IntEnz

EC 1.5.8.2 - Trimethylamine dehydrogenase

IntEnz Enzyme Nomenclature
EC 1.5.8.2

Names

Reaction

• trimethylamine + H2O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

Cofactors

• iron-sulfur
• FMN

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

References

1. Colby, J. and Zatman, L.J.
   The purification and properties of a bacterial trimethylamine dehydrogenase.
   Biochem. J. 121 : 9P-10P (1971).
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 : 361-369 (1978). [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 : 23958-23965 (1995). [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 : 8457-8465 (2002). [PMID: 11756429]
5. Scrutton, N.S. and Sutcliffe, M.J.
   Trimethylamine dehydrogenase and electron transferring flavoprotein.
   Subcell. Biochem. 35 : 145-181 (2000). [PMID: 11192721]

[EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2]