1.11.1.24 2 thioredoxin + cumene hydroperoxide - Seriola lalandi thioredoxin disulfide + H2O + 2-phenylpropan-2-ol - ? 413869 1.11.1.24 2 thioredoxin + cumene hydroperoxide - Thunnus maccoyii thioredoxin disulfide + H2O + 2-phenylpropan-2-ol - ? 413869 1.11.1.24 2 thioredoxin + cumene hydroperoxide - Xylella fastidiosa thioredoxin disulfide + H2O + 2-phenylpropan-2-ol - ? 413869 1.11.1.24 2 thioredoxin + cumene hydroperoxide - Treponema pallidum thioredoxin disulfide + H2O + 2-phenylpropan-2-ol - ? 413869 1.11.1.24 2 thioredoxin + H2O2 - Aeropyrum pernix thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Seriola lalandi thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Thunnus maccoyii thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Xylella fastidiosa thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Treponema pallidum thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Trichoderma reesei thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Aeropyrum pernix DSM 11879 thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + H2O2 - Trichoderma reesei QM6a thioredoxin disulfide + 2 H2O - ? 413870 1.11.1.24 2 thioredoxin + ROOH - Seriola lalandi thioredoxin disulfide + H2O + ROH - ? 413182 1.11.1.24 2 thioredoxin + ROOH - Bombus ignitus thioredoxin disulfide + H2O + ROH - ? 413182 1.11.1.24 2 thioredoxin + t-butyl hydroperoxide - Seriola lalandi thioredoxin disulfide + H2O + t-butanol - ? 413871 1.11.1.24 2 thioredoxin + t-butyl hydroperoxide - Thunnus maccoyii thioredoxin disulfide + H2O + t-butanol - ? 413871 1.11.1.24 2 thioredoxin + t-butyl hydroperoxide - Xylella fastidiosa thioredoxin disulfide + H2O + t-butanol - ? 413871 1.11.1.24 2 thioredoxin + t-butyl hydroperoxide - Treponema pallidum thioredoxin disulfide + H2O + t-butanol - ? 413871 1.11.1.24 2 thioredoxin + tert-butyl hydroperoxide - Trichoderma reesei thioredoxin disulfide + H2O + tert-butyl alcohol - ? 461904 1.11.1.24 2 thioredoxin + tert-butyl hydroperoxide - Trichoderma reesei QM6a thioredoxin disulfide + H2O + tert-butyl alcohol - ? 461904 1.11.1.24 cumene hydroperoxide + dithiothreitol - Homo sapiens 2-phenylpropan-2-ol + oxidized dithiothreitol - ? 388411 1.11.1.24 cumene hydroperoxide + dithiothreitol - Pyrococcus horikoshii 2-phenylpropan-2-ol + oxidized dithiothreitol - ? 388411 1.11.1.24 cumene hydroperoxide + dithiothreitol - Pyrococcus horikoshii OT-3 2-phenylpropan-2-ol + oxidized dithiothreitol - ? 388411 1.11.1.24 cumene hydroperoxide + reduced dithiothreitol low activity Homo sapiens 2-phenylpropan-2-ol + oxidized dithiothreitol - ? 396796 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Cereibacter sphaeroides 2-phenylpropan-2-ol + oxidized thioredoxin + H2O - ? 372785 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Arabidopsis thaliana 2-phenylpropan-2-ol + oxidized thioredoxin + H2O - ? 372785 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Arenicola marina 2-phenylpropan-2-ol + oxidized thioredoxin + H2O - ? 372785 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Salmonella enterica subsp. enterica serovar Typhimurium 2-phenylpropan-2-ol + oxidized thioredoxin + H2O - ? 372785 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Haliotis discus discus 2-phenylpropan-2-ol + oxidized thioredoxin + H2O - ? 372785 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Taenia solium ? - ? 388413 1.11.1.24 cumene hydroperoxide + reduced thioredoxin - Fasciola hepatica ? - ? 388413 1.11.1.24 cumene hydroperoxide + tryparedoxin 2 57% of the activity with H2O2 Leishmania infantum 2-phenylpropan-2-ol + oxidized tryparedoxin 2 - ? 372786 1.11.1.24 dithiothreitol + H2O2 - Echinococcus multilocularis H2O + oxidized dithiothreitol - ? 462453 1.11.1.24 ethyl hydroperoxide + reduced thioredoxin - Salmonella enterica subsp. enterica serovar Typhimurium ? + oxidized thioredoxin - ? 397144 1.11.1.24 Gardos channel + ? activates the Gardos channel Homo sapiens ? - ? 397226 1.11.1.24 glycine chloramine + dithiothreitol slow reaction Homo sapiens ? - ? 397352 1.11.1.24 H2O2 + dithiothreitol - Homo sapiens H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Pisum sativum H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Rhizobium etli H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Taiwanofungus camphoratus H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Saccharolobus solfataricus H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Pyrococcus horikoshii H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Chilo suppressalis H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol no activity with glutathione Branchiostoma belcheri tsingtauense H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + dithiothreitol - Pyrococcus horikoshii OT-3 H2O + oxidized dithiothreitol - ? 