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Dimethylamine dehydrogenase

From Wikipedia, the free encyclopedia
dimethylamine dehydrogenase
Identifiers
EC no.1.5.8.1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a dimethylamine dehydrogenase (EC 1.5.8.1) is an enzyme that catalyzes the chemical reaction

dimethylamine + H2O + electron-transferring flavoprotein 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

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  • 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.