ENZYME entry: EC 1.5.8.2
| Accepted Name |
|---|
| Trimethylamine dehydrogenase.
|
| Alternative Name(s) |
|---|
| TMADh. |
| Reaction catalysed |
|---|
| Trimethylamine + H(2)O + electron-transferring flavoprotein <=> dimethylamine + formaldehyde + reduced electron-transferring flavoprotein |
| Cofactor(s) |
|---|
| FMN; Iron-sulfur.
|
| Comment(s) |
|---|
- A number of alkyl-substituted derivatives of trimethylamine can also
act as electron donors.
- Phenazine methosulfate and 2,6-dichloroindophenol can act as electron
acceptors.
- Formerly EC 1.5.99.7.
|
| Cross-references |
|---|
| BRENDA | 1.5.8.2 |
| EC2PDB | 1.5.8.2 |
| ExplorEnz | 1.5.8.2 |
| PRIAM enzyme-specific profiles | 1.5.8.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.5.8.2 |
| IUBMB Enzyme Nomenclature | 1.5.8.2 |
| IntEnz | 1.5.8.2 |
| MEDLINE | Find literature relating to 1.5.8.2 |
| MetaCyc | 1.5.8.2 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.5.8.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-