Trimethylamine dehydrogenase

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trimethylamine dehydrogenase

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

trimethylamine + H₂O + electron-transferring flavoprotein

\rightleftharpoons

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.

v t e Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase
1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase
1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase
1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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