IntEnz

EC 1.5.8.2 - Trimethylamine dehydrogenase

IntEnz Enzyme Nomenclature
EC 1.5.8.2

Names

Reaction

• 11867 [IUBMB]
  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  oxidized [electron-transfer flavoprotein]

  oxidized [electron-transfer flavoprotein]

  GENERIC:10685

  Is ROOT: no
  ROOT compound: GENERIC:10684

  Number of residues: 1

  FAD FAD Name origin: UniProt - CHECKED (C) CHEBI:57692 Formula: C27H30N9O15P2 Charge: -3 Position: undefined ChEBI compound status: CHECKED (C)

  +

  trimethylamine

  trimethylamine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58389

  Formula: C3H10N
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  <=>

  dimethylamine

  dimethylamine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58040

  Formula: C2H8N
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  formaldehyde

  formaldehyde

  Name origin: UniProt - CHECKED (C)

  CHEBI:16842

  Formula: CH2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  reduced [electron-transfer flavoprotein]

  reduced [electron-transfer flavoprotein]

  GENERIC:10686

  Is ROOT: no
  ROOT compound: GENERIC:10684

  Number of residues: 1

  FADH2 FADH2 Name origin: UniProt - CHECKED (C) CHEBI:58307 Formula: C27H33N9O15P2 Charge: -2 Position: undefined ChEBI compound status: CHECKED (C)

Cofactors

• FMN
• iron-sulfur

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]