EC 1.5.8.2 - Trimethylamine dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.5.8.2

Names

Accepted name:
trimethylamine dehydrogenase
Systematic name:
trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating)

Reaction

Cofactors

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050470
CAS Registry Number: 39307-09-0
UniProtKB/Swiss-Prot:

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]