IUBMB Enzyme Nomenclature


Accepted name: trimethylamine dehydrogenase

Reaction: trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

Systematic name: trimethylamine:electron-transferring 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, KEGG, Metacyc, PDB, CAS registry number: 39307-09-0


1. Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P-10P.

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. [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. [PMID: 11756429]

5. Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145-181. [PMID: 11192721]

[EC created 1976 as EC, transferred 2002 to EC]

Return to EC 1.5.8 home page
Return to EC 1.5 home page
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page