1.5.8.1: dimethylamine dehydrogenase

This is an abbreviated version!
For detailed information about dimethylamine dehydrogenase, go to the full flat file.

Word Map on EC 1.5.8.1

Reaction

Dimethylamine
+
H2O
+
electron-transfer flavoprotein
=
methylamine
+
formaldehyde
+
reduced electron-transfer flavoprotein

Synonyms

dehydrogenase, dimethylamine, dehydrogenase, dimethylamine (Hyphomicrobium strain X clone pUHA65/pUHB49 gene dmd precursor), dehydrogenase, dimethylamine (Hyphomicrobium strain X clone pUHA65/pUHB49 gene dmd), dimethylamine monooxygenase, DMADH

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.8 With a flavin or flavoprotein as acceptor
                1.5.8.1 dimethylamine dehydrogenase

Reference

Reference on EC 1.5.8.1 - dimethylamine dehydrogenase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eur. J. Biochem.
232
264-271
1995
Hyphomicrobium sp., Hyphomicrobium sp. X
Manually annotated by BRENDA team
Steenkamp, D.J.; Beinert, H.
Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 2. Kinetic studies on the intramolecular electron transfer in trimethylamine and dimethylamine dehydrogenase
Biochem. J.
207
241-252
1982
Hyphomicrobium sp., Hyphomicrobium sp. X
Manually annotated by BRENDA team
Kasprzak, A.A.; Papas, E.J.; Steenkamp, D.J.
Identity of the subunits and the stoicheiometry of prosthetic groups in trimethylamine dehydrogenase and dimethylamine dehydrogenase
Biochem. J.
211
535-541
1983
Hyphomicrobium sp., Hyphomicrobium sp. X
Manually annotated by BRENDA team
Meiberg, J.B.M.; Harder, W.
Dimethylamine dehydrogenase from Hyphomicrobium X: purification and some properties of a new enzyme that oxidizes secondary amines
J. Gen. Microbiol.
115
49-58
1979
Hyphomicrobium sp., Hyphomicrobium sp. X
-
Manually annotated by BRENDA team
Steenkamp, D.J.
Identification of the prosthetic groups of dimethylamine dehydrogenase from Hyphomicrobium X
Biochem. Biophys. Res. Commun.
88
244-250
1979
Hyphomicrobium sp., Hyphomicrobium sp. X
Manually annotated by BRENDA team
Large, P.J.; Meiberg, J.B.M.; Harder, W.
Cytochrome cCO is not a primary electron acceptor for the amine dehydrogenases of Hyphomicrobium X
FEMS Microbiol. Lett.
5
281-286
1979
Hyphomicrobium sp., Hyphomicrobium sp. X
-
Manually annotated by BRENDA team
Beinert, H.; Shaw, R.W.; Steenkamp, D.J.; Singer, T.P.; Stevenson, R.; Dunham, W.R.; Sands, R.H.
Dehydrogenases of methylotrophic bacteria as possible models for electron transfer in iron-sulfur flavoproteins
Dev. Biochem.
21
727-735
1982
Hyphomicrobium sp., Hyphomicrobium sp. X
-
Manually annotated by BRENDA team
Kasprzak, A.A.; Steenkamp, D.J.
Localization of the major dehydrogenases in two methylotrophs by radiochemical labeling
J. Bacteriol.
156
348-353
1983
Hyphomicrobium sp., Hyphomicrobium sp. X
Manually annotated by BRENDA team
Kim, S.G.; Bae, H.S.; Lee, S.T.
A novel denitrifying bacterial isolate that degrades trimethylamine both aerobically and anaerobically via two different pathways
Arch. Microbiol.
176
271-277
2001
Paracoccus sp.
Manually annotated by BRENDA team
Liffourrena, A.S.; Salvano, M.A.; Lucchesi, G.I.
Pseudomonas putida A ATCC 12633 oxidizes trimethylamine aerobically via two different pathways
Arch. Microbiol.
192
471-476
2010
Pseudomonas putida, Pseudomonas putida ATCC 12633
Manually annotated by BRENDA team