373378 1.11.1.24 H2O2 + ferrithiocyanate - Babesia microti H2O + ? - ? 455757 1.11.1.24 H2O2 + NADPH + H+ isoform Prx2 is able to reduce H2O2 in vitro in the presence of thioredoxin A/thioredoxin reductase as electron donors Vibrio vulnificus 2 H2O + 2 NADP+ - ? 426469 1.11.1.24 H2O2 + NADPH + H+ isoform Prx2 is able to reduce H2O2 in vitro in the presence of thioredoxin A/thioredoxin reductase as electron donors Vibrio vulnificus MO6-24/O 2 H2O + 2 NADP+ - ? 426469 1.11.1.24 H2O2 + pyrogallol - Trichoderma reesei ? - ? 462562 1.11.1.24 H2O2 + pyrogallol - Trichoderma reesei QM6a ? - ? 462562 1.11.1.24 H2O2 + reduced dithiothreitol - Rhodospirillum rubrum H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced dithiothreitol - Homo sapiens H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced dithiothreitol - Schizosaccharomyces pombe H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced dithiothreitol - Saccharolobus solfataricus H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced dithiothreitol reduced Prx2 is exceptionally reactive withH2O2 and other peroxides but shows very low reactivity with other thiol oxidants and alkylating agents Homo sapiens H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced dithiothreitol - Saccharolobus solfataricus P2 H2O + oxidized dithiothreitol - ? 397402 1.11.1.24 H2O2 + reduced plasmoredoxin - Plasmodium falciparum H2O + oxidized plasmoredoxin - ? 388868 1.11.1.24 H2O2 + reduced thioredoxin - Mus musculus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Homo sapiens H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Saccharomyces cerevisiae H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Cereibacter sphaeroides H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Arabidopsis thaliana H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Trypanosoma brucei H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Mycobacterium tuberculosis H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Trypanosoma cruzi H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Helicobacter pylori H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Plasmodium falciparum H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Taenia solium H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Rhizobium etli H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Rattus norvegicus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Brassica napus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Arenicola marina H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Schizosaccharomyces pombe H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Azumapecten farreri H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Pisum sativum H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Salmonella enterica subsp. enterica serovar Typhimurium H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Haliotis discus discus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Taiwanofungus camphoratus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Psoroptes ovis H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Caenorhabditis elegans H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin - Fasciola hepatica H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin ping-pong mechanism Toxoplasma gondii H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin ping-pong kinetics Plasmodium falciparum H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin thioredoxin from Escherichia coli and thioredoxin f and m from spinach Hordeum vulgare H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner Plasmodium falciparum H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin H2O2 is the preferred substrate compared to tert-butyl hydroperoxide Saccharolobus solfataricus H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin Prx 3 displays strong reactivity with H2O2 Homo sapiens H2O + oxidized thioredoxin - ? 373387 1.11.1.24 H2O2 + reduced thioredoxin highest activity Trichoderma reesei oxidized thioredoxin + H2O - ? 