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10-[(N,N-dimethylaminopentyl)]-2-(trifluoromethylphenothiazine) + NADPH + H+ + O2
?
-
functional substrate
-
-
?
3-dimethylaminopropan-1-ol + NADPH + H+ + O2
?
-
-
-
-
?
3-dimethylaminopropan-2-ol + NADPH + H+ + O2
?
-
-
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
cysteamine + NADPH + H+ + O2
?
-
-
-
-
?
danusertib + NADPH + H+ + O2
danusertib N-oxide + NADP+ + H2O
-
-
-
-
?
diethylmethylamine + NADPH + H+ + O2
?
-
-
-
-
?
dimethylaniline + NADPH + H+ + O2
?
-
-
-
-
?
dimethylsulfide + NADPH + H+ + O2
?
-
-
-
-
?
DMSO + NADPH + H+ + O2
?
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
ethyldimethylamine + NADPH + H+ + O2
?
-
-
-
-
?
methimazole + NADPH + H+ + O2
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
methyl 4-tolyl sulfide + NADPH + H+ + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADH + H+ + O2
N,N,N-trimethylamine N-oxide + NAD+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
N,N-dimethyl-2-chloroethylamine + NADPH + H+ + O2
?
-
-
-
-
?
N,N-dimethylamine + NADPH + H+ + O2
N,N-dimethylamine N-oxide + NADP+ + H2O
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylbutylamine + NADPH + H+ + O2
N,N-dimethylbutylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylethanolamine + NADPH + H+ + O2
?
-
-
-
-
?
N,N-dimethylethylenediamine + NADPH + H+ + O2
?
-
-
-
-
?
N,N-dimethylpropylenediamine + NADPH + H+ + O2
?
-
-
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
tozasertib + NADPH + H+ + O2
tozasertib N-oxide + NADP+ + H2O
-
-
-
-
?
triethylamine + NADPH + H+ + O2
?
-
-
-
-
?
tyramine + NADPH + H+ + O2
-
-
-
-
-
?
additional information
?
-
-
no activity with N-monomethylamine, glutathione, and cysteine
-
-
-
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2

5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
i.e. 5-dimethylaminopropylamino-8-hydroxytriazoloacridinone
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
i.e. 5-dimethylaminopropylamino-8-hydroxytriazoloacridinone
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2

5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2

benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
ethionamide + NADPH + H+ + O2

ethionamide S-oxide + NADP+ + H2O
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
-
-
-
?
methimazole + NADPH + H+ + O2

?
-
-
-
-
?
methimazole + NADPH + H+ + O2
?
-
-
-
-
?
methimazole + NADPH + H+ + O2

methimazole N-oxide + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2

N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
highest affinity substrate
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylamine + NADPH + H+ + O2

N,N-dimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylamine + NADPH + H+ + O2
N,N-dimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
sulindac sulfide + NADPH + H+ + O2

sulindac + NADP+ + H2O
-
the enzyme does not display saturability at concentrations through 1 mM of sulindac sulfide
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
-
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
the enzyme does not display saturability at concentrations through 1 mM of sulindac sulfide
-
-
?
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3-dimethylaminopropan-1-ol
-
inhibitory at concentrations above about 1 mM
3-dimethylaminopropan-2-ol
-
inhibitory at concentrations above about 1 mM
Cu2+
-
0.2 mM Cu2+ inhibits the enzyme strongly without any preincubation
diethylmethylamine
-
inhibitory at concentrations above about 1 mM
ethyldimethylamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethyl-2-chloroethylamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylethanolamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylethylenediamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylpropylenediamine
-
inhibitory at concentrations above about 1 mM
N-ethylmaleimide
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 1.0 mM N-ethylmaleimide inhibits the enzymatic activity approximately by 25%
p-chloromercuribenzoate
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 0.2 mM p-chloromercuribenzoate inhibits the enzymic activity approximately by 90%
triethylamine
-
inhibitory at concentrations above about 1 mM
Thiourea

