichia coli
-
expressed as soluble protein in Escherichia coli
B4Y9T5
overexpression in Nicotiana tabacum cv. Xanthi-nc constitutively expressing the enzyme. Transgenic plants show a germination frequency similar to control plants. The transgenic lines exhibit higher resistance against oxidative stress
-
the recombinant PcPrx-1 protein is expressed as a histidine fusion protein in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells
A0ZXY5
expression using vector pET3d
-
the 171-amino-acid mature protein (estimated molecular weight 18600 Da) is cloned into the pET3d vector and overexpressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Q8S3L0
no post-translational modification occurs in Escherichia coli
-
expressed in Escherichia coli BL21 CodonPlus (DE3)-RIL cells
B6V3F6
expression in Escherichia coli
O58966
DNA and amino acid sequence determination, analysis, and comparison
-
expressed in Escherichia coli cells; expression in A-549 cells
-
expressed in Escherichia coli strain JM109
-
expression in COS cells and in Sf21 cells
-
expression in Escherichia coli
O69777
chitin-tagged protein is expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli
-
expression of His6-tagged wild-type and mutant Gpx1 in Escherichia coli, and of HA-tagged wild-type and mutant Gpx1 in yeast cells lacking gxp1, trx1, and trx2
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain FB810
Q74887
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)
B9USM4
expression of His-tagged enzyme in Escherichia coli
Q2FXL3
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
Q97WG5
expression in Escherichia coli
-
mutant enzymes are overproduced in soluble form as fusion with a C-terminal eight-residue histidine tag in Escherichia coli BL21
-
expression in Escherichia coli
-
coding region is subcloned into pAVD10, transformed into Escherichia coli, and expressed as a His-tagged fusion protein
A1KXU3
expressed in Escherichia coli C43(DE3) cells
A1KXR1
expression in Escherichia coli
A1KZ88
expressed in Escherichia coli BL21(DE3) cells
-
Prx 2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression in Escherichia coli
A9QKS0
expression in Escherichia coli strain BL21
-
TgTrx-Px1 and TgTrx-Px2, expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
gene prxq, expression of wild-type and mutant PrxQs in Escherichia coli strain BL21(DE3)
Q9PER7
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced as a cellular adaptation in response to the addition of exogenous H2O2
-
induced as a cellular adaptation in response to the addition of exogenous H2O2
Aeropyrum pernix DSM 11879
-
-
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
-
oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
expression is not induced by flooding treatment
-
oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
in Pyrococcus horikoshii cells the enzyme is induced by oxygen and hydrogen peroxide
O58966
transcription of Prdx6 message in dermal epithelium is induced by treatment with keratinocyte growth factor, a response of presumed importance related to wound healing, requiring ARE and Nrf2. Dexamethasone induces Prdx6 expression in adult lung cells and regulates transcription through its interaction with a glucocorticoid response element in the promoter region of the Prdx6 gene. Oxidant stress is, e.g. by H2O2, paraquat, a potent inducer of Prdx6 expression and stimulates Prdx6 gene expression by a transcriptional mechanism involving its antioxidant response element, ARE
-
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
E8VQ78, E8VUX3
isoform Prx2 is induced by trace amounts of H2O2 and thereby residential in cells grown aerobically
E8VQ78, E8VUX3
isoform Prx2 is induced by trace amounts of H2O2 and thereby residential in cells grown aerobically
-
-
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C207S
-
like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. Peroxidase activity is less effective than the wild type activity
C207S
-
tertiary structure of a selenomethionine derivative of the C207S mutant enzyme
C207S
-
the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method
C207S/C213S
-
forms a toroid-shaped structure. The size and shapes of the top view are similar to those of the wild type. The octameric form of C207S/C213S mutant dissociates into monomer in the presence of 10 mM DTT. Peroxidase activity is similar to wilde type activity
C213S
-
like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. No peroxidase activity
C50S
-
no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity
C50S/C207S
-
no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity
C207S
Aeropyrum pernix DSM 11879
-
tertiary structure of a selenomethionine derivative of the C207S mutant enzyme
-
C207S
Aeropyrum pernix DSM 11879
-
the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method, like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. Peroxidase activity is less effective than the wild type activity
-
C213S
Aeropyrum pernix DSM 11879
-
like the wild-type enzyme the mutant enzyme exists as a hexadecamer, DTT treatment has no effect on their quaternary structure. No peroxidase activity
-
C50S
Aeropyrum pernix DSM 11879
-
