EC number:1.8.98.2
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.98 With other, known, physiological acceptors |
| ID: | 1.8.98.2 |
|---|---|
| Description: | Sulfiredoxin. |
| Alternative Name: |
Peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase. |
| Cath: | 3.90.1530.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.98.2 |
| BRENDA Enzyme Link: | BRENDA 1.8.98.2 |
| KEGG Enzyme Link: | KEGG1.8.98.2 |
| BioCyc Enzyme Link: | BioCyc 1.8.98.2 |
| ExPASy Enzyme Link: | ExPASy1.8.98.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.98.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.98.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.98.2 |
| IntEnz Enzyme Link: | IntEnz 1.8.98.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.98.2 |
| RHEA:17545 | [peroxiredoxin]-S-hydroxy-S-oxy-L-cysteine + [protein]-dithiol + ATP = [peroxiredoxin]-S-hydroxy-L-cysteine + [protein]-disulfide + ADP + H(+) + phosphate |
| RULE(radius=1) | [*:1]-[S;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[SH;+0:6].[*:7]-[SH;+0:8].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[O;H0;+0:13]-[*:14]>>[*:14]-[OH;+0:13].[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[S;H0;+0:6]-[S;H0;+0:8]-[*:7].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[OH;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The University Association for Emergency Medical Services. History and perspective. | Rutherford RB | 1973 Dec | 4586471 |
| Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin. | Iglesias-Baena I, Barranco-Medina S, Lázaro-Payo A, López-Jaramillo FJ, Sevilla F, Lázaro JJ | 2010 Mar | 20176891 |
| Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. | Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG | 2005 Feb 4 | 15590625 |
| Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. | Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG | 2004 Dec 3 | 15448164 |