-
-
Thiourea
thiourea reduces ethionamide oxygenation to ethionamide S-oxide by an average of 73.5% in liver and 76.9% in lung
additional information

-
the enzyme is not inhibited by CO, cyanide or SKF 525-A (2-diethylaminoethyl 2,2-diphenylvalerate hydrochloride), nor by chelating agents
-
additional information
-
10 mM EDTA, 1 mM potassium cyanide and 1 mM sodium azide do not inhibit the enzyme. Bubbling the enzyme solution with CO for 2 min at 0°C or including CO (CO:O2 ratio 1:1) during the tests has no effect on enzyme activity
-
additional information
-
enzyme reactions are not inhibited by gas phase containing up to 80% carbon monoxide/20% oxygen mixture
-
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0.1116
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO3, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.1624
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO3, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.0186 - 0.056
Benzydamine
3.139
cysteamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0357
dimethylaniline
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0103
Dimethylsulfide
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
3.575
DMSO
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.114 - 0.336
Ethionamide
0.0282 - 0.035
Methimazole
0.0003 - 0.0548
N,N,N-trimethylamine
0.0897
N,N-dimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
2
NADH
-
pH and temperature not specified in the publication
0.022 - 0.0693
sulindac sulfide
0.0186
Benzydamine

-
in in 0.1 M tricine buffer, pH 7.4, at 37°C
0.0426
Benzydamine
-
in in 0.1 M tricine buffer, pH 7.4, at 37°C
0.045
Benzydamine
-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.056
Benzydamine
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.114
Ethionamide

isozyme FMO3, at pH 9.5 and 37°C
0.336
Ethionamide
-
isozyme FMO3, at pH 9.5 and 37°C
0.0282
Methimazole

-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0285
Methimazole
-
mutant enzyme, at pH and 37°C
0.03
Methimazole
-
native enzyme, at pH and 37°C
0.03
Methimazole
isoform FMO3, at pH 8.4, temperature not specified in the publication
0.033
Methimazole
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.035
Methimazole
-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0003
N,N,N-trimethylamine

-
in potassium diphosphate buffer (pH 7.7), at 14°C
0.0094
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.013 - 0.0548
N,N,N-trimethylamine
-
the Km for isoform FMO3 determined in human liver microsomes ranges from 0.013.to 0.0548 mM, at pH 7.4 and 22°C
0.0208
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0216
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0275
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.028
N,N,N-trimethylamine
-
recombinant isoform FMO3, at pH 7.4 and 22°C
0.0285
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0008
NADPH

-
in potassium diphosphate buffer (pH 7.7), at 14°C
0.016
NADPH
-
pH and temperature not specified in the publication
0.022
sulindac sulfide

