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Information on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin
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1.11.1.24 thioredoxin-dependent peroxiredoxinIUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
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Word Map
- 1.11.1.24
- catalase
- dismutase
- peroxidases
- s-transferase
- chloroplast
-
peroxidatic
-
hyperoxidation
- gsh
-
anti-oxidant
- glutaredoxins
-
detoxify
-
annexin
- ascorbate
-
thiol-dependent
-
neuroprotective
- leishmania
- cumene
-
sulfenic
-
redox-sensitive
- trx1
-
tert-butyl
-
redox-active
-
h2o2-induced
-
decameric
- mnsod
- trypanothione
-
t-butyl
-
nitrosative
- paraquat
-
glutathionylation
-
h2o2-mediated
- sod2
-
redox-dependent
- cyclophilin
-
2d-dige
- hepatica
- selenocysteine
-
thioredoxin-like
-
peroxide-mediated
-
peroxide-induced
-
peroxidase-like
-
redox-regulated
- ask1
- catalase-peroxidase
- auranofin
- fasciola
-
thiol-based
-
excretory-secretory
-
metal-catalyzed
- thioredoxin-1
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
peroxiredoxin, prdx2, prx i, peroxiredoxin 1, prx ii, peroxiredoxin 2, prdx5, alkyl hydroperoxide reductase, thioredoxin peroxidase, 2-cys prx, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-Cys peroxiredoxin
2-Cys peroxiredoxin
2-Cys Prx
Ahp
-
peroxiredoxin activity is located within the carboxyl-terminal AhpC/thiol-specific antioxidant domain (Ahp) of Rhodospirillum rubrum adenylyltransferase GlnE
AhpC
alkyl hydroperoxide reductase
alkyl hydroperoxide reductase C component
-
APE2278
ApTPx
atypical two-cysteine peroxidase
bacterioferritin comigratory protein
BCP
Bcp4
EC 1.11.1.15
-
-
formerly, part transferred
-
EcTpx
-
an atypical 2Cys Tpx with an intramolecular disulfide bond formed between the peroxidatic Cys61 and the resolving Cys95 residue
GPX
heme-binding protein 23/peroxiredoxin
belongs to the 2-Cys peroxiredoxin type I family and exhibits peroxidase activity coupled with reduced thioredoxin as an electron donor
ncgl2403
peroxiredoxin
peroxiredoxin 2
peroxiredoxin 5
peroxiredoxin 6
peroxiredoxin IV
PH1217
PRDX III
PRDX2
Prdx6
Prx
Prx I
Prx II
PRx IV
Prx V
Prx VI
Prx1
Prx2
PrxQ
SAOUHSC_01822
SSO2613
tgTPx1/2
thioredoxin peroxidase
thioredoxin peroxidase 1/2
thioredoxin peroxidase 2
thioredoxin-dependent alkyl hydroperoxide reductase
thioredoxin-dependent peroxiredoxin Q
TM0807
Tpx
TPx I
TPx-1
TPx1
TPx1/2
TPX2
TRIREDRAFT_47136
tryparedoxin peroxidase
Tsa1
-
has dual activities as a peroxidase and as a molecular chaperone, Tsa1 functions predominantly as an antioxidant in protecting both the cytosol and actively translating ribosomes against endogenous reactive oxygen species, but shifts towards its chaperone function in response to oxidative stress conditions
TsaA
TXNPx
typical 2-Cys Prx
additional information
BCP
-
-
-
-
peroxiredoxin 2
-
previously known as torin, calpromotin, NKEF-B, HRPRP, band 8 or TPx-B
peroxiredoxin 5
classified in the atypical 2-Cys subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues
Prdx6
PRDX6 is a typical 2-Cys PRDX that functions more like a cytoprotective antioxidant enzyme or a modulator of peroxide-dependent cell signaling rather than a molecular chaperone
Prx
Prx from Penaeus japonicus belongs to the 2-Cys peroxiredoxin subgroup
Prx
-
belongs to the group of 1-Cys peroxiredoxins, Prx from Thermotoga maritima is part of a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus
Prx V
PRX V is an atypical 2-Cys PRX that can form intramolecular disulfide bridges through the N-terminal and C-terminal cysteines
PrxQ
-
-
-
-
thioredoxin peroxidase
-
-
-
-
Tpx
-
-
-
-
additional information
the enzyme belongs to the peroxiredoxin enzyme family
additional information
peroxiredoxin PrxQ belongs to the subdivision of the bacterioferritin comigratory protein family of bacterial peroxiredoxins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thioredoxin + ROOH = thioredoxin disulfide + H2O + ROH
-
-
-
-
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
the enzyme exhibits a saturable, single-displacement-like reaction mechanism rather than non-saturable double displacement (ping-pong) enzyme substitution mechanism
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
thioredoxin:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [4]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cumene hydroperoxide + reduced dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
low activity
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
cumene hydroperoxide + tryparedoxin 2
2-phenylpropan-2-ol + oxidized tryparedoxin 2
-
57% of the activity with H2O2
-
-
?
dithiothreitol + H2O2
H2O + oxidized dithiothreitol
-
-
-
?
ethyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
oxidized thioredoxin + H2O
highest activity
-
-
?
H2O2 + thioredoxin
?
1-Cys peroxiredoxin is less active than 2-Cys peroxiredoxin
-
-
?
iodoacetamide + reduced thioredoxin
?
-
Prx 3 reacts very slowly with iodoacetamide
-
-
?
linoleic acid hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
-
-
-
?
linoleic acid hydroperoxide + tryparedoxin 2
?
-
7.8% of the activity with H2O2
-
-
?
N-ethylmaleimide + reduced thioredoxin
?
-
Prx 3 reacts very slowly with N-ethylmaleimide
-
-
?
peroxynitrite + H2O2
nitrite + ?
-
CPX and MPX catalytically reduce peroxynitrite to nitrite through a fast-reacting thiol group located at the peroxidatic cysteine residue (Cys52 and Cys81 in CPX and MPX respectively), thus acting as tryparedoxin/peroxynitrite oxidoreductases
-
-
?
peroxynitrite + reduced thioredoxin
?
