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Information on EC 1.14.13.238 - dimethylamine monooxygenase
for references in articles please use BRENDA:EC1.14.13.238
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.238 dimethylamine monooxygenase
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.13.238
- heme
-
prosthetic
-
axial
-
ferric
- trimethylamine
- flavin
- protoporphyrin
- aminovorans
- myoglobin
-
heme-containing
-
myoglobin-like
- oxygenases
showSynonyms
secondary amine monooxygenase, secondary amine mono-oxygenase, dmmabc, dimethylamine mono-oxygenase, more
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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
MetaCyc
trimethylamine degradation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dipropylamine + NADH + H+ + O2
propylamine + acetaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
ethyl-n-propylamine + NADH + H+ + O2
?
-
Substrates: 22% activity compared to dimethylamine
Products: -
Products: -
?
ethylamine + NADH + H+ + O2
?
-
Substrates: 65% activity compared to dimethylamine
Products: -
Products: -
?
methyl-n-propylamine + NADH + H+ + O2
?
-
Substrates: 87% activity compared to dimethylamine
Products: -
Products: -
?
n-butylmethylamine + NADH + H+ + O2
?
-
Substrates: 54% activity compared to dimethylamine
Products: -
Products: -
?
n-methylethanolamine + NADH + H+ + O2
?
-
Substrates: 19% activity compared to dimethylamine
Products: -
Products: -
?
dibutylamine + NADH + H+ + O2
butylamine + acetaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
dibutylamine + NADH + H+ + O2
butylamine + acetaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
Substrates: 40% activity compared to dimethylamine
Products: -
Products: -
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
diethylamine + NADH + H+ + O2
ethylamine + acetaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
diethylmethylamine + NADH + H+ + O2
?
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
Substrates: 100% activity
Products: -
Products: -
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADH + H+ + O2
methylamine + formaldehyde + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: good substrate
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with methylamine, methanol or formaldehyde. The partially purified enzyme shows no significant activity with primary, tertiary and quaternary amines, nor with sarcosine
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 + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
dimethylamine + NADPH + H+ + O2
methylamine + formaldehyde + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
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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
Highest Expressing Human Cell Lines
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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
EXTERNAL LINKS (specific for EC-Number 1.14.13.238)
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Release 2023.1 (January 2023)
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