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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.8.1 82523
-
 x * 82523, calculation from nucleotide sequence Hyphomicrobium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.5.8.1 Hyphomicrobium sp.
-
 X
-
1.5.8.1 Hyphomicrobium sp. X
-
 X
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.8.1 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

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