-
AhpE reduces peroxynitrite 2 orders of magnitude faster than H2O2
-
-
?
phosphatidyl choline hydroperoxide + tryparedoxin 2
?
-
3.8% of the activity with H2O2
-
-
?
tert-butyl hydroperoxide + tryparedoxin 2
tert-butanol + oxidized tryparedoxin 2
-
95% of the activity with H2O2
-
-
?
thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + cumene hydroxide
-
-
-
?
thioredoxin A + cumene hydroperoxide
thioredoxin A disulfide + H2O + cumene hydroxide
-
-
-
?
thioredoxin A + H2O2
thioredoxin A disulfide + 2 H2O
-
-
-
?
thioredoxin A + tert-butyl hydroperoxide
thioredoxin A disulfide + H2O + tert-butyl alcohol
-
-
-
?
thioredoxin B + H2O2
thioredoxin B disulfide + 2 H2O
-
-
-
?
thioredoxin C + H2O2
thioredoxin C disulfide + H2O
-
-
-
-
?
thioredoxin Q + H2O2
thioredoxin Q disulfide + 2 H2O
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
-
-
-
?
2 thioredoxin + tert-butyl hydroperoxide
thioredoxin disulfide + H2O + tert-butyl alcohol
-
-
-
?
2 thioredoxin + tert-butyl hydroperoxide
thioredoxin disulfide + H2O + tert-butyl alcohol
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
no activity with glutathione
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + NADPH + H+
2 H2O + 2 NADP+
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+
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
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
reduced Prx2 is exceptionally reactive withH2O2 and other peroxides but shows very low reactivity with other thiol oxidants and alkylating agents
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
Prx 3 displays strong reactivity with H2O2
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
thioredoxin from Escherichia coli and thioredoxin f and m from spinach
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
ping-pong kinetics
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
-
ping-pong mechanism
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
-
-
-
?
H2O2 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
low activity
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
9.5% of the activity with tert-butyl hydroperoxide and tryparedoxin 2
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
H2O2 is the preferred substrate compared to tert-butyl hydroperoxide
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
-
-
-
?
thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide
-
-
?
thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide
-
-
?
thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
-
the ability of AhpC in reducing hydrogen peroxide is depend on the thioredoxin/thioredoxin reductase system. Cys47 (a peroxidatic cysteine) and Cys167 (a resolving cysteine) were critical to maintaining the enzymatic activity of AhpC
-
-
?
thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
peroxiredoxin Cys51 and glutaredoxin Cys27 are involved in the catalytic mechanism. The enzyme also accepts glutaredoxin as electron donor
-
-
?
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
-
-
-
?
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
the enzyme defends against oxidative stress through decomposition of hydroperoxide
-
-
?
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
-
-
-
?
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
the enzyme defends against oxidative stress through decomposition of hydroperoxide
-
-
?
thioredoxin + tert-butyl hydroperoxide
thioredoxin disulfide + H2O + tert-butyl alcohol
the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide
-
-
?
thioredoxin + tert-butyl hydroperoxide
thioredoxin disulfide + H2O + tert-butyl alcohol
the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide
-
-
?
thioredoxin + tert-butyl hydroperoxide
thioredoxin disulfide + H2O + tert-butyl alcohol
-
-
-
?
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
?
-
-
insignificant affinity towards complex phospholipid hydroperoxide
-
-
?
additional information
?
-
enzyme reduces hydrogen peroxide and peroxynitrite with rate constants of 11000 and 2000 mM/s, respectively, at pH 7.4 and 25°C. Reduction of tert-butyl hydroperoxide is slower
-
-
?
additional information
?
-
-
enzyme reduces hydrogen peroxide and peroxynitrite with rate constants of 11000 and 2000 mM/s, respectively, at pH 7.4 and 25°C. Reduction of tert-butyl hydroperoxide is slower
-
-
?
additional information
?
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
?
additional information
?
-
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
?
additional information
?
-
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
?
additional information
?
-
enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone
-
-
?
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
?
additional information
?
-
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
?
additional information
?
-
-
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
?
additional information
?
-
-
the enzyme promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue
-
-
?
additional information
?
-
-
together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2
-
-
?
additional information
?
-
Prx1 shows a androgen receptor-stimulating function in response to hypoxia/reoxygenation
-
-
?
additional information
?
-
-
thioredoxin 2 directly associates with Prx3 in vivo and functions in protection against cell death
-
-
?
additional information
?
-
-
peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream
-
-
?
additional information
?
-
-
the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane
-
-
?
additional information
?
-
-
tryparedoxin peroxidase activity. The enzyme does not follow a classic ping-pong mechanism
-
-
?
additional information
?
-
-
the enzyme is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
?
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
?
additional information
?
-
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
-
-
?
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
?
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
?
additional information
?
-
-
after subjection to exogenous and endogenous oxidative stress, the Plasmodium falciparum blood stage form shows a marked elevation of PfTrx-Px1 mRNA and protein levels consistent with the structure of related proteins
-
-
?
additional information
?
-
-
the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
-
-
?
additional information
?
-
-
cumene hydroperoxide is not accepted as a substrate
-
-
?
additional information
?
-
-
PfTPx1 also possesses peroxynitrite reductase activity
-
-
?
additional information
?
-
enzyme is inactivated by hyperoxidation of the peroxidatic cysteine to a sulfinic acid in a catalytic cycle-dependent manner. The peroxidase activity of isoform Prx-4 is almost completely inhibited in the reaction with t-butyl hydroperoxide. When H2O2 is used as the substrate, the peroxidase activity significantly remains after oxidative damage. Both reactions result in the same oxidative damage, i.e. sulfinic acid formation at the peroxidatic cysteine
-
-
?
additional information
?
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
?
additional information
?
-
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
?
additional information
?