no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity
-
C183S
-
strongly reduced activity
C45S
-
inactive
C45S
-
dimeric mutant
C53S
Q9FUC5
autophosphorylation of C53S 2-Cys Prx does not require successive incubation with dithiothreitol and the hydroperoxide but is extremely sensitive to the addition of dithiothreitol
W179F
Q9FUC5
neither the basal nor the ATP-inhibited peroxidase activities are appreciably different from wild type 2-Cys Prx
Y166F
Q9FUC5
autophosphorylation is similar to wild-type 2-Cys Prx
DELTA66-273
Q9SQJ4
the mutant enzyme prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the DELTAC2C-Prx exhibits peroxidase activity on H2O2
L49C
-
site-directed mutagenesis, introduction of a resolving cysteine into BcBCP changes the activity from a 1-Cys pathway to an atypical 2-Cys pathway, analogous to the Escherichia coli enzyme, substrate specificity, overview. Recombinant knockout strain XOA14 is created by insertional inactivation of the strain K56-2 bcp homologue
L49C
Burkholderia cenocepacia K56-2
-
site-directed mutagenesis, introduction of a resolving cysteine into BcBCP changes the activity from a 1-Cys pathway to an atypical 2-Cys pathway, analogous to the Escherichia coli enzyme, substrate specificity, overview. Recombinant knockout strain XOA14 is created by insertional inactivation of the strain K56-2 bcp homologue
-
A167T
P0AE08
49% activity compared to the wild type enzyme
C165S
P0AE08
inactive
P161S
P0AE08
97% activity compared to the wild type enzyme
P166L
P0AE08
94% activity compared to the wild type enzyme
S159P
P0AE08
32% activity compared to the wild type enzyme
C151S
-
the mutation of the resolving cysteine residue does not affect peroxidatic cysteine residue reactivity
C152S
-
mutant enzyme shows no detectable thioredoxin-dependent peroxidase activity
C47S
-
mutation abolishes peroxidase activity,mutation has no effect on lipase activity
C48S
-
mutant enzyme shows no detectable thioredoxin-dependent peroxidase activity
C52S
-
mutant lacks antioxidant activity
C52S/C173S
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
C72S
-
the C72S mutation improves the crystallization in oxidizing conditions
C73S
-
mutation has no effect on activity
C83S
-
increased activity compared to wild type Prx1
C83S
-
residue Cys83 is not essential for the formation of high molecular weight complexes, it affects the dimer/decamer equilibrium. Glutathionylation of the C83S mutant leads to accumulation of dimers and monomers
C91S
-
mutation has no effect on lipase activity
S32A
-
mutation has no effect on lipase activity
S32G
-
mutation has no effect on lipase activity
C60S
-
inactive mutant enzyme
C80S
-
mutant is indistinguishable from the wild-type enzyme
C93S
-
the mutant is fully active as a thioredoxin-dependent peroxidase and remains active despite exposure to peroxynitrite, pronounced instability of the mutant enzyme under oxidizing conditions
C185S
-
inactive mutant enzyme
C48S
A0ZXY5
12% activity compared to the wild type enzyme
C59S
A0ZXY5
inactive
C170A
-
kcat/Km of mutant enzyme is reduced for thioredoxin as a substrate approximately 50fold. In contrast to the wildtype enzyme, covalently linked dimers are not formed
R129Q
-
inactive with H2O2 or tert-butyl hydroperoxide, catalyzes degradation of cumene hydroperoxide with low efficiency
T48V
-
inactive with H2O2 or tert-butyl hydroperoxide, catalyzes degradation of cumene hydroperoxide with low efficiency
C126S
Q9Z0V5
very weak activity both with substrate H2O2 and t-butyl hydroperoxide
C150S
Q9Z0V5
activity similar to wild-type
C173S
-
decameric mutant enzyme, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions
C247S
Q9Z0V5
weak activity both with substrate H2O2 and t-butyl hydroperoxide
C47S
-
inactive
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
D140A
-
mutant shows decreased peroxidase activity
H26A
-
mutant shows decreased peroxidase activity
S32A
-
mutant shows decreased peroxidase activity with H2O2 and no activity with 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide as substrate
C156S
O69777
no peroxidase activity
C56S
O69777
no peroxidase activity
C81S
O69777
although the PrxS C81S mutant protein can be overexpressed and purified under denaturing conditions, it is not possible to obtain any active C81S PrxS. the C81S mutant is prone to inclusion body formation
C80S
-
reduced activity
C102S
-
activity is similar to the wild type enzyme
C48S
-
reduced activity
C48S/C102S
-
reduced activity
C144S
-
site-directed mutagenesis, the pattern of reduced/oxidized protein of Gpx1C144S is similar to that of Gpx1 wild-type
C152S
-
site-directed mutagenesis, the pattern of reduced/oxidized protein of Gpx1C152S is similar to that of Gpx1 wild-type
C36S
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C36S protein even in the presence of t-butylhydroperoxide
C47S
-
the Cys47 residue of Tsa1 is not required for chaperone activity but is essential for peroxidase activity
C82S
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C82S protein, but merges following the treatment of the cells with t-butylhydroperoxide
C98S
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C98S protein, but merges following the treatment of the cells with t-butylhydroperoxide
