EC Number   |
Natural Substrates |
|---|
   1.8.98.2 | more |
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation |
| 1.8.98.2 | more |
AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo |
| 1.8.98.2 | more |
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 |
| 1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH |
- |
| 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 Parkinsons disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific |
| 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 |
| 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 |
| 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 |
| 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 cysteinesulphinic acid modifications, and in signalling pathways involving protein oxidation |
| 1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin |
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