-
-
cPrx I and cPrx II function both as peroxidases and as molecular chaperones. The peroxidase function predominates in the lower molecular weight forms, whereas the chaperone function predominates in the higher molecular weight complexes. Oxidative stress and heat shock exposure of yeasts cause the protein structures of cPrxl and cPrx II to shift from low MW species to high molecular weight complexes. This triggers a peroxidase-to-chaperone functional switch
-
-
?
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
?
additional information
?
-
-
Tpx1 is an upstream activator of Pap1. At low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations
-
-
?
additional information
?
-
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
-
-
?
additional information
?
-
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
-
-
?
additional information
?
-
-
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
?
-
TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
-
-
?
additional information
?
-
-
TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
-
-
?
additional information
?
-
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
?
additional information
?
-
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
?
additional information
?
-
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
?
additional information
?
-
alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
-
-
?
additional information
?
-
Cys83 is the resolving cysteine of XfPrxQ
-
-
?
additional information
?
-
-
Cys83 is the resolving cysteine of XfPrxQ
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
the enzyme defends against oxidative stress through decomposition of hydroperoxide
-
-
?
thioredoxin + linoleic acid hydroperoxide
thioredoxin disulfide + H2O + linoleic acid
the enzyme defends against oxidative stress through decomposition of hydroperoxide
-
-
?
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 might function as a major antioxidant enzyme in Ascaris suum
-
-
?
additional information
?
-
-
the enzyme might function as a major antioxidant enzyme in Ascaris suum
-
-
?
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
?
additional information
?
-
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
?
additional information
?
-
-
the enzyme plays a critical role in defending the organism against oxygen toxicity
-
-
?
additional information
?
-
-
the enzyme promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue
-
-
?
additional information
?
-
-
together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism. In addition Prx I and II might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentration of H2O2
-
-
?
additional information
?
-
-
peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream
-
-
?
additional information
?
-
-
the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane
-
-
?
additional information
?
-
-
the enzyme is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress
-
-
?
additional information
?
-
-
Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK
-
-
?
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
?
additional information
?
-
1-Cys peroxiredoxin protects DNA from degradation by reactive O2 species in presence of low molecular mass thiols such as dithiothreitol and glutathione
-
-
?
additional information
?
-
-
after subjection to exogenous and endogenous oxidative stress, the Plasmodium falciparum blood stage form shows a marked elevation of PfTrx-Px1 mRNA and protein levels consistent with the structure of related proteins
-
-
?
additional information
?
-
-
the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species
-
-
?
additional information
?
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
?
additional information
?
-
-
constitutive expression of prxS confers enhanced survival and growth to Rhizobium etli in presence of H2O2. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys peroxiredoxin
-
-
?
additional information
?
-
-
peroxiredoxin induces the expression of Ym1 in macrophages and the development of Th2 immune responses, peroxiredoxin activates macrophages independently of interleukin-4 and interleukin-13
-
-
?
additional information
?
-
-
Tpx1 is an upstream activator of Pap1. At low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations
-
-
?
additional information
?
-
shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
-
-
?
additional information
?
-
-
peroxidases belonging to the class of 1-Cys and 2-Cys peroxiredoxins play crucial roles in maintaining redox balance. TgTrx-Px1 is an extremely potent antioxidant
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
thioredoxin m is more efficent than thioredoxin f in reducing the enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
benzoate
in orthorhombic 1 form, the benzoate ion is present close to the Cp residue in both fully folded subunits the benzoate ion is not observed in the six oxidized subunits in which the disulfide bond is formed
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
3 mM ATP in concert with Mg2+, Ca2+, Mn2+, or Zn2+ lowers the peroxidase activity in a dose-dependent manner
Mg2+
in the presence of 2 mM Mg2+, the rate of H2O2 removal is inhibited by 60%, 5% and 5% when it is assayed with 2 mM ADP, AMP or phosphate, respectively, total inactivation of 2-Cys Prx is caused by incubation with 3 mM ATP and 3 mM Mg2+
peptidoglycan
downregulates Prx expression in lymphoid tissue and heart, but not in hemocytes
praziquantel
Opisthorchis viverrini infection predisposes the infected for cholangiocarcinoma, a cancer of the gall bladder and its ducts. Praziquantel is the drug most commonly used to cure the Opisthorchis viverrini. In the case of drug resistance of Opisthorchis viverrini, this causes the decreased cure efficiency of praziquantel. Therefore, the invention of a new drug used to supplement or substitute praziquantel especially in the case of drug resistance of Opisthorchis viverrini is very necessary. Study of drug likeness of praziquantel derivatives for the inhibition of thioredoxin peroxidase in Opisthorchis viverrini by molecular docking method. The derivative, most suitable for development as a drug for inhibiting thioredoxin peroxidase, is the derivative substituted with -CH2CH2OCH3 in R3 position
H2O2
highly susceptible to inactivation by H2O2; highly susceptible to inactivation by H2O2
H2O2
significant reductions in Prx II is detected at H2O2 concentrations above 0.6 mM; significant reductions in Prx I is detected at H2O2 concentrations above 0.6 mM
H2O2
high concentrations of H2O2 temporarily inactivate Tpx1
H2O2
1 mM H2O2 overoxidizes isoform Prx2 at the peroxidatic cysteine and results in the loss of the peroxidase activity
imidazole
approximately 70% of the Prx activity is lost in the presence of 0.4 M imidazole or higher. The presence of 1.6 M imidazole seems to promote protein degradation
SDS
activity is lost completely in the presence of 1% SDS or higher
additional information
during exposure to haemorrhagic septicaemia virus, HdPrxVI mRNA transcription is downregulated in the gill
-
additional information
-
during exposure to haemorrhagic septicaemia virus, HdPrxVI mRNA transcription is downregulated in the gill
-
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
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
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
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
-
insensitive to hygromycin, paromomycin, and cycloheximide
-
additional information
neither tert-butyl hydroperoxide nor cumene hydroperoxide demonstrate any observable inactivation of the enzyme, even when present at concentrations as high as 60 mM
