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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

Reaction

2 R'-SH +

ROOH
=
R'-S-S-R'
 +
H2O
 +
ROH

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 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.24 thioredoxin-dependent peroxiredoxin

Engineering

Engineering on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
C183S
strongly reduced activity
C86S
rate constant of H2O2 reduction is similar to wild-type
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
Y166F
autophosphorylation is similar to 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
C80S
-
reduced activity
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
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
-
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
mutant lacks antioxidant activity
C52S/C173S
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
C72S
the C72S mutation improves the crystallization in oxidizing conditions
C73S
-
mutation has no effect on activity
C60S
-
inactive mutant enzyme
C80S
-
mutant is indistinguishable from the wild-type enzyme
C93S
-
the mutant is fully active as a thioredoxin-dependent peroxidase and remains active despite exposure to peroxynitrite, pronounced instability of the mutant enzyme under oxidizing conditions
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
C48S
12% activity compared to the wild type enzyme
C59S
inactive
C170A
-
kcat/Km of mutant enzyme is reduced for thioredoxin as a substrate approximately 50fold. In contrast to the wildtype enzyme, covalently linked dimers are not formed
C51A
mutation abolishes catalysis
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
C150S
activity similar to wild-type
C173S
decameric mutant enzyme, cannot form an intermolecular disulfide bridge in the vicinity of the active site under oxidative conditions
C247S
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
C156S
no peroxidase activity
C56S
no peroxidase activity
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
C102S
-
activity is similar to the wild type enzyme
C48S
-
reduced activity
C48S/C102S
-
reduced activity
C45S
-
inactive in assay with H2O2 and reduced dithiothreitol
-
C50S
-
still active in assay with H2O2 and reduced dithiothreitol. Mutant enzyme occurs in a dimeric and a tetrameric form
-
C47S
-
the Cys47 residue of Tsa1 is not required for chaperone activity but is essential for peroxidase activity
C169S
decreased activity
C48S
completely inactive
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
C171S
complete loss of activity
C50S
complete loss of activity
C171S
-
complete loss of activity
-
C50S
-
complete loss of activity
-
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