EC Number |
Natural Substrates |
---|
1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH |
- |
1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin |
- |
1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 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 | 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 | 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 |
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 | 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 | 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 |