| EC |
1.5.8.2 |
| Accepted name: |
trimethylamine dehydrogenase |
| Reaction: |
trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein |
| Systematic name: |
trimethylamine:electron-transfer flavoprotein oxidoreductase (demethylating) |
| Comments: |
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. Contains FAD and a [4Fe-4S] cluster. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 39307-09-0 |
| References: |
| 1. |
Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P–10P. [PMID: 5116569] |
| 2. |
Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361–369. [PMID: 204297] |
| 3. |
Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958–23965. [DOI] [PMID: 7592591] |
| 4. |
Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457–8465. [DOI] [PMID: 11756429] |
| 5. |
Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145–181. [PMID: 11192721] |
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| [EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2] |
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