Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Systematic Name

Systematic Name on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.