S64S
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C64S protein, but merges following the treatment of the cells with t-butylhydroperoxide
C152S
Saccharomyces cerevisiae YPH250
-
site-directed mutagenesis, the pattern of reduced/oxidized protein of Gpx1C152S is similar to that of Gpx1 wild-type
-
C36S
Saccharomyces cerevisiae YPH250
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C36S protein even in the presence of t-butylhydroperoxide
-
C82S
Saccharomyces cerevisiae YPH250
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C82S protein, but merges following the treatment of the cells with t-butylhydroperoxide
-
C98S
Saccharomyces cerevisiae YPH250
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C98S protein, but merges following the treatment of the cells with t-butylhydroperoxide
-
S64S
Saccharomyces cerevisiae YPH250
-
site-directed mutagenesis, in contrast to Gpx1 wild-type, no oxidized Gpx1 appears in cells carrying the Gpx1C64S protein, but merges following the treatment of the cells with t-butylhydroperoxide
-
T77D
-
mutation disrupts the decamer stability, mutant enzyme exhibits ca. 100fold lower catalytic efficiency than wild-type enzyme
T77I
-
mutation disrupts the decamer stability, mutant enzyme exhibits ca. 100fold lower catalytic efficiency than wild-type enzyme
T77V
-
mutation enhances the decamer stability, mutant enzyme has slightly higher activity than wild-type enzyme
C169S
Q74887
decreased activity
C45S
-
mutation in cysteine 45 results in complete loss of DTT-dependent peroxidase activity
C45S
-
inactive in assay with H2O2 and reduced dithiothreitol
C50S
-
the C50S mutant enzyme retains almost all the activity of the wild-type enzyme (DTT-dependent peroxidase activity). Unlike the wild-type enzyme, the mutant enzyme is able to form in vitro a homodimer via an intermolecular disulfide bond
C50S
-
still active in assay with H2O2 and reduced dithiothreitol. Mutant enzyme occurs in a dimeric and a tetrameric form
C45S
-
inactive in assay with H2O2 and reduced dithiothreitol
-
C50S
-
still active in assay with H2O2 and reduced dithiothreitol. Mutant enzyme occurs in a dimeric and a tetrameric form
-
C52A
-
parasites expressing CPX C52A fail to confer peroxynitrite resistance
C81A
-
parasites expressing MPX C81A fail to confer peroxynitrite resistance
C171S
-
complete loss of activity
C50S
-
complete loss of activity
C171S
-
complete loss of activity
-
C50S
-
complete loss of activity
-
C101S
Q9PER7
site-directed mutagenesis, structure comparison to the wild-type enzyme
C23S
Q9PER7
site-directed mutagenesis, structure comparison to the wild-type enzyme
C47S
Q9PER7
site-directed mutagenesis, structure comparison to the wild-type enzyme
C83S
Q9PER7
site-directed mutagenesis, structure comparison to the wild-type enzyme, dimedone likely inactivated the XfPrxQ C83S protein because sulfenic acids persist long enough to react with dimedone only in the absence of Cys83
C50S/C213S
-
mutant enzyme only exists in the monomeric form. No peroxidase activity
additional information
-
mutagenesis studies suggest that the sulfhydryl group of Cys50 is the site of oxidation by peroxide and that oxidized Cys50 reacts with the sulfhydryl group of Cys213 of another subunit to form an intermolecular disulfide bond. Mutants lacking either Cys50 or Cys213 show no thioredoxin peroxidase activity, whereas the mutant lacking Cys207 has a thioredoxin peroxidase activity
C50S/C207S
Aeropyrum pernix DSM 11879
-
no toroid shaped particles are observed, DTT treatment has no effect on their quaternary structure. No peroxidase activity
-
additional information
Aeropyrum pernix DSM 11879
-
mutagenesis studies suggest that the sulfhydryl group of Cys50 is the site of oxidation by peroxide and that oxidized Cys50 reacts with the sulfhydryl group of Cys213 of another subunit to form an intermolecular disulfide bond. Mutants lacking either Cys50 or Cys213 show no thioredoxin peroxidase activity, whereas the mutant lacking Cys207 has a thioredoxin peroxidase activity
-
additional information
Q96291
construction of a 2-Cys-Prx knockout mutant, phenotype, overview
additional information
Arabidopsis thaliana Columbia
-
construction of a 2-Cys-Prx knockout mutant, phenotype, overview
-
C86S
Q1AN22
rate constant of H2O2 reduction is similar to wild-type
additional information
-
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
C46S
P0AE08
decreased activity
additional information
P0AE08
AhpC can be converted through a single amino acid insertion to a disulfide reductase, AhpC*, active in the glutathione and glutaredoxin pathway
additional information
-
an engineered BCP, lacking the resolving cysteine, retains enzyme activity through a different catalytic pathway compared to the wild-type enzyme
C48S
Q74887
completely inactive
additional information
B9USM4
construction of shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
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
medicine
-
Prx plays a crucial role against oxidative stress in vascular smooth muscles during hypertension
medicine
P35704, Q9R063, Q9Z0V6
Prxs play a crucial role against oxidative stress in vascular smooth muscles during hypertension