1.11.1.24: thioredoxin-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about thioredoxin-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.24
-
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
- 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
Reaction
2 R'-SH
+
Synonyms
1-Cys peroxiredoxin, 1-Cys Prx, 1-Cys type Prx, 2-Cys peroxiredoxin, 2-Cys peroxiredoxin 4, 2-Cys Prx, 2-Cys type Prx, 25 kDa thiol-specific oxidant, 2Cys-peroxiredoxin, AbTPx1, AbTPx2, Ac-1-Cys Prx, Ahp, Ahp1, AhpC, AhpC-like peroxiredoxin, AhpC-like Prx, AhpC2, AhpE, alkyl hydroperoxide reductase, alkyl hydroperoxide reductase C component, alkyl hydroperoxide reductase subunit C, alkylhydroperoxide reductase subunit C, APE2278, ApTPx, AsPrx, atypical two-cysteine peroxidase, bacterioferritin comigratory protein, BCP, Bcp1, Bcp3, Bcp4, BiPrx1, BiTPx1, BmTPx-Q, C-PrxII, C2C-Prx, calpromotin, CIC-Prx, cPrx I, cPrx II, CPX, DTT-dependent peroxidase, EC 1.11.1.15, EcTpx, EgTPx, FhePrx, GPX, HBP23/Prx I, heme-binding protein 23/peroxiredoxin, LimTXNPx, More, MPX, MtTPx, natural killer enhancing factor-B, ncgl2403, NES-Prx1, NLS-Prx1, nuclear export signal-Prx1, nuclear localization signal-Prx1, peroxiredoxin, peroxiredoxin 1, peroxiredoxin 2, peroxiredoxin 3, peroxiredoxin 4, peroxiredoxin 5, peroxiredoxin 6, peroxiredoxin I, peroxiredoxin II, peroxiredoxin III, peroxiredoxin IV, peroxiredoxin Q, peroxiredoxin V, peroxiredoxin-1, peroxiredoxin-3, peroxiredoxin-4, PfTrx-Px1, PfTrx-Px2, PH1217, PH1217 protein, PRDX I, PRDX II, PRDX III, PRDX-2, PRDX-3, PRDX2, PRDX5, Prdx6, Prx, Prx 2, Prx 3, Prx 4, Prx I, Prx II, Prx III, PRx IV, Prx Q, Prx Q1, Prx Q2, Prx V, Prx VI, Prx-4, Prx1, Prx2, Prx3, Prx5, PrxII, PrxII F, PrxQ, PrxT, PrxV, PrxVI, Rv2238c, SAOUHSC_01822, SF2523, sll0221, sll0755, sll1621, slr0242, slr1198, SSO2613, tgTPx1/2, TgTrx-Px1, TgTrx-Px2, thiol-specific antioxidant/protector protein, thioredoxin peroxidase, thioredoxin peroxidase 1, thioredoxin peroxidase 1/2, thioredoxin peroxidase 2, thioredoxin peroxidase B, thioredoxin peroxidase II, thioredoxin peroxidase TSA2, thioredoxin-dependent alkyl hydroperoxide reductase, thioredoxin-dependent peroxiredoxin Q, thioredoxin-dependent thiol peroxidase, TM0807, torin, TP0509, Tpx, TPx I, TPx II, TPx-1, TPx-B, TPx1, TPx1/2, TPX2, Tpx3, TRIREDRAFT_47136, tryparedoxin peroxidase, tryparedoxin/peroxynitrite oxidoreductase, Ts2-CysPrx, TSA, TSA thioredoxin peroxidase Tpx, Tsa1, TsaA, two-cysteine peroxiredoxin, TXNPx, type II peroxiredoxin, typical 2-Cys peroxiredoxin, typical 2-Cys Prx
ECTree
1.11.1.24 thioredoxin-dependent peroxiredoxinAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin
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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
?
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Tpx1 is an upstream activator of Pap1. At low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations
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shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not
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both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics
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peroxidases belonging to the class of 1-Cys and 2-Cys peroxiredoxins play crucial roles in maintaining redox balance. TgTrx-Px1 is an extremely potent antioxidant
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TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
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TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview
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alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
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alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
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additional information
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alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
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additional information
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alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity
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additional information
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Cys83 is the resolving cysteine of XfPrxQ
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Cys83 is the resolving cysteine of XfPrxQ
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