-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.025
sulindac sulfide
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0693
sulindac sulfide
-
in in 0.1 M tricine buffer, pH 9.0, at 37°C
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Adali, O.; Carver, G.C.; Philpot, R.M.
The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine
Exp. Toxicol. Pathol.
51
271-276
1999
Homo sapiens
brenda
Klick, D.E.; Shadley, J.D.; Hines, R.N.
Differential regulation of human hepatic flavin containing monooxygenase 3 (FMO3) by CCAAT/enhancer-binding protein beta (C/EBPbeta) liver inhibitory and liver activating proteins
Biochem. Pharmacol.
76
268-278
2008
Homo sapiens
brenda
Lickteig, A.J.; Riley, R.; Melton, R.J.; Reitz, B.A.; Fischer, H.D.; Stevens, J.C.
Expression and characterization of functional dog flavin-containing monooxygenase 3
Drug Metab. Dispos.
37
1987-1990
2009
Canis lupus familiaris, Homo sapiens
brenda
Henderson, M.C.; Siddens, L.K.; Morre, J.T.; Krueger, S.K.; Williams, D.E.
Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes
Toxicol. Appl. Pharmacol.
233
420-427
2008
Homo sapiens (P31513), Mus musculus (P97501)
brenda
Large, P.; Boulton, C.; Crabbe, M.
The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans
Biochem. J.
128
137P-138P
1972
Aminobacter aminovorans
brenda
Lang, D.H.; Yeung, C.K.; Peter, R.M.; Ibarra, C.; Gasser, R.; Itagaki, K.; Philpot, R.M.; Rettie, A.E.
Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes: selective catalysis by FMO3
Biochem. Pharmacol.
56
1005-1012
1998
Homo sapiens
brenda
Catucci, G.; Gilardi, G.; Jeuken, L.; Sadeghi, S.
In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3
Biochem. Pharmacol.
83
551-558
2012
Homo sapiens
brenda
Strøm, A.
Biosynthesis of trimethylamine oxide in Calanus finmarchicus. Properties of a soluble trimethylamine monooxygenase
Comp. Biochem. Physiol. B
65
243-249
1980
Calanus finmarchicus
-
brenda
Haining, R.; Hunter, A.; Sadeque, A.; Philpot, R.; Rettie, A.
Baculovirus-mediated expression and purification of human FMO3: Catalytic, immunochemical, and structural characterization
Drug Metab. Dispos.
25
790-797
1997
Homo sapiens
brenda
Gut, I.; Conney, A.H.
The FAD-containing monooxygenase-catalyzed N-oxidation and demethylation of trimethylamine in rat liver microsomes
Drug Metabol. Drug Interact.
9
201-208
1991
Rattus norvegicus
brenda
Dolphin, C.; Riley, J.; Smith L, R.; Shephard, E.; Phillips, I.
Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA
Genomics
46
260-267
1997
Homo sapiens (P31513)
brenda
Treacy, E.; Akerman, B.; Chow, L.; Youil, R.; Bibeau, C.; Lin, J.; Bruce, A.; Knight, M.; Danks, D.; Cashman, J.; Forrest, S.
Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication
Hum. Mol. Genet.
7
839-845
1998
Homo sapiens
brenda
Burnettt, V.; Lawton, M.; Philpot, R.
Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3
J. Biol. Chem.
269
14314-14322
1994
Oryctolagus cuniculus (P32417), Oryctolagus cuniculus (P36367)
brenda
Koukouritaki, S.; Poch, M.; Cabacungan, E.; McCarver, D.; Hines, R.
Discovery of novel flavin-containing monooxygenase 3 (FMO3) single nucleotide polymorphisms and functional analysis of upstream haplotype variants
Mol. Pharmacol.
68
383-392
2005
Homo sapiens (P31513)
brenda
Chen, Y.; Patel, N.A.; Crombie, A.; Scrivens, J.H.; Murrell, J.C.
Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase
Proc. Natl. Acad. Sci. USA
108
17791-17796
2011
Candidatus Pelagibacter ubique, Candidatus Pelagibacter ubique HTCC1002, Candidatus Pelagibacter ubique HTCC7211, Methylocella silvestris, no activity in Dinoroseobacter shibae, no activity in Oceanicola batsensis, no activity in Roseobacter sp., no activity in Roseobacter sp. SK209-2-6, no activity in Sagittula stellata, Roseovarius sp. 217, Roseovarius sp., Ruegeria pomeroyi
brenda
Mitchell, S.; Smith, R.
A physiological role for flavin-containing monooxygenase (FMO3) in humans
Xenobiotica
40
301-305
2010
Homo sapiens
brenda
Fedejko-Kap, B.; Niemira, M.; Radominska-Pandya, A.; Mazerska, Z.
Flavin monooxygenases, FMO1 and FMO3, not cytochrome P450 isoenzymes, contribute to metabolism of anti-tumour triazoloacridinone, C-1305, in liver microsomes and HepG2 cells
Xenobiotica
41
1044-1055
2011
Homo sapiens (P31513), Rattus norvegicus
brenda