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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

Crystallization

Crystallization on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin

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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°
hanging drop vapor diffusion method
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
crystal form of human peroxiredoxin 5 is described at 2.0 A resolution
hanging drop vapour diffusion method with 100 mM citrate (pH 4.6) and 10% polyethylene glycol
structure of decameric 2-Cys peroxiredoxin at 1.7 A resolution
-
sulfredoxin in complex with PrxI, hanging-drop vapour diffusion method, in 20 mM HEPES pH 7.5 and 100 mM NaCl
the C72S mutant is crystallized by hanging drop vapour diffusion method with sodium cacodylate 0.1 M pH 6.5, PEG8000 20% (w/v), sodium acetate 0.1 M, and 6-aminocaproic acid 3% (w/v), at 18°C
hanging drop vapor diffusion method, using 0.1 M sodium citrate and 16% (w/v) ammonium sulfate, at pH 6.4
-
sitting-drop vapour diffusion
-
isoform PvTrx-Px1, in reduced and oxidized form, to 2.45 and 2.5 A resolution. The structures contain the typical thioredoxin-fold found in known peroxiredoxins. There is a central 7-stranded beta-sheet sandwiched by alpha1 and alpha4 on one side and alpha2, alpha3, and alpha5 on the other side. Isoform Trx-Px1 is a H2O2-sensitive peroxiredoxin
-
isoform Trx-Px1, in oxidized form, to 2.2 A resolution. The structure contains the typical thioredoxin-fold found in known peroxiredoxins. There is a central 7-stranded beta-sheet sandwiched by alpha1 and alpha4 on one side and alpha2, alpha3, and alpha5 on the other side. Isoform Trx-Px1 is a H2O2-sensitive peroxiredoxin
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