-
additional information
-
neither tert-butyl hydroperoxide nor cumene hydroperoxide demonstrate any observable inactivation of the enzyme, even when present at concentrations as high as 60 mM
-
additional information
TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates
-
additional information
-
TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates
-
additional information
isoform Prx1 is not overoxidized by H2O2
-
additional information
isoform Prx1 is not overoxidized by H2O2
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
in the H2O2 reduction assay, AbTPx1 shows the ability to remove H2O2 without the presence of dithiothreitol. However, removal of H2O2 is promoted with the presence of dithiothreitol
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
dithiothreitol is capable of reducing the oxidised form of the Prx1 to regenerate its activity
H2O2
treatment of with H2O2 results in the dose-dependent expressions of Prx I at protein and mRNA levels
H2O2
treatment of with H2O2 results in the dose-dependent expressions of Prx II at protein and mRNA levels
additional information
AbTPx1 gene expression is induced by oxidative stress
-
additional information
AbTPx1 gene expression is induced by oxidative stress
-
additional information
AbTPx2 gene expressions is induced by oxidative stress
-
additional information
AbTPx2 gene expressions is induced by oxidative stress
-
additional information
Prx1's ability to remove H2O2 is not supported by the presence of 1 mM GSH
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
Ethyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.00665
cumene hydroperoxide
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
0.00848
cumene hydroperoxide
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
0.107
cumene hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.152
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
0.191
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
0.00098
H2O2
pH 7.0, temperature not specified in the publication, Prx231
0.0014
H2O2
in 50 mM potassium phosphate pH 7.0, at 25°C
0.0032
H2O2
pH 7.0, temperature not specified in the publication, Prx197
0.01719
H2O2
-
mutant enzyme A67D, at pH 7.0 and 25°C
0.18
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
0.193
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
0.238
tert-butyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.0009
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.0046
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.0066
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.0096
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.0122
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.00218
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.0026
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.0029
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.0173
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.0208
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.00074
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
0.0021
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
0.0026
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
0.0028
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
additional information
additional information
-
the Km-value for H2O2 is below 0.02 mM
-
additional information
additional information
both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
-
additional information
additional information
SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH
-
additional information
additional information
-
SBT Prx displays Michaelis-Menten kinetics with Trx but sigmoidal kinetics with H2O2 and CuOOH
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
52.7
Ethyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.274
cumene hydroperoxide
-
PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
0.281
cumene hydroperoxide
-
PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C
7.3
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
15.2
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
52
cumene hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
22.3
H2O2
pH 7.0, temperature not specified in the publication, Prx197
24.6
H2O2
pH 7.0, temperature not specified in the publication, Prx231
52.4
H2O2
in 50 mM potassium phosphate pH 7.0, at 25°C
3.2
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
10.4
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
54.7
tert-butyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25°C
0.01
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.015
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.092
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.099
thioredoxin A
pH 7.0, temperature not specified in the publication
-
0.009
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.045
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.072
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.212
thioredoxin B
pH 7.0, temperature not specified in the publication
-
0.01
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
0.063
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
380
cumene hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
2500
H2O2
pH 7.0, temperature not specified in the publication, Prx231
160
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx197
580
t-butyl hydroperoxide
pH 7.0, temperature not specified in the publication, Prx231
2
thioredoxin A
pH 7.0, temperature not specified in the publication
-
6
thioredoxin A
pH 7.0, temperature not specified in the publication
-
10
thioredoxin A
pH 7.0, temperature not specified in the publication
-
11
thioredoxin A
pH 7.0, temperature not specified in the publication
-
22
thioredoxin A
pH 7.0, temperature not specified in the publication
-
2
thioredoxin B
pH 7.0, temperature not specified in the publication
-
3
thioredoxin B
pH 7.0, temperature not specified in the publication
-
9.7
thioredoxin B
pH 7.0, temperature not specified in the publication
-
13
thioredoxin B
pH 7.0, temperature not specified in the publication
-
39
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
54
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
85
thioredoxin Q
pH 7.0, temperature not specified in the publication
-
additional information
additional information
characterized quinone- and nitroreductase reactions of a hybrid peroxiredoxin-nitroreductase protein, that consists of a FMN-containing nitroreductase domain fused to a peroxiredoxin domain
-
additional information
additional information
-
characterized quinone- and nitroreductase reactions of a hybrid peroxiredoxin-nitroreductase protein, that consists of a FMN-containing nitroreductase domain fused to a peroxiredoxin domain
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
0.04
0.08
mutant enzyme C83S/R128K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.1
0.12
0.18
mutant enzyme C83S/R151E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.19
mutant enzyme C83S/R151K, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.67
pH 7.4, 37°C, 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 25°C
1
mutant enzyme C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
1.07
mutant enzyme C83S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
1.49
pH 7.4, 37°C, recombinant enzyme, substrate cumene hydroperoxide
1.95
mutant enzyme C83S/C173S, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
2.32
mutant enzyme C83S, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
2.74
wild type enzyme, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.03
