peroxiredoxin EC#: 1.11.1.15; ChemWhat Code: 1374843

Product Name peroxiredoxin
Example Structure Example Structure of peroxiredoxin EC#: 1.11.1.15
Synonyms 1-Cys peroxiredoxin, 1-Cys Prdx, 1-Cys Prx, 1-Cys type Prx, 1Cys-peroxiredoxin, 2-CP, 2-Cys peroxiredoxin, 2-Cys peroxiredoxin 4, 2-Cys peroxiredoxin TPx-1, 2-Cys Prx, 2-Cys type Prx, 2-cysteine peroxiredoxin, 25 kDa thiol-specific oxidant, 2Cys-peroxiredoxin, AbTPx1, AbTPx2, Ac-1-Cys Prx, Ahp, AhpC, AhpC-like peroxiredoxin, AhpC-like Prx, AhpE, Alkyl hydroperoxide reductase, alkyl hydroperoxide reductase C component, APE2278, ApTPx, AsPrx, atypical 2-Cys peroxiredoxin, atypical two-cysteine peroxidase, bacterioferritin comigratory protein, BCP, Bcp1, Bcp2, Bcp3, Bcp4, BiPrx1, BiTPx1, C-PrxII, C2C-Prx, calpromotin, CIC-Prx, cPrx I, cPrx II, CPX, DTT-dependent peroxidase, EcTpx, FhePrx, GPX1, Gpx2, HBP23/Prx I, heme-binding protein 23/peroxiredoxin, LimTXNPx, More, MPX, MtTPx, natural killer enhancing factor-B, NES-Prx1, NLS-Prx1, nuclear export signal-Prx1, nuclear localization signal-Prx1, PcPrx-1, 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 VI, peroxiredoxin-1, peroxiredoxin-3, peroxiredoxin-4, Pf1-Cys-Prx, PfAOP, PfTrx-Px1, PfTrx-Px2, PH1217, PH1217 protein, PRDX I, PRDX II, PRDX III, PRDX-2, PRDX-3, PRDX1, PRDX2, PRDX5, Prdx6, Prx, Prx 2, Prx 3, Prx 4, Prx I, Prx II, Prx III, PRx IV, Prx Q, Prx V, Prx VI, Prx-4, Prx1, Prx2, Prx3, Prx5, Prx6, PrxII F, PrxQ, PrxT, PrxV, PrxVI, Px IV, rDiPrx-1, Rv2238c, SAOUHSC_01822, SSO2613, TgPrx2, TgTrx-Px1, TgTrx-Px2, thiol-specific antioxidant/protector protein, thioredoxin peroxidase, thioredoxin peroxidase 1, thioredoxin peroxidase B, thioredoxin peroxidase II, thioredoxin-dependent alkyl hydroperoxide reductase, thioredoxin-dependent peroxidase, TM0807, torin, TP0509, Tpx, TPx I, TPx II, TPx-1, TPx-B, TPx1, tryparedoxin peroxidase, tryparedoxin/peroxynitrite oxidoreductase, Ts2-CysPrx, TSA, TSA thioredoxin peroxidase Tpx, Tsa1, TsaA, two-cysteine peroxiredoxin, TXNPx, type II peroxiredoxin, type II peroxiredoxin F, typical 2-Cys peroxiredoxin, typical 2-Cys Prx
EC Number 1.11.1.15
CAS Registry Number
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 [1]. 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). 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 (R’-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), 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 [1]. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor [3]. The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule [4].
Cofactor
History
Reactions 2 R’-SH + Rooh = R’-S-S-R’ + H(2)O + roh.

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