462563 1.11.1.24 H2O2 + reduced thioredoxin 2 - Homo sapiens H2O + oxidized thioredoxin 2 - ? 397403 1.11.1.24 H2O2 + reduced thioredoxin A - Vibrio vulnificus 2 H2O + oxidized thioredoxin A - ? 426470 1.11.1.24 H2O2 + reduced thioredoxin A - Vibrio vulnificus MO6-24/O 2 H2O + oxidized thioredoxin A - ? 426470 1.11.1.24 H2O2 + thioredoxin 1-Cys peroxiredoxin is less active than 2-Cys peroxiredoxin Plasmodium falciparum ? - ? 373388 1.11.1.24 H2O2 + tryparedoxin - Homo sapiens H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Saccharomyces cerevisiae H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Trypanosoma brucei H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Mycobacterium tuberculosis H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Trypanosoma cruzi H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Helicobacter pylori H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin - Plasmodium falciparum H2O + oxidized tryparedoxin - ? 405403 1.11.1.24 H2O2 + tryparedoxin 2 - Leishmania infantum H2O + oxidized tryparedoxin 2 - ? 373389 1.11.1.24 histamine chloramine + dithiothreitol slow reaction Homo sapiens ? - ? 397430 1.11.1.24 HOCl + dithiothreitol low activity Homo sapiens ? - ? 397434 1.11.1.24 iodoacetamide + reduced thioredoxin Prx 3 reacts very slowly with iodoacetamide Homo sapiens ? - ? 405495 1.11.1.24 linoleic acid hydroperoxide + reduced thioredoxin - Salmonella enterica subsp. enterica serovar Typhimurium ? + oxidized thioredoxin - ? 397701 1.11.1.24 linoleic acid hydroperoxide + tryparedoxin 2 7.8% of the activity with H2O2 Leishmania infantum ? - ? 373711 1.11.1.24 linoleoyl hydroperoxide + reduced thioredoxin - Arabidopsis thaliana ? - ? 389099 1.11.1.24 monochloramine + dithiothreitol slow reaction Homo sapiens ? - ? 397777 1.11.1.24 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 Plasmodium falciparum ? - ? 89 1.11.1.24 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 Plasmodium falciparum ? - ? 89 1.11.1.24 additional information 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 Toxoplasma gondii ? - ? 89 1.11.1.24 additional information the enzyme is essential for sustaining life span of erythrocytes in mice by protecting them from oxidative stress Mus musculus ? - ? 89 1.11.1.24 additional information the enzyme might function as a major antioxidant enzyme in Ascaris suum Ascaris suum ? - ? 89 1.11.1.24 additional information the enzyme plays a critical role in defending the organism against oxygen toxicity Helicobacter pylori ? - ? 89 1.11.1.24 additional information the enzyme promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue Homo sapiens ? - ? 89 1.11.1.24 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 Hordeum vulgare ? - ? 89 1.11.1.24 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 Homo sapiens ? - ? 89 1.11.1.24 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 Saccharomyces cerevisiae ? - ? 89 1.11.1.24 additional information no activity with glutaredoxin or glutathione Homo sapiens ? - ? 89 1.11.1.24 additional information thioredoxin m is more efficent than thioredoxin f in reducing the enzyme Pisum sativum ? - ? 89 1.11.1.24 additional information tryparedoxin peroxidase activity. The enzyme does not follow a classic ping-pong mechanism Leishmania infantum ? - ? 89 1.11.1.24 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 Rhizobium etli ? - ? 89 1.11.1.24 additional information Prx I has at least two distinct roles: as an antioxidant enzyme and as a regulator of p38 MAPK Mus musculus ? - ? 89 1.11.1.24 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 Arabidopsis thaliana ? - ? 89 1.11.1.24 additional information the enzyme is involved in the detoxification of reactive oxygen species and of reactive nitrogen species Plasmodium falciparum ? - ? 89 1.11.1.24 additional information 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 Schizosaccharomyces pombe ? - ? 89 1.11.1.24 additional information cumene hydroperoxide is not accepted as a substrate Plasmodium falciparum ? - ? 89 1.11.1.24 additional information insignificant affinity towards complex phospholipid hydroperoxide Arabidopsis thaliana ? - ? 89 1.11.1.24 additional information PfTPx1 also possesses peroxynitrite reductase activity Plasmodium falciparum ? - ? 89 1.11.1.24 additional information Prx1 shows a androgen receptor-stimulating function in response to hypoxia/reoxygenation Homo sapiens ? - ? 