mutant enzyme C83S/R128E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.03
mutant enzyme C83S/R128E, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.04
mutant enzyme C83S/R128A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.04
mutant enzyme C83S/R128A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.04
mutant enzyme C83S/R128K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.1
mutant enzyme C83S/R151A, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.1
mutant enzyme C83S/R151E, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
0.12
mutant enzyme C83S/R151A, using thioredoxin as a substrate, in 150 mM potassium phosphate buffer, pH 7.4, at 25°C
0.12
mutant enzyme C83S/R151K, using dithiothreitol as a substrate, in 50 mM HEPES-NaOH (pH 7.0), at 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4 - 9
no activity at or below pH 5.4, optimal activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
80
85
95 - 100
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
5.6
7.3
7.65
Bcp4, calculated from amino acid sequence
7.73
Bcp1, calculated from amino acid sequence
8.2
8.84
Bcp3, calculated from amino acid sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
brenda
-
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
brenda
the enzyme is strongly expressed under microaerobic conditions and during the sambiotic interaction with Phaseolus vulgaris
brenda
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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
brenda
TPx1 is expressed in all developmental stages, with the highest level in gastrula
brenda
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the enzyme is mainly localized in the muscle, eggs, gut wall, uterus wall and hypodermis
brenda
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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
brenda
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the enzyme is mainly localized in the muscle, eggs, gut wall, uterus wall and hypodermis
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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the enzyme is mainly localized in the muscle, eggs, gut wall, uterus wall and hypodermis
brenda
additional information
PRDX I is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body
brenda
PRDX II is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body
brenda
PRDX III is localized to the non-pigmented epithelial cells and ciliary muscle fibers of the ciliary body
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the enzyme is mainly localized in the muscle, eggs, gut wall, uterus wall and hypodermis
brenda
the enzyme is expressed in all adult amphioxus tissues except testis, with the highest level found in the gill
brenda
upregulation after anti-white spot syndrome virus challenge
brenda
upregulation after anti-white spot syndrome virus challenge
brenda
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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
brenda
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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
brenda
stimulation of Listonella anguillarum significantly enhances the mRNA expression of PRX in hemocytes
brenda
upregulation after anti-white spot syndrome virus challenge
brenda
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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
brenda
expressed most highly during the fifth-instar larval stage
brenda
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about equal acttivity in young and mature leaves. The amount of Prx Q is decreased in senescent leaves
brenda
the gene is predominantly expressed in leaf tissue of seedlings
brenda
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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
brenda
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the enzyme is mainly localized in the muscle, eggs, gut wall, uterus wall and hypodermis
brenda
transcript level is abundant at the seed stage, but rapidly decreases after imbibitions
brenda
transcript is not detected in the seeds, but its expression level increases at germination and is maintained thereafter
brenda
transcript level is low at the seed stage, rapidly increases for 10 days after imbibitions, and gradually disappears thereafter
brenda
additional information
no activity is detected in muscles, coelomic fluid, and other internal structures
brenda
additional information
-
no activity is detected in muscles, coelomic fluid, and other internal structures
brenda
additional information
the mRNA is generally expressed in most tissues of mature plant, except root
brenda
additional information
PrxVI mRNA is constitutively expressed in all tissues in a tissue-specific manner
brenda
additional information
-
PrxVI mRNA is constitutively expressed in all tissues in a tissue-specific manner
brenda
additional information
TPx is also detected in bile fluid and bile duct epithelial cells surrounding the flukes 2 weeks after infection of hamsters with Opisthorchis viverrini
brenda
additional information
-
TPx is also detected in bile fluid and bile duct epithelial cells surrounding the flukes 2 weeks after infection of hamsters with Opisthorchis viverrini
brenda
additional information
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
brenda
additional information
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
brenda
additional information
-
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
reversible binding of the oligomeric form of the enzyme to the thylakoid membrane
brenda
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the nuclear-encoded protein TgTPx1/2 is trafficked to the apicoplast via a secretory route through the endoplasmic reticulum and to the mitochondrion via a non-secretory pathway comprising of translocon uptake. The signals for apicoplast and mitochondrial trafficking lie in the N-terminal 50 amino acids of the protein and are overlapping
brenda
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the nuclear-encoded protein TgTPx1/2 is trafficked to the apicoplast via a secretory route through the endoplasmic reticulum and to the mitochondrion via a non-secretory pathway comprising of translocon uptake. The signals for apicoplast and mitochondrial trafficking lie in the N-terminal 50 amino acids of the protein and are overlapping
-
brenda
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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
brenda
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secreted thioredoxin peroxidase protein is accumulated in the worm incubation medium under conditions of oxidative stress and in bile duct cells of hamsters with chronic opisthorchiasis
-
brenda
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after spermiation, PRDX2 localization becomes confined to the mitochondrial sheath of the sperm tail midpiece
brenda
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the nuclear-encoded protein TgTPx1/2 is trafficked to the apicoplast via a secretory route through the endoplasmic reticulum and to the mitochondrion via a non-secretory pathway comprising of translocon uptake. The signals for apicoplast and mitochondrial trafficking lie in the N-terminal 50 amino acids of the protein and are overlapping
brenda
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the nuclear-encoded protein TgTPx1/2 is trafficked to the apicoplast via a secretory route through the endoplasmic reticulum and to the mitochondrion via a non-secretory pathway comprising of translocon uptake. The signals for apicoplast and mitochondrial trafficking lie in the N-terminal 50 amino acids of the protein and are overlapping
