EC number:1.7.2.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.7 Acting on other nitrogenous compounds as donors |
| 1.7.2 With a cytochrome as acceptor |
| ID: | 1.7.2.3 |
|---|---|
| Description: | Trimethylamine-N-oxide reductase. |
| Alternative Name: |
Trimethylamine-N-oxide reductase (cytochrome c). TOR. TMAO reductase. |
| Cath: | 3.40.50.740; 3.90.55.10; 2.40.40.20; 3.40.228.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.7.2.3 |
| BRENDA Enzyme Link: | BRENDA 1.7.2.3 |
| KEGG Enzyme Link: | KEGG1.7.2.3 |
| BioCyc Enzyme Link: | BioCyc 1.7.2.3 |
| ExPASy Enzyme Link: | ExPASy1.7.2.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.7.2.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.7.2.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.7.2.3 |
| IntEnz Enzyme Link: | IntEnz 1.7.2.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.7.2.3 |
| RHEA:24236 | 2 [Fe(III)cytochrome c] + H2O + trimethylamine = 2 [Fe(II)cytochrome c] + 3 H(+) + trimethylamine N-oxide |
| RULE(radius=1) | [*:1]-[N;H0;+0:2](-[*:3])-[*:4].[Fe+3;H0:5].[Fe+3;H0:6].[OH2;+0:7]>>[*:1]-[N+;H0:2](-[*:3])(-[*:4])-[OH;+0:7].[Fe+2;H0:5].[Fe+2;H0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution. | Czjzek M, Dos Santos JP, Pommier J, Giordano G, Méjean V, Haser R | 1998 Nov 27 | 9813128 |
| Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus. | Knäblein J, Dobbek H, Ehlert S, Schneider F | 1997 Mar-Apr | 9165084 |
| Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans. | Arata H, Shimizu M, Takamiya K | 1992 Oct | 1337081 |
| Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. | Gon S, Giudici-Orticoni MT, Méjean V, Iobbi-Nivol C | 2001 Apr 13 | 11056172 |
| RHEA:22024 | 2 H(+) + NADH + trimethylamine N-oxide = H2O + NAD(+) + trimethylamine |
| RULE(radius=1) | [*:1]-[N+;H0:2](-[*:3])(-[*:4])-[OH;+0:5].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[C;H0;+0:9](-[*:10])-[CH2;+0:11]-[CH;+0:12]=[CH;+0:13]-1.[H+;H0:14].[H+;H0:15]>>[*:1]-[N;H0;+0:2](-[*:3])-[*:4].[*:6]-[n+;H0:7]1:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:[cH;+0:12]:[cH;+0:13]:1.[OH2;+0:5] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Intracellular localization and properties of trimethylamine-N-oxide reductase in Vibrio parahaemolyticus. | Unemoto T, Hayashi M, Miyaki K, Hayashi M | 1965 Nov 22 | 4286289 |