89 1.11.1.24 additional information thioredoxin 2 directly associates with Prx3 in vivo and functions in protection against cell death Homo sapiens ? - ? 89 1.11.1.24 additional information peroxiredoxin 2 is a key antioxidant enzyme for the erythrocyte and renders red blood cells as active oxidant scrubbers in the bloodstream Homo sapiens ? - ? 89 1.11.1.24 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 Schistosoma mansoni ? - ? 89 1.11.1.24 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 Fasciola hepatica ? - ? 89 1.11.1.24 additional information shorter versions of the enzyme, Prx231 and Prx197, both exhibit thioredoxin-dependent peroxidase activity, whereas fill-length Prx264 does not Seriola lalandi ? - ? 89 1.11.1.24 additional information both active forms of the enzyme displayed a single-displacement reaction mechanism and typical saturable Michaelis-Menten type kinetics Seriola lalandi ? - ? 89 1.11.1.24 additional information Cys83 is the resolving cysteine of XfPrxQ Xylella fastidiosa ? - ? 89 1.11.1.24 additional information TpAhpC is a broad specificity peroxiredoxin, substrate specificity, overview Treponema pallidum ? - ? 89 1.11.1.24 additional information alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity Vibrio vulnificus ? - ? 89 1.11.1.24 additional information enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone Brassica napus ? - ? 89 1.11.1.24 additional information enzyme has dual functions as peroxidase and as a molecular chaperone. Presence prevents aggregation of malate dehydrogenase as a molecular chaperone Brassica rapa subsp. oleifera ? - ? 89 1.11.1.24 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 Rattus norvegicus ? - ? 89 1.11.1.24 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 Arenicola marina ? - ? 89 1.11.1.24 additional information no activity with glutathione Trichoderma reesei ? - - 89 1.11.1.24 additional information alkyl hydroperoxidase subunit F is not able to reduce oxidized isoform Prx2 to reactivate its peroxidase activity Vibrio vulnificus MO6-24/O ? - ? 89 1.11.1.24 additional information no activity with glutathione Trichoderma reesei QM6a ? - - 89 1.11.1.24 N-ethylmaleimide + reduced thioredoxin Prx 3 reacts very slowly with N-ethylmaleimide Homo sapiens ? - ? 406011 1.11.1.24 NADPH + H2O2 - Brassica rapa NADP+ + H2O - ? 260335 1.11.1.24 peroxinitrite + reduced thioredoxin - Homo sapiens ? - ? 398086 1.11.1.24 peroxinitrite + thioredoxin - Mycobacterium tuberculosis ? - ? 389529 1.11.1.24 peroxynitrite + dithiothreitol - Homo sapiens ? - ? 398090 1.11.1.24 peroxynitrite + H2O2 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 Trypanosoma cruzi nitrite + ? - ? 398091 1.11.1.24 peroxynitrite + paredoxin - Homo sapiens ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Saccharomyces cerevisiae ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Trypanosoma brucei ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Mycobacterium tuberculosis ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Trypanosoma cruzi ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Helicobacter pylori ? - ? 406367 1.11.1.24 peroxynitrite + paredoxin - Plasmodium falciparum ? - ? 406367 1.11.1.24 peroxynitrite + reduced thioredoxin AhpE reduces peroxynitrite 2 orders of magnitude faster than H2O2 Mycobacterium tuberculosis ? - ? 406368 1.11.1.24 phosphatidyl choline hydroperoxide + tryparedoxin 2 3.8% of the activity with H2O2 Leishmania infantum ? - ? 374329 1.11.1.24 taurine chloramine + dithiothreitol slow reaction Homo sapiens ? - ? 398398 1.11.1.24 tert-butyl hydroperoxide + dithiothreitol - Pisum sativum tert-butanol + oxidized dithiothreitol - ? 374698 1.11.1.24 tert-butyl hydroperoxide + dithiothreitol - Homo sapiens tert-butanol + oxidized dithiothreitol - ? 374698 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Homo sapiens ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Saccharomyces cerevisiae ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Trypanosoma brucei ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Mycobacterium tuberculosis ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Trypanosoma cruzi ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Helicobacter pylori ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + peroxynitrite - Plasmodium falciparum ? - ? 406742 1.11.1.24 tert-butyl hydroperoxide + reduced dithiothreitol - Taiwanofungus camphoratus tert-butanol + oxidized dithiothreitol - ? 