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
additional information
drug target
-
the enzyme is a possible drug target for the development of strategies to control Babesia microti infection
drug target
-
the enzyme is unsuitable as a diagnostic antigen for baylisascariasis in pandas
malfunction
Bcp null mutant grows more slowly than its wild type in aerobic culture and shows the hypersensitivity toward various oxidants such as H2O2, tert-butyl hydroperoxide, and linoleic acid hydroperoxide
malfunction
the lack of prxQ gene results in enhanced cell sensitivity, increased ROS accumulation, and elevated protein carbonylation levels under adverse stress conditions
malfunction
-
the lack of prxQ gene results in enhanced cell sensitivity, increased ROS accumulation, and elevated protein carbonylation levels under adverse stress conditions
-
malfunction
-
Bcp null mutant grows more slowly than its wild type in aerobic culture and shows the hypersensitivity toward various oxidants such as H2O2, tert-butyl hydroperoxide, and linoleic acid hydroperoxide
-
metabolism
the enzyme plays an important role in the antioxidant defense system (peroxide-scavenging system) in an anaerobic archaeon Pyrococcus horikoshii
metabolism
-
the enzyme plays an important role in the antioxidant defense system (peroxide-scavenging system) in an anaerobic archaeon Pyrococcus horikoshii
-
physiological function
peroxiredoxins are cysteine-dependent peroxidases that function as antioxidant enzymes and also in H2O2-mediated cell signaling
physiological function
the enzyme plays a major role in the reponse of the bacterium to oxidative stress
physiological function
to survive under oxidative stress imposed by the host, microorganisms express antioxidant proteins, including cysteine-based peroxidases named peroxiredoxins
physiological function
the enzyme may play an important role in the resistance against oxygen
physiological function
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 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
the enzyme defends against oxidative stress through decomposition of hydroperoxide
physiological function
-
AhpC of Leptospira interrogans is a thioredoxin-dependent peroxiredoxin that plays an important role in protecting Leptospira interrogans against oxidative stress in macrophages
physiological function
CsTPX3 is involved in the defense against oxidative stress
physiological function
Echinococcus granulosus infection and excretory-secretory products, including thioredoxin peroxidase, can induce peritoneal macrophage recruitment and alternative activation, at least in part, via the PI3K/AKT/mTOR pathway thioredoxin peroxidase-induced alternatively activated macrophages might play a key role in the resolution of inflammation and thereby favour the establishment of hydatid cysts in the host
physiological function
the enzyme plays an antioxidant role in vivo and helps cells survive the oxidative stress. It might participate in innate immunity
physiological function
the enzyme plays an important role in defense against oxidative stress
physiological function
-
the enzyme plays an important role in defense against oxidative stress
physiological function
the stress-inducible peroxidase TSA2 underlies a conditionally beneficial chromosomal duplication
physiological function
the enzyme can protect DNA from oxidative damages. The enzyme plays a critical role in oxidative stresses and M2 macrophage polarization
physiological function
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
physiological function
-
the enzyme is involved in protecting Grapholita molesta from stresses induced by emamectin benzoate. The enzyme contribute to the defense of oxidative damage induced by exposure to emamectin benzoate through scavenging excessive reactive oxygen species
physiological function
-
the enzyme switches macrophages into the M2 phenotype during Trichinella spiralis infection
physiological function
-
the enzyme plays a major role in the reponse of the bacterium to oxidative stress
-
physiological function
-
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
-
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
-
the enzyme plays an important role in defense against oxidative stress
-
physiological function
Trichinella spiralis ISS534
-
the enzyme switches macrophages into the M2 phenotype during Trichinella spiralis infection
-
physiological function
-
the enzyme defends against oxidative stress through decomposition of hydroperoxide
-
additional information
although this Tp peroxiredoxin closely resembles AhpC-like peroxidoxins, Treponema pallidum lacks AhpF, the typical reductant for such enzymes. Functionally, TpAhpC resembles largely eukaryotic, nonAhpC typical 2-Cys Prx proteins in using thioredoxin as an efficient electron donor and exhibiting broad specificity toward hydroperoxide substrates
additional information
-
although this Tp peroxiredoxin closely resembles AhpC-like peroxidoxins, Treponema pallidum lacks AhpF, the typical reductant for such enzymes. Functionally, TpAhpC resembles largely eukaryotic, nonAhpC typical 2-Cys Prx proteins in using thioredoxin as an efficient electron donor and exhibiting broad specificity toward hydroperoxide substrates
additional information
regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body
additional information
regulation of BiPrx1 and BiTPx1 expression via reduction of transcript levels in the fat body with RNA interference, overview. RNAi-induced BiPrx1 knockdown in worker bees causes upregulated expression of BiTPx1. Reciprocally, BiTPx1 RNAi knockdown causes upregulation of BiPrx1 expression in the fat body
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
the fish Prx 2 contains the GGLG motif associated with the sensitivity of eukaryotic typical 2-Cys Prx proteins to overoxidation and consequent inactivation by H2O2
additional information
-
the fish Prx 2 contains the GGLG motif associated with the sensitivity of eukaryotic typical 2-Cys Prx proteins to overoxidation and consequent inactivation by H2O2
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16980
Bcp3, calculated from amino acid sequence
17000
17460
18000
18530
20000
20100
21800
22000
23000
24000
24700
x * 24700, 1-Cys peroxiredoxin, calculation from nucleotide sequence
25000
250000
27000
27345
-
10 * 27345, the enzyme exists as a homodecameric ring structure composed of five dimers, MALDI-TOF spectrometry
400000
50000
17460
Bcp1, calculated from amino acid sequence
17460
Bcp4, calculated from amino acid sequence
21800
x * 21800, 2-Cys peroxiredoxin, calculation from nucleotide sequence
22000
1 * 22000, mutant enzyme DELTA66-273 migrates as a monomer under reducing conditions
22000
2 * 22000, mutant enzyme DELTA66-273 migrates as a dimer under non-reducing SDS-PAGE
22000
-
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
22000
1 * 22000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer
22000
2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms
23000
10 * 23000, SDS-PAGE, the wild type enzyme exists as a mixture of various forms, favoring the homodecamer at higher protein concentration and lower ionic salt concentration and in the presence of dithiothreitol
25000
1 * 25000, SDS-PAGE, after reduction with 10 mM dithiothreitol the protein appears as a reduced monomer
50000
2 * 50000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
hexadecamer
hexamer
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
monomer
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
additional information
?
x * 21800, 2-Cys peroxiredoxin, calculation from nucleotide sequence
?
