EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   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 |
Homo sapiens |
? |
- |
- |
| 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. 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 |
? |
- |
- |
| 1.8.98.2 | more |
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 |
? |
- |
- |
| 1.8.98.2 | more |
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 |
? |
- |
- |
| 1.8.98.2 | more |
assay conditions optimization, overview |
Arabidopsis thaliana Columbia |
? |
- |
? |
| 1.8.98.2 | overoxidized human peroxiredoxin V + reduced thioredoxin |
Arabidopsis enzyme is able to reduce overoxidized human Prx V |
Arabidopsis thaliana |
? + oxidized thioredoxin |
- |
? |
| 1.8.98.2 | peroxiredoxin IIF-(S-hydroxy-S-oxocysteine) + ATP + GSH |
- |
Pisum sativum |
peroxiredoxin IIF-(S-hydroxycysteine) + ADP + phosphate + GSSG |
- |
? |
| 1.8.98.2 | peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH |
- |
Mus musculus |
peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG |
- |
? |
| 1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT |
- |
Arabidopsis thaliana |
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide |
- |
? |
| 1.8.98.2 | peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT |
- |
Homo sapiens |
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide |
- |
? |
