1.8.98.2 2-Cys peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH - Pisum sativum 2-Cys peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 440662 1.8.98.2 additional information no activity with CTP, UTP, dCTP, or dTTP Homo sapiens ? - ? 89 1.8.98.2 additional information catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation Mus musculus ? - ? 89 1.8.98.2 additional information catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation Homo sapiens ? - ? 89 1.8.98.2 additional information catalyzes the deglutathionylation of actin Homo sapiens ? - ? 89 1.8.98.2 additional information promotes the reversal of cysteine modified PTP1B to its reduced and enzymatically active form Homo sapiens ? - ? 89 1.8.98.2 additional information reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress Homo sapiens ? - ? 89 1.8.98.2 additional information assay conditions optimization, overview Arabidopsis thaliana ? - ? 89 1.8.98.2 additional information enzyme is able to act as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme. Sulfiredoxin functions as a nuclease enzyme that can use single-stranded and double-stranded DNAs as substrates. The active site of the reductase function of sulfiredoxin is not involved in its nuclease function Arabidopsis thaliana ? - ? 89 1.8.98.2 additional information AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo Arabidopsis thaliana ? - - 89 1.8.98.2 additional information Srx forms a complex with the endoplasmic reticulum-resident protein thioredoxin domain-containing protein 5 (TXNDC5) in vivo and in vitro. TXNDC5 directly interacts with Srx through its thioredoxin-like domains, mapping of the interacting domains between Srx and TXNDC5, the thioredoxin-like domains 1 and 3 are responsible for the binding to Srx, overview. Deletion of the first or third thioredoxin-like domain in TXNDC5 results in a significant loss of its binding to Srx, whereas deletion of the second (the one in the middle) thioredoxin-like domain does not compromise its binding to Srx. The Srx-TXNDC5 is a relatively stable complex that is not affected by the treatment with exogenous H2O2 Homo sapiens ? - - 89 1.8.98.2 additional information AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo. Overall structure of ADP-bound AtSrx, ADP is bound at a positive charged pocket of AtSrx, detailed overview. AtSrx forms a complex with AtPrxA in vitro, modeling Arabidopsis thaliana ? - - 89 1.8.98.2 additional information specificity of human sulfiredoxin for reductant and peroxiredoxin oligomeric state, overview. The resolution of the Prx-Srx complex involves the reduction of the thiosulfinate intermediate (Prx-CP-S=O-S-Srx) to yield the Prx Cys-sulfenic acid intermediate (Prx-CP-SOH). Yeast Srx contains an adjacent resolving Cys residue (Cys-SR) that can react with the thiosulfinate intermediate leading to the formation of an Srx intramolecular disulfide (Srx-(S-S)). In contrast, human Srx has only one Cys residue and requires an exogenous reductant. Possible reductants include the Trx system (Trx/TrxR/NADPH), glutathione (GSH) and hydrogen sulfide (H2S), these reductants would ultimately yield reduced Srx (Srx-SH). Enzyme-substrate binding studies with mutant Prx1 (e.g. Prx1 C83V and Prx1 C71S/C173S). Repair of hyperoxidized Prx2, Prx3 and their chimeras, the C-terminal sequence differences between Prx2 and Prx3 impact the rate of repair by Srx Homo sapiens ? - - 89 1.8.98.2 additional information Srx transfers the gamma-phosphate of ATP to Cp sulfinic acid on hyperoxidized Prxs and produces sulfinic phosphoryl ester. Subsequent involvement of GSH and thioredoxin will ensure the reduction of sulfinic phosphoryl ester to sulfenic acid Homo sapiens ? - - 89 1.8.98.2 additional information assay conditions optimization, overview Arabidopsis thaliana Columbia ? - ? 89 1.8.98.2 overoxidized human peroxiredoxin V + reduced thioredoxin Arabidopsis enzyme is able to reduce overoxidized human Prx V Arabidopsis thaliana ? + oxidized thioredoxin - ? 426887 1.8.98.2 peroxiredoxin IIF-(S-hydroxy-S-oxocysteine) + ATP + GSH - Pisum sativum peroxiredoxin IIF-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 441852 1.8.98.2 peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH - Mus musculus peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 441853 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT - Arabidopsis thaliana peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide - ? 415112 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide - ? 415112 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT - Arabidopsis thaliana Columbia peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide - ? 415112 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH - Arabidopsis thaliana peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G - ? 415113 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH combined GSH and H2S for the repair of cytosolic Prx2 Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G - ? 415113 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH - Arabidopsis thaliana Columbia peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G - ? 415113 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 H2S preference for H2S to support the repair of mitochondrial hyperoxidized Prx3 by Srx. Combined GSH and H2S for the repair of cytosolic Prx2 Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + HS-SH - ? 462899 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Mus musculus peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - r 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Rattus norvegicus peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - r 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Arabidopsis thaliana peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH - Oryza sativa peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage Rattus norvegicus peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH both glutathione and thioredoxin are potential physiological electron donors Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH the ATP molecule is cleaved between the beta- and gamma-phosphate groups Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH the rate-limiting step of the reaction is associated with the chemical process of transfer of the gamma-phosphate of ATP to the sulfinic acid. Two pKapp values of 6.2 and 7.5 of the bell-shaped pH-rate profile correspond to the gamma-phosphate of ATP, and to an acid-base catalyst, respectively Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH hyperoxidized Prx1 Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 375238 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin - Mus musculus peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide - ? 415114 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin - Arabidopsis thaliana peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide - ? 415114 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide - ? 415114 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin - Arabidopsis thaliana Columbia peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide - ? 415114 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 398087 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH - Rattus norvegicus peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 398087 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG - ? 398087 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G - ? 462900 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 394951 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH - Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 394951 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature Arabidopsis thaliana peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R - ? 394951 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + thioredoxin 1 - Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin 1 disulfide - r 451790 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH both glutathione and thioredoxin are potential physiological electron donors Homo sapiens peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R - ? 377491 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + 2 R-SH both glutathione and thioredoxin are potential physiological electron donors Homo sapiens peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R - ? 377492 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + R-SH formation of a covalent thiosulfinate peroxiredoxin-sulfiredoxin species as an intermediate on the catalytic pathway Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R - ? 398088 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH - Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R - ? 426912 1.8.98.2 peroxiredoxin-(S-hydroxy-S-oxocysteine) + GTP + 2 R-SH both glutathione and thioredoxin are potential physiological electron donors Homo sapiens peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R - ? 377493 1.8.98.2 sulfinic form of peroxiredoxin IIF + oxidized thioredoxin in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent Pisum sativum ? + reduced thioredoxin - ? 427086 1.8.98.2 sulfinic form of peroxiredoxin IIF + reduced thioredoxin in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent Arabidopsis thaliana ? + oxidized thioredoxin - ? 427087