x * 24700, 1-Cys peroxiredoxin, calculation from nucleotide sequence
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
decamer
-
10 * 27345, the enzyme exists as a homodecameric ring structure composed of five dimers, MALDI-TOF spectrometry
decamer
-
consisting of pentamers of homodimers that have a doughnut-like shape
dimer
2 * 24000, existed as a dimer under non-reducing conditions, and is dissociated into monomers by dithiothreitol. It might predominantly exist in oligomeric form, SDS-PAGE
dimer
2 * 22000, mutant enzyme DELTA66-273 migrates as a dimer under non-reducing SDS-PAGE
dimer
2 * 22000, SDS-PAGE, the protein readily interconverts between dimer and oligomeric forms
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
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
-
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
-
homodimer
2 * 50000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer
monomer
1 * 22000, SDS-PAGE, under atmospheric oxidations the protein appears as a small oxidized monomer and as a major oxidized dimer
monomer
1 * 25000, SDS-PAGE, after reduction with 10 mM dithiothreitol the protein appears as a reduced monomer
monomer
1 * 22000, mutant enzyme DELTA66-273 migrates as a monomer under reducing conditions
monomer
1 * 17000, SDS-PAGE, the enzyme does not form a homodimer under non-reducing conditions, even after treatment with H2O2
additional information
-
Prx is a toroid-shaped pentamer of homodimers, or an (alpha2)5 decamer
additional information
the crystal structure shows that peroxiredoxin 5 does not form a dimer
additional information
-
the crystal structure shows that peroxiredoxin 5 does not form a dimer
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
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
-
the enzyme occurs in both dimeric and decameric forms when purified under non-reducing conditions
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 native SBT Prx enzyme exists as a mixture of dimers, tetramers, decamers and a higher order aggregate
additional information
-
the native SBT Prx enzyme exists as a mixture of dimers, tetramers, decamers and a higher order aggregate
additional information
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
-
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
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
-
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.3 A resolution, microbatch method at 18°C, using a crystallization robot, TERA
-
in complex with H2O2, hanging drop vapour diffusion method, at 20°C, 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
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 18°C, 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
hanging drop vapour diffusion method with 100 mM citrate (pH 4.6) and 10% polyethylene glycol
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 18°C
hanging drop vapor diffusion method, using 0.1 M sodium citrate and 16% (w/v) ammonium sulfate, at pH 6.4
-
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
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
enzyme complexed with thioredoxin Trx2 mutant C34S, sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol 3,350, 0.2 M lithium sulfate, 0.1 M HEPES-NaOH, pH 7.5
crystallized using the vapour-diffusion method. The crystal grows in a condition consisting of 1.8 mol/l tri-ammonium citrate, pH 7.0 using 1 g/l protein solution at 16°C. A complete data set is collected from a crystal to 2.75 A resolution. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 35.80 A, b = 50.63 A, c = 88.52 A, alpha = beta = gamma = 90°. One molecule is found in the asymmetric unit
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, 25°C, 2 days, X-ray diffraction structur determination and analysis at 2.3 A resolution
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
-
hanging drop vapor diffusion method, using 30% (w/v) PEG 400, 200 mM MgCl2, and 100 mM HEPES pH 7.5
structure in a reduced state and non-catalytic conformation. The overall fold is similar to the other phospholipid-hydroperoxide glutathione peroxidases
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 20°C, X-ray diffraction structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C207S
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
C50S/C213S
mutant enzyme only exists in the monomeric form. No peroxidase activity
C207S
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
-
C45S
C53S
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
neither the basal nor the ATP-inhibited peroxidase activities are appreciably different from wild type 2-Cys Prx
DELTA66-273
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
C45S
mutation results in a complete loss of thiol peroxidase activity
C50S
mutant enzyme show about 55% of wild-type activity with H2O2 as substrate
C99S
mutant enzyme show about 95% of wild-type activity with H2O2 as substrate
C50S
-
mutant enzyme show about 55% of wild-type activity with H2O2 as substrate
-
C99S
-
mutant enzyme show about 95% of wild-type activity with H2O2 as substrate
-
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
C48S
-
mutant enzyme shows no detectable thioredoxin-dependent peroxidase 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
C83S
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
A67D
-
the mutant shows reduced activity compared to the wild type enzyme
A67D/C176S
-
the mutant shows reduced activity compared to the wild type enzyme
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
C76A
mutant enzyme retains about 25% of the wild type peroxiredoxin activity
V152C
the mutant enzyme is inactive with glutaredoxin as a proton donor, it is catalytically active with thioredoxin
C126S
very weak activity both with substrate H2O2 and t-butyl hydroperoxide
C173S
decameric mutant enzyme, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions
C247S
weak activity both with substrate H2O2 and t-butyl hydroperoxide
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
C81S
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
C45S
C50S
C50S
-
still active in assay with H2O2 and reduced dithiothreitol. Mutant enzyme occurs in a dimeric and a tetrameric form
-
C47S
-
the Cys47 residue of Tsa1 is not required for chaperone activity but is essential for peroxidase activity
C44S
expression of PrxQ suppresses the hypersensitivity of an Escherichia coli bcp mutant to peroxides, indicating that it might exert an antioxidant activity in vivo. Escherichia coli bcp cells producing the mutant enzyme show the same sensitivities to the organic peroxides as those of the control bcp cells
C49S
expression of PrxQ suppresses the hypersensitivity of an Escherichia coli bcp mutant to peroxides, indicating that it might exert an antioxidant activity in vivo. Escherichia coli bcp cells producing the mutant enzyme show the same sensitivities to the organic peroxides as those of the control bcp cells. Except that the bcp cells producing C49S show partial resistance to tert-butyl hydroperoxide
C52A
-
parasites expressing CPX C52A fail to confer peroxynitrite resistance
C81A
-
parasites expressing MPX C81A fail to confer peroxynitrite resistance
C101S
site-directed mutagenesis, structure comparison to the wild-type enzyme
C23S
site-directed mutagenesis, structure comparison to the wild-type enzyme
C47S
site-directed mutagenesis, structure comparison to the wild-type enzyme
C83S
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
additional information
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
the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method
C207S
-
the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method
-
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
-
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
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
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
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
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
-
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
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
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
additional information
construction of shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
additional information
peroxiredoxin-nitroreductase hybrid enzyme that consists of a FMN-containing nitroreductase domain fused to a peroxiredoxin domain
additional information
-
