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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
?
-
-
-
-
?
dimethyl sulfide + NADPH + H+ + O2
dimethyl sulfoxide + NADP+ + H2O
-
-
-
?
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
? + NADP+ + H2O
-
-
-
?
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
4-[(2E)-2-(hydroxyimino)ethyl]phenol + NADP+ + H2O
-
-
-
-
?
additional information
?
-
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 + NADH + H+ + O2
N,N,N-trimethylamine N-oxide + NAD+ + 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,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
-
substrate from salmon protein hydrolysate
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
substrate from salmon protein hydrolysate
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
substrate from salmon protein hydrolysate
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
substrate from salmon protein hydrolysate
-
-
?
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
-
-
-
?
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
-
-
?
additional information
?
-
-
no activity with N-monomethylamine, glutathione, and cysteine
-
-
?
additional information
?
-
-
enzyme is capable of oxidizing N,N,N-trimethylamine, in presence of a sufficient amount of NADPH, yielding increased amounts of N,N,N-trimethylamine N-oxide
-
-
-
additional information
?
-
-
enzyme is capable of oxidizing N,N,N-trimethylamine, in presence of a sufficient amount of NADPH, yielding increased amounts of N,N,N-trimethylamine N-oxide
-
-
-
additional information
?
-
enzyme is capable of oxidizing N,N,N-trimethylamine, in presence of a sufficient amount of NADPH, yielding increased amounts of N,N,N-trimethylamine N-oxide
-
-
-
additional information
?
-
-
enzyme is capable of oxidizing N,N,N-trimethylamine, in presence of a sufficient amount of NADPH, yielding increased amounts of N,N,N-trimethylamine N-oxide
-
-
-
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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
0.25
Dimethyl sulfide
wild-type, pH 7, 25°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 - 0.116
Methimazole
0.0003 - 0.139
N,N,N-trimethylamine
0.0897 - 0.181
N,N-dimethylamine
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
isoform FMO3, at pH 8.4, temperature not specified in the publication
0.03
Methimazole
-
native enzyme, at pH and 37°C
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
0.116
Methimazole
wild-type, pH 7, 25°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
0.139
N,N,N-trimethylamine
wild-type, pH 7, 25°C
0.0897
N,N-dimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.181
N,N-dimethylamine
wild-type, pH 7, 25°C
0.0008
NADPH
-
in potassium diphosphate buffer (pH 7.7), at 14°C
0.0097
NADPH
mutant D314E, pH 7, 25°C
0.0128
NADPH
wild-type, pH 7, 25°C
0.016
NADPH
-
pH and temperature not specified in the publication
0.032
NADPH
mutant D314A, pH 7, 25°C
0.0341
NADPH
mutant N72A, pH 7, 25°C
0.0412
NADPH
mutant H227A, pH 7, 25°C
0.0449
NADPH
mutant R409A, pH 7, 25°C
0.0611
NADPH
mutant N288A, pH 7, 25°C
0.1018
NADPH
mutant R226A, pH 7, 25°C
0.1348
NADPH
mutant S203A, pH 7, 25°C
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
Strm, 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
Ruegeria pomeroyi, Roseovarius sp., Candidatus Pelagibacter ubique, no activity in Oceanicola batsensis, no activity in Roseobacter sp., no activity in Sagittula stellata, Methylocella silvestris, no activity in Dinoroseobacter shibae, Candidatus Pelagibacter ubique HTCC7211, no activity in Roseobacter sp. SK209-2-6, Candidatus Pelagibacter ubique HTCC1002, Roseovarius sp. 217
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
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Rattus norvegicus, Homo sapiens (P31513)
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Methylophaga aminisulfidivorans, Nocardiopsis alba, Micrococcus terreus (A0A1I7MIR7), Methylophaga aminisulfidivorans SK1
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Wang, X.; Zhang, N.; Teng, Z.; Wang, P.; Zhang, W.; Chen, X.; Zhang, Y.; Chen, Y.; Fu, H.; Li, C.
Structural and mechanistic insights into dimethylsulfoxide formation through dimethylsulfide oxidation
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Candidatus Pelagibacter sp. HTCC7211 (B6BT33)
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