389856 1.11.1.24 tert-butyl hydroperoxide + reduced dithiothreitol - Rattus norvegicus tert-butanol + oxidized dithiothreitol - ? 389856 1.11.1.24 tert-butyl hydroperoxide + reduced dithiothreitol - Arenicola marina tert-butanol + oxidized dithiothreitol - ? 389856 1.11.1.24 tert-butyl hydroperoxide + reduced dithiothreitol low activity Homo sapiens tert-butanol + oxidized dithiothreitol - ? 389856 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Arabidopsis thaliana tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Toxoplasma gondii tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Salmonella enterica subsp. enterica serovar Typhimurium tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Haliotis discus discus tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Trichoderma reesei tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Saccharomyces cerevisiae tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin 9.5% of the activity with tert-butyl hydroperoxide and tryparedoxin 2 Leishmania infantum tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin the peroxiredoxin preferrs PfTrx2 to PfTrx1 as a reducing partner Plasmodium falciparum tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin H2O2 is the preferred substrate compared to tert-butyl hydroperoxide Saccharolobus solfataricus tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Trichoderma reesei QM6a tert-butanol + oxidized thioredoxin + H2O - ? 374700 1.11.1.24 tert-butyl hydroperoxide + reduced thioredoxin - Fasciola hepatica ? - ? 389857 1.11.1.24 tert-butyl hydroperoxide + tryparedoxin 2 95% of the activity with H2O2 Leishmania infantum tert-butanol + oxidized tryparedoxin 2 - ? 374701 1.11.1.24 thioredoxin + cumene hydroperoxide - Sedum lineare thioredoxin disulfide + H2O + cumene hydroxide - ? 450754 1.11.1.24 thioredoxin + H2O2 - Sedum lineare thioredoxin disulfide + 2 H2O - ? 412976 1.11.1.24 thioredoxin + H2O2 peroxiredoxin Cys51 and glutaredoxin Cys27 are involved in the catalytic mechanism. The enzyme also accepts glutaredoxin as electron donor Populus trichocarpa thioredoxin disulfide + 2 H2O - ? 412976 1.11.1.24 thioredoxin + H2O2 the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli thioredoxin disulfide + 2 H2O - ? 412976 1.11.1.24 thioredoxin + H2O2 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 Leptospira interrogans thioredoxin disulfide + 2 H2O - ? 412976 1.11.1.24 thioredoxin + H2O2 the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli K12 thioredoxin disulfide + 2 H2O - ? 412976 1.11.1.24 thioredoxin + linoleic acid hydroperoxide - Escherichia coli thioredoxin disulfide + H2O + linoleic acid - ? 448989 1.11.1.24 thioredoxin + linoleic acid hydroperoxide the enzyme defends against oxidative stress through decomposition of hydroperoxide Escherichia coli thioredoxin disulfide + H2O + linoleic acid - ? 448989 1.11.1.24 thioredoxin + linoleic acid hydroperoxide - Escherichia coli K12 thioredoxin disulfide + H2O + linoleic acid - ? 448989 1.11.1.24 thioredoxin + linoleic acid hydroperoxide the enzyme defends against oxidative stress through decomposition of hydroperoxide Escherichia coli K12 thioredoxin disulfide + H2O + linoleic acid - ? 448989 1.11.1.24 thioredoxin + tert-butyl hydroperoxide - Sedum lineare thioredoxin disulfide + H2O + tert-butyl alcohol - ? 450755 1.11.1.24 thioredoxin + tert-butyl hydroperoxide the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli thioredoxin disulfide + H2O + tert-butyl alcohol - ? 450755 1.11.1.24 thioredoxin + tert-butyl hydroperoxide the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli K12 thioredoxin disulfide + H2O + tert-butyl alcohol - ? 450755 1.11.1.24 thioredoxin A + cumene hydroperoxide - Synechocystis sp. PCC 6803 thioredoxin A disulfide + H2O + cumene hydroxide - ? 450756 1.11.1.24 thioredoxin A + H2O2 - Synechocystis sp. PCC 6803 thioredoxin A disulfide + 2 H2O - ? 450757 1.11.1.24 thioredoxin A + tert-butyl hydroperoxide - Synechocystis sp. PCC 6803 thioredoxin A disulfide + H2O + tert-butyl alcohol - ? 450758 1.11.1.24 thioredoxin B + H2O2 - Synechocystis sp. PCC 6803 thioredoxin B disulfide + 2 H2O - ? 450759 1.11.1.24 thioredoxin C + H2O2 - Mycobacterium tuberculosis variant bovis thioredoxin C disulfide + H2O - ? 463059 1.11.1.24 thioredoxin Q + H2O2 - Synechocystis sp. PCC 6803 thioredoxin Q disulfide + 2 H2O - ? 450760