peroxiredoxin-nitroreductase hybrid enzyme that consists of a FMN-containing nitroreductase domain fused to a peroxiredoxin domain
additional information
-
peroxiredoxin-nitroreductase hybrid enzyme that consists of a FMN-containing nitroreductase domain fused to a peroxiredoxin domain
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
AhpE is unstable and precipitates under low pH conditions (below pH 4.5)
696360
5 - 11
5 - 11
the enzyme is stable under a broad pH range from 5.0 to 11.0
698042
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 90
H2O2 reduction activity increases from 30 to 37°C and gradually decreases from 37 to 90°C
60
80
80 - 100
80 - 100
Bcp1 shows no loss of activity after 2 h incubation at 80°C, displays a half-life of 2 h at 95°C but after a 60 min incubation at 100°C its relative activity drops to 20% of the starting value
80 - 100
Bcp3 shows no loss of activity after 2 h incubation at 80°C, after 2 h at 95°C relative activity drops to 60%
80 - 100
Bcp4 shows no loss of activity after 2 h incubation at 80°C, after 2 h at 95°C relative activity drops to 92%
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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
-
sensitive to trypsin and chymotrypsin treatment. Very little or no activity detected after 40 min incubation with either protease
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
the enzyme shows 57% activity after 40 min of incubation at 37°C with trypsin, the enzyme shows 46% activity after 20 min of incubation at 37°C with one-tenth its weight of chymotrypsin, the enzyme retains about 45% activity in 0.2 M imidazole
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
Bcp4 retains 50% of its activity after a 30 min incubation in 6 M urea
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
688901
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
722563
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ACA44 gel filtration, and DEAE Sephacel column chromatography
-
DE-52 column chromatography and 2',5'-ADP-Sepharose affinity column chromatography
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
-
HisTrap HP column chromatography, Resource S column chromatography, and Resource Q column chromatography
Ni-NTA resin column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
nickel-chelate affinity column chromatography
phenyl-Sepharose column chromatography, S-Sepharose column chromatography, hydroxyapatite column chromatography, and G25 gel filtration
recombinant enzyme versions PRX264, Prx231, and Prx197 from Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme from Escherichia coli by nickle affinity chromatography and gel filtration
recombinant Prx 2 from Escherichia coli by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chitin-tagged protein is expressed in Escherichia coli BL21(DE3) cells
-
coding region is subcloned into pAVD10, transformed into Escherichia coli, and expressed as a His-tagged fusion protein
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli C43(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed with a polyhistidine-tag in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli overexpression system (BL21 DE3)pKD601. Expression of PrxQ suppresses the hypersensitivity of an Escherichia coli bcp mutant to peroxides, indicating that it might exert an antioxidant activity in vivo
expression of N-terminally truncated enzyme in Escherichia coli, DELTA66-273
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
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)
gene prxq, expression of wild-type and mutant PrxQs in Escherichia coli strain BL21(DE3)
mutant enzymes are overproduced in soluble form as fusion with a C-terminal eight-residue histidine tag in Escherichia coli BL21
Prx 2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression in Escherichia coli
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
72-fold upregulation is induced by a short oxygen exposure
enzyme expression is neither induced by H2O2 nor controlled by OxyR
exposure to various oxidative stressors, such as cold (8°C), heat (35°C), bacteria (Escherichia coli), and insecticides (chlorpyrifos and lambda-cyhalothrin), significantly upregulates transcription of CsTpx3
following the addition of 1 mM hydrogen peroxide to Synechocystis cultures, the transcript level of the gene decreases during the first 15 min and thereafter increases to the initial levels
following the addition of 1 mM hydrogen peroxide to Synechocystis cultures, the transcript level of the gene decreases during the first 15 min and thereafter increases to the initial levels. Induction of the 2-cys prx gene in response to high light intensity
following the addition of 1 mM hydrogen peroxide to Synechocystis cultures, the transcript level of the gene decreases during the first 15 min and thereafter increases to the initial levels. The transcript level of the prxII gene increases during nitrogen starvation
in Pyrococcus horikoshii cells the enzyme is induced by oxygen and hydrogen peroxide
induced as a cellular adaptation in response to the addition of exogenous H2O2
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
isoform Prx2 is induced by trace amounts of H2O2 and thereby residential in cells grown aerobically
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
SigH activates prxQ expression by directly binding to the prxQ promoter
the expression level gradually elevates during exponential growth until mid-log phase growth beyond which the expression level is decreased
the expression level gradually elevates during exponential growth until mid-log phase growth. The enzyme (BCP) is induced 3fold by the oxidative stress given by changing the growth conditions from the anaerobic to aerobic culture
the mRNA expression is upregulated 24 h after treatment with emamectin benzoate
-
transcription of the gene increases by the addition of exogenous oxygen and by the addition of an oxidative stress-inducing reagent, and reaches maximum within 30 min
when incubated with chloroquine diphosphate salt for 24 h in vitro, the expression of BmTPx-Q shows a marked downward trend with the increase of drug concentration
-
enzyme expression is neither induced by H2O2 nor controlled by OxyR
enzyme expression is neither induced by H2O2 nor controlled by OxyR
-
-
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
-
-
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
isoform Prx1 is occasionally expressed only in cells exposed to high levels of H2O2
-
-
isoform Prx2 is induced by trace amounts of H2O2 and thereby residential in cells grown aerobically
isoform Prx2 is induced by trace amounts of H2O2 and thereby residential in cells grown aerobically
-
-
SigH activates prxQ expression by directly binding to the prxQ promoter
SigH activates prxQ expression by directly binding to the prxQ promoter
-
-
the expression level gradually elevates during exponential growth until mid-log phase growth beyond which the expression level is decreased
the expression level gradually elevates during exponential growth until mid-log phase growth beyond which the expression level is decreased
-
-
the expression level gradually elevates during exponential growth until mid-log phase growth. The enzyme (BCP) is induced 3fold by the oxidative stress given by changing the growth conditions from the anaerobic to aerobic culture
the expression level gradually elevates during exponential growth until mid-log phase growth. The enzyme (BCP) is induced 3fold by the oxidative stress given by changing the growth conditions from the anaerobic to aerobic culture
-
-
transcription of the gene increases by the addition of exogenous oxygen and by the addition of an oxidative stress-inducing reagent, and reaches maximum within 30 min
transcription of the gene increases by the addition of exogenous oxygen and by the addition of an oxidative stress-inducing reagent, and reaches maximum within 30 min
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the enzyme is a potential vaccine candidate against trichinosis
medicine
Trichinella spiralis ISS534
-
the enzyme is a potential vaccine candidate against trichinosis
-
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EXTERNAL LINKS (specific for EC-Number 1.11.1.24)
Transporter Classification Database (TCDB): 8.A.147.1.1
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Release 2023.1 (January 2023)
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