| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.4 With a disulfide as acceptor |
| ID: | 1.8.4.13 |
|---|---|
| Description: | L-methionine (S)-S-oxide reductase. |
| Alternative Name: |
Methyl sulfoxide reductase I and II. Methionine-S-oxide reductase. Methionine sulfoxide reductase. FSMsr. Free-methionine (S)-S-oxide reductase. Acetylmethionine sulfoxide reductase. |
| Cath: | 3.30.450.40; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.8.4.13 |
| BRENDA Enzyme Link: | BRENDA 1.8.4.13 |
| KEGG Enzyme Link: | KEGG1.8.4.13 |
| BioCyc Enzyme Link: | BioCyc 1.8.4.13 |
| ExPASy Enzyme Link: | ExPASy1.8.4.13 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.4.13 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.4.13 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.4.13 |
| IntEnz Enzyme Link: | IntEnz 1.8.4.13 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.4.13 |
| RHEA:19993 | [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide |
| RULE(radius=1) | [*:1]-[S;H0;+0:2]-[*:3].[*:4]-[S;H0;+0:5]-[S;H0;+0:6]-[*:7].[OH2;+0:8]>>[*:1]-[S;H0;+0:2](-[*:3])=[O;H0;+0:8].[*:7]-[SH;+0:6].[*:4]-[SH;+0:5] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The purification of methionine sulfoxide reductase from Escherichia coli. | Ejiri SI, Weissbach H, Brot N | 1980 Mar 1 | 6999943 |
| Reduction of methionine sulfoxide to methionine by Escherichia coli. | Ejiri SI, Weissbach H, Brot N | 1979 Jul | 37234 |
| Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. | Weissbach H, Resnick L, Brot N | 2005 Jan 17 | 15680228 |