| Entry |
|
| Name |
sulfiredoxin;
Srx1;
sulphiredoxin;
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
|
| Class |
Oxidoreductases;
Acting on a sulfur group of donors;
With other, known, acceptors
 |
| Sysname |
peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
|
| Reaction(IUBMB) |
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
|
| Substrate |
peroxiredoxin-(S-hydroxy-S-oxocysteine);
ATP [CPD: C00002];
RSH [CPD: C01336]
|
| Product |
peroxiredoxin-(S-hydroxycysteine);
ADP [CPD: C00008];
phosphate [CPD: C00009];
R-S-S-R
|
| Comment |
In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. Apparently the reductase first catalyses the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes. Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.
|
| Orthology |
|
| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | SHR: | | OAA: | | GGA: | | TGU: | | DRE: | | TRU: | | OLA: | | BFO: | | CIN: | | SPU: | | DME: | | DPO: | | DAN: | | DER: | | DPE: | | DSE: | | DSI: | | DWI: | | DYA: | | DGR: | | DMO: | | DVI: | | AAG: | | CQU: | | NVI: | | TCA: | | API: | | PHU: | | ISC: | | NVE: | | CRE: | | VCN: | | SCE: | | AGO: | | ERC: | | KLA: | | LTH: | | PPA: | | VPO: | | ZRO: | | CGR: | | NCS: | | NDI: | | TPF: | | TBL: | | TDL: | | KAF: | | DHA: | | PIC: | | PGU: | | LEL: | | CAL: | | CTP: | | CDU: | | COT: | | YLI: | | CLU: | | SPO: | | CNB: | | NGR: | | DPP: | | » show all
 |
| Reference |
|
| Authors |
Biteau B, Labarre J, Toledano MB. |
| Title |
ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. |
| Journal |
Nature. 425 (2003) 980-4. |
| Organism |
Saccharomyces cerevisiae [GN: sce] |
| Reference |
|
| Authors |
Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. |
| Title |
Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. |
| Journal |
J. Biol. Chem. 279 (2004) 50994-1001. |
| Organism |
Homo sapiens [GN: hsa], Mus musculus [GN: mmu], Rattus norvegicus [GN: rno] |
| Reference |
|
| Authors |
Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG. |
| Title |
Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. |
| Journal |
J. Biol. Chem. 280 (2005) 3125-8. |
| Organism |
Homo sapiens [GN: hsa], Rattus norvegicus [GN: rno] |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 710319-61-2 |