Trimethylamine dehydrogenase

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trimethylamine dehydrogenase
Identifiers
EC no.1.5.8.2
CAS no.39307-09-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a trimethylamine dehydrogenase (EC 1.5.8.2) is an enzyme that catalyzes the chemical reaction

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

The 3 substrates of this enzyme are trimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are dimethylamine, formaldehyde, and reduced electron-transferring flavoprotein.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating). This enzyme participates in methane metabolism.

References

  • Colby J; Zatman LJ (1971). "The purification and properties of a bacterial trimethylamine dehydrogenase". Biochem. J. 121 (1): 9P–10P. PMC 1176516. PMID 5116569.
  • Steenkamp DJ, Singer TP (1978). "Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis". Biochem. J. 169 (2): 361–9. PMC 1184175. PMID 204297.
  • Huang L, Rohlfs RJ, Hille R (1995). "The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein". J. Biol. Chem. 270 (41): 23958–65. doi:10.1074/jbc.270.41.23958. PMID 7592591.
  • Jones M; Talfournier, F; Bobrov, A; Grossmann, JG; Vekshin, N; Sutcliffe, MJ; Scrutton, NS (2002). "Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein". J. Biol. Chem. 277 (10): 8457–65. doi:10.1074/jbc.M111105200. PMID 11756429.
  • Scrutton NS, Sutcliffe MJ (2000). "Trimethylamine dehydrogenase and electron transferring flavoprotein". Subcell. Biochem. 35: 145–81. doi:10.1007/0-306-46828-X_5. PMID 11192721.