Literature summary for 1.5.8.1 extracted from

Yang, C.C.; Packman, L.C.; Scrutton, N.S.
The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition (1995), Eur. J. Biochem., 232, 264-271.

Search for more literature for 1.5.8.1

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Hyphomicrobium sp.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
82523	-	x * 82523, calculation from nucleotide sequence	Hyphomicrobium sp.

Organism

Organism	UniProt	Comment	Textmining
Hyphomicrobium sp.	-	X	-
Hyphomicrobium sp. X	-	X	-

Reaction

Reaction	Comment	Organism	Reaction ID
dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transfer flavoprotein	the enzyme functions as a 2:1e- transformase. The flavin component accepts two electrons from the substrate while the [4Fe-4S] cluster provides an output of single electrons to a flavoprotein which functions as a one-electron acceptor	Hyphomicrobium sp.	a

Subunits

Subunits	Comment	Organism
?	x * 82523, calculation from nucleotide sequence	Hyphomicrobium sp.

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)