EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.4 With a disulfide as acceptor |
ID: | 1.8.4.11 |
---|---|
Description: | Peptide-methionine (S)-S-oxide reductase. |
Alternative Name: |
Peptide methionine sulfoxide reductase. Peptide Met(O) reductase. Methionine sulphoxide reductase A. Methionine sulfoxide reductase A. Methionine sulfoxide reductase. Methionine S-oxide reductase (S-form oxidizing). Methionine S-oxide reductase. |
Cath: | 3.30.1060.10; 2.170.150.20; 3.40.30.10; |
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 1.8.4.11 |
BRENDA Enzyme Link: | BRENDA 1.8.4.11 |
KEGG Enzyme Link: | KEGG1.8.4.11 |
BioCyc Enzyme Link: | BioCyc 1.8.4.11 |
ExPASy Enzyme Link: | ExPASy1.8.4.11 |
EC2PDB Enzyme Link: | EC2PDB 1.8.4.11 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.4.11 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.4.11 |
IntEnz Enzyme Link: | IntEnz 1.8.4.11 |
MEDLINE Enzyme Link: | MEDLINE 1.8.4.11 |
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 |
RHEA:14217 | [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein] |
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 three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions. | Kauffmann B, Aubry A, Favier F | 2005 Jan 17 | 15680233 |
The enzymology and biochemistry of methionine sulfoxide reductases. | Boschi-Muller S, Olry A, Antoine M, Branlant G | 2005 Jan 17 | 15680231 |
Methionine sulfoxide reductases in prokaryotes. | Ezraty B, Aussel L, Barras F | 2005 Jan 17 | 15680230 |
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. | Weissbach H, Resnick L, Brot N | 2005 Jan 17 | 15680228 |
Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. | Taylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ | 2003 Jul | 12837786 |
Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis. | Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van Dorsselear A, Branlant G | 2002 Apr 5 | 11812798 |
Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. | Moskovitz J, Singh VK, Requena J, Wilkinson BJ, Jayaswal RK, Stadtman ER | 2002 Jan 11 | 11779133 |