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Information on EC 1.14.13.238 - dimethylamine monooxygenase
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1.14.13.238 dimethylamine monooxygenaseIUBMB Comments
The enzyme, characterized from several bacterial species, is involved in a pathway for the degradation of methylated amines. It is composed of three subunits, one of which is a ferredoxin, and contains heme iron and an FMN cofactor.
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Word Map
- 1.14.13.238
- heme
-
prosthetic
-
axial
-
ferric
- trimethylamine
- flavin
- protoporphyrin
- aminovorans
- myoglobin
-
heme-containing
-
myoglobin-like
- oxygenases
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
secondary amine monooxygenase, secondary amine mono-oxygenase, dmmabc, dimethylamine mono-oxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimethylamine mono-oxygenase
dmmABC
dmmABC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
dimethylamine,NADPH:oxygen oxidoreductase (formaldehyde-forming)
The enzyme, characterized from several bacterial species, is involved in a pathway for the degradation of methylated amines. It is composed of three subunits, one of which is a ferredoxin, and contains heme iron and an FMN cofactor.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dipropylamine + NADH + H+ + O2
propylamine + acetaldehyde + NAD+ + H2O
-
-
-
-
?
ethyl-n-propylamine + NADH + H+ + O2
?
-
22% activity compared to dimethylamine
-
-
?
ethylamine + NADH + H+ + O2
?
-
65% activity compared to dimethylamine
-
-
?
methyl-n-propylamine + NADH + H+ + O2
?
-
87% activity compared to dimethylamine
-
-
?
n-butylmethylamine + NADH + H+ + O2
?
-
54% activity compared to dimethylamine
-
-
?
n-methylethanolamine + NADH + H+ + O2
?
-
19% activity compared to dimethylamine
-
-
?
dibutylamine + NADH + H+ + O2
butylamine + acetaldehyde + NAD+ + H2O
-
-
-
-
?
dibutylamine + NADH + H+ + O2
butylamine + acetaldehyde + NAD+ + H2O
-
-
-
-
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
40% activity compared to dimethylamine
-
-
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
-
-
-
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
-
-
-
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
100% activity
-
-
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
-
-
-
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
-
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
good substrate
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
additional information
?
-
-
no activity with methylamine, ethylamine, n-propylamine, ethanolamine, aniline, 1,2-diaminopropane, 1,3-diaminopropane, di-isopropylamine, di-n-propylamine, di-isobutylamine, di-n-butylamine, diethanolamine, methyl-n-octylamine, N-methylaniline, benzylmethylamine, putrescine, spermidine, piperidine, sarcosine, N-methylglutamate, noradrenaline, trimethylamine, triethylamine, N,N-dimethylaniline, tetramethylammonium chloride, and tetraethylammonium chloride
-
-
?
additional information
?
-
-
no activity with methylamine, methanol or formaldehyde. The partially purified enzyme shows no significant activity with primary, tertiary and quaternary amines, nor with sarcosine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
NADH can replace NADPH as electron donor and is slightly (1-2fold) more active
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dimethylamine
-
the enzyme is inhibited by dimethylamine concentrations above 1 mM
Dimethylamine
-
substrate inhibition at concentrations higher than 1 mM
additional information
-
dimethylamine oxidation is not inhibited by semicarbazide hydrochloride
-
additional information
-
not inhibited by aminoacetonitrile, metyrapone, iodoacetamide, and N-ethylmaleimide
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000833
diethylmethylamine
-
with NADH as cosubstrate, at pH 7.0 and 25°C
0.004
dimethylethylamine
-
with NADH as cosubstrate, at pH 7.0 and 25°C
0.654
Methylethanolamine
-
with NADH as cosubstrate, at pH 7.0 and 25°C
0.278
methylisopropylamine
-
with NADH as cosubstrate, at pH 7.0 and 25°C
0.0665
Dimethylamine
-
pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
Sepharose 2B column chromatography and 4-aminobutyl-Sepharose 4B column chromatography
-
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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
Eady, R.; Large, P.
Bacterial oxidation of dimethylamine, a new mono-oxygenase reaction
Biochem. J.
111
37P-38P
1969
Aminobacter aminovorans
brenda
Eady, R.; Jarman, T.; Large, P.
Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein
Biochem. J.
125
449-459
1971
Aminobacter aminovorans
brenda
Lidbury, I.; Mausz, M.A.; Scanlan, D.J.; Chen, Y.
Identification of dimethylamine monooxygenase in marine bacteria reveals a metabolic bottleneck in the methylated amine degradation pathway
ISME J.
11
1592-1601
2017
Ruegeria pomeroyi
brenda
Hawkins, B.; Dawson, J.; Hawkins, B.; Dawson, J.
Intrasubstituent isotope effect studies of oxidative N-demethylations catalyzed by secondary amine monooxygenase. Comparison to cytochrome P-450
J. Am. Chem. Soc.
114
3547-3549
1992
Aminobacter aminovorans
-
brenda
Alberta, J.; Andersson, L.; Dawson, J.
Spectroscopic characterization of secondary amine mono-oxygenase. Comparison to cytochrome P-450 and myoglobin
J. Biol. Chem.
264
20467-20473
1989
Aminobacter aminovorans
brenda
Green, J.; Large, P.
Subcellular localization and properties of partially purified dimethylamine and trimethylamine mono-oxygenase activities in Candida utilis
J. Gen. Microbiol.
130
2577-2588
1984
Cyberlindnera jadinii, Cyberlindnera jadinii WY-3
brenda
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Release 2023.1 (January 2023)
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