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Dimethylamine dehydrogenase

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dimethylamine dehydrogenase
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EC no.1.5.8.1
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In enzymology, a dimethylamine dehydrogenase (EC 1.5.8.1) is an enzyme that catalyzes the chemical reaction

dimethylamine + H2O + electron-transferring flavoprotein {\displaystyle \rightleftharpoons } methylamine + formaldehyde + reduced electron-transferring flavoprotein

The 3 substrates of this enzyme are dimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are methylamine, 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 dimethylamine:electron-transferring flavoprotein oxidoreductase. This enzyme participates in methane metabolism. It employs one cofactor, FMN.

References

  • Yang CC, Packman LC, Scrutton NS (1995). "The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition". Eur. J. Biochem. 232 (1): 264–71. doi:10.1111/j.1432-1033.1995.tb20808.x. PMID 7556160.
Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor
1.5.3: oxygen acceptor
1.5.5: quinone acceptor
1.5.99
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