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Information on EC 1.5.8.1 - dimethylamine dehydrogenase
for references in articles please use BRENDA:EC1.5.8.1
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EC Tree 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
IUBMB Comments
Contains FAD and a [4Fe-4S] cluster.
The enzyme appears in viruses and cellular organisms
- 1.5.8.1
- trimethylamine
- hyphomicrobium
- flavin
- dehydrogenases
-
prosthetic
- ammonia
- mononucleotide
- demethylase
- formaldehyde
- histamine
-
6-s-cysteinyl
- strands
- methylophilus
- n-oxide
- simplex
- methylotrophus
-
nocardioides
-
cation-pi
Reaction Schemes
showSynonyms
dimethylamine dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
-
-
EC 1.5.99.10
-
-
formerly
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transfer flavoprotein
dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transfer flavoprotein
-
-
-
-
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
-
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
dimethylamine:electron-transferring flavoprotein oxidoreductase
Contains FAD and a [4Fe-4S] cluster.
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CAS REGISTRY NUMBER
COMMENTARY
172522-63-3
dehydrogenase, dimethylamine (Hyphomicrobium strain X clone pUHA65/pUHB49 gene dmd precursor)
172522-64-4
dehydrogenase, dimethylamine (Hyphomicrobium strain X clone pUHA65/pUHB49 gene dmd)
68247-64-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylamine + H2O + 2,6-dichlorophenolindophenol
methylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
dimethylamine + H2O + phenazine methosulfate
methylamine + formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
r
N,N,N,N-tetramethyl-o-phenylenediamine + H2O + electron-transfer flavoprotein
?
-
Substrates: -
Products: -
Products: -
r
diethylamine + H2O + acceptor
ethylamine + acetaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
diethylamine + H2O + acceptor
ethylamine + acetaldehyde + reduced acceptor
-
Substrates: at 78.3% of the activity with dimethylamine
Products: -
Products: -
?
dimethylamine + H2O + 2,6-dichlorophenolindophenol
methylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + 2,6-dichlorophenolindophenol
methylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + acceptor
methylamine + formaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
dimethylamine + H2O + acceptor
methylamine + formaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: reverse reaction is catalyzed only under anaerobic growth conditions
Products: -
Products: -
?
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: reverse reaction is catalyzed only under anaerobic growth conditions
Products: -
Products: -
?
ethylpropylamine + H2O + acceptor
?
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
ethylpropylamine + H2O + acceptor
?
-
Substrates: at 6.8% of the activity with dimethylamine
Products: -
Products: -
?
methylethanolamine + H2O + acceptor
?
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
methylethanolamine + H2O + acceptor
?
-
Substrates: at 54.2% of the activity with dimethylamine
Products: -
Products: -
?
methylethylamine + H2O + acceptor
ethylamine + formaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
methylethylamine + H2O + acceptor
ethylamine + formaldehyde + reduced acceptor
-
Substrates: at 92.1% of the activity with dimethylamine
Products: -
Products: -
?
methylethylamine + H2O + acceptor
ethylamine + formaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
methylethylamine + H2O + acceptor
ethylamine + formaldehyde + reduced acceptor
-
Substrates: at 92.1% of the activity with dimethylamine
Products: -
Products: -
?
methylpropylamine + H2O + acceptor
propylamine + formaldehyde + reduced acceptor
-
Substrates: acceptor: phenazine methosulfate, phenazine ethosulfate, methylene blue, N,N,N,N-tetramethyl-o-phenylenediamine
Products: -
Products: -
?
methylpropylamine + H2O + acceptor
propylamine + formaldehyde + reduced acceptor
-
Substrates: at 12.9% of the activity with dimethylamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with cytochrome c
Products: -
Products: -
?
additional information
?
-
-
Substrates: cytochrome cCO is not reduced directly by the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with primary and tertiary amines and quarternary ammonium salts
Products: -
Products: -
?
additional information
?
-
-
Substrates: when Hyphomicrobium X grows anaerobically on dimethylamine as sole carbon source with nitrate as terminal electron acceptor, the organism gets its energy from the oxidation of the amine substrate by dimethylamine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with cytochrome c
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with primary and tertiary amines and quarternary ammonium salts
Products: -
Products: -
?
additional information
?
-
-
Substrates: cytochrome cCO is not reduced directly by the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: when Hyphomicrobium X grows anaerobically on dimethylamine as sole carbon source with nitrate as terminal electron acceptor, the organism gets its energy from the oxidation of the amine substrate by dimethylamine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: anaerobic and aerobic metabolism of ethylamines, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: anaerobic and aerobic metabolism of ethylamines, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + electron-transfer flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: reverse reaction is catalyzed only under anaerobic growth conditions
Products: -
Products: -
?
dimethylamine + H2O + electron-transferring flavoprotein
methylamine + formaldehyde + reduced electron-transferring flavoprotein
-
Substrates: reverse reaction is catalyzed only under anaerobic growth conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: when Hyphomicrobium X grows anaerobically on dimethylamine as sole carbon source with nitrate as terminal electron acceptor, the organism gets its energy from the oxidation of the amine substrate by dimethylamine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: when Hyphomicrobium X grows anaerobically on dimethylamine as sole carbon source with nitrate as terminal electron acceptor, the organism gets its energy from the oxidation of the amine substrate by dimethylamine dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: anaerobic and aerobic metabolism of ethylamines, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: anaerobic and aerobic metabolism of ethylamines, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-S-cysteinyl-FMN
-
the flavin component accepts two electrons from the substrate
6-S-cysteinyl-FMN
-
each subunit contains a covalently bound 6-S-cysteinyl-FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
contains a [4Fe-4S]cluster that provides an output of single electrons to a flavoprotein which functions as a one-electron acceptor
Iron
-
the enzyme as a possible model for electron transfer in iron-sulfur flavoproteins
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenazine methosulfate
-
serves as electron acceptor, maximal activity at 2.4 mM. Above 2.4 mM inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
no activity in cells grown on tetradecyltrimethylammonium bromide
brenda
additional information
-
no activity in cells grown on tetradecyltrimethylammonium bromide
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2R5F9S5_9PROT
730
0
81457
TrEMBL
-
A0A841BPI2_9ACTN
697
0
76662
TrEMBL
-
F7ZGR4_ROSLO
Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149)
689
0
76461
TrEMBL
-
A0A0P0RMC1_9BURK
730
0
81328
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
-
x * 70000-80000, SDS-PAGE, disc PAGE in presence of 8 M urea, after carboxymethylation
?
-
x * 70000-80000, SDS-PAGE, disc PAGE in presence of 8 M urea, after carboxymethylation
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
-
brenda
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
-
brenda
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
brenda
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.
brenda
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
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.8.1)
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