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amphetamine + NADPH + H+ + O2
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
-
-
-
?
clomiphene + NADPH + H+ + O2
clomiphene N-oxide + NADP+ + H2O
clomipramine + NADPH + H+ + O2
clomipramine N-oxide + NADP+ + H2O
-
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
dasatinib + NADPH + H+ + O2
dasatinib N-oxide + NADP+ + H2O
-
-
-
?
deprenyl + NADPH + H+ + O2
?
ethionamide + NADPH + H+ + O2
?
GSK5182 + NADPH + H+ + O2
GSK5182 N-oxide + NADP+ + H2O
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
K11777 + NADPH + H+ + O2
K11777 N-oxide + NADP+ + H2O
a cysteine protease inhibitor against Trypanosoma cruzi, is converted to the N-oxide
-
-
?
loxapine + NADPH + H+ + O2
loxapine N-oxide + NADP+ + H2O
-
-
-
?
methamphetamine + NADPH + H+ + O2
?
methimazole + NADPH + H+ + O2
?
a thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
MK-0767 methyl sulfide + NADPH + H+ + O2
?
a peroxisome proliferator receptor activator, is converted to the S-oxide
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
N-deacetyl ketoconazole + NADPH + H+ + O2
?
an antifungal agent, is converted to the N-hydroxyl
-
-
?
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
a stimulant, is converted to the trans-N-oxide
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
an antihistamininc drug, is converted to the N-oxide
-
-
?
pyrazolacridine + NADPH + H+ + O2
pyrazolacridine N-oxide + NADP+ + H2O
an antitumor drug, is converted to the N-oxide
-
-
?
ranitidine + NADPH + H+ + O2
?
an antihistamininc drug, is converted to the N-oxide and/or S-oxide
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
?
a cytokine production inhibitor, is converted to the S-oxide
-
-
?
S16020 + NADPH + H+ + O2
S16020 N-oxide + NADP+ + H2O
a topoisomerase II inhibitor and antitumor drug, is converted to the N-oxide
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
a nonsteroidal antiinflammatory drug, is converted to the S-oxide
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac sulfide S-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
tazarotenic acid + NADPH + H+ + O2
?
a retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
thiacetazone + NADPH + H+ + O2
?
tozasertib + NADPH + H+ + O2
tozasertib N-oxide + NADP+ + H2O
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
(R)-metamphetamine + NADPH + H+ + O2
(R)-metamphetamine N-oxide + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
(S)-metamphetamine + NADPH + H+ + O2
(S)-metamphetamine N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
(S)-nicotine + NADPH + H+ + O2
?
-
-
-
-
?
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
-
(S)-nicotine N-1'-oxygenation
-
-
?
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
10-([N,N-dimethylaminopentyl]-2-trifluoromethyl)phenothiazine + NADPH + O2
?
-
-
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine + NADPH + H+ + O2
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine N-oxide + NADP+ + H2O
-
-
-
-
?
10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine + NADPH + O2
?
-
i.e. 5-DPT or diethylenetriaminepentaacetic acid
-
-
?
3-hydroxy-nabumetone + NADPH + H+ + O2
? + NADP+ + H2O
activation reaction
-
-
?
4-aminobenzoic acid hydrazide + NADPH + O2
?
-
-
-
?
5,6-dimethylxanthenone-4-acetic acid + NADPH + H+ + O2
?
-
substrate of isoform FMO3, methyl hydroxylation
-
-
?
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. C-1305
-
-
?
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
9-hydroxy-5,6-dimethyl-N-(2-(dimethylamino)ethyl)-6H-pyrido(4,3-B)-carbazole-1-carboxamide + NADPH + H+ + O2
2-(9-hydroxy-5,6-dimethyl-6H-pyrido[4,3-b]carbazole-1-carboxamido)-N,N-dimethylethan-1-amine oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
albendazole + NADPH + H+ + O2
albendazole S-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
almotriptan + NADPH + H+ + O2
almotriptan N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
ammonia + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
amphetamine + NADPH + H+ + O2
amphetamine N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
amphetamine + NADPH + O2
amphetamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
?
-
i.e. 3-(1-benzyl-1H-indazol-3-yloxy)-N,N-dimethylpropan-1-amine
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
benzylamine + [reduced NADPH-hemoprotein reductase] + O2
benzylamine N-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
chlorpromazine + NADPH + O2
chlorpromazine N-oxide + NADP+ + H2O
-
-
-
-
?
cimetidine + NADPH + H+ + O2
cimetidine S-oxide + NADP+ + H2O
cimetidine + NADPH + O2
cimetidine S-oxide + NADP+ + H2O
-
-
-
-
?
clomiphene + NADPH + H+ + O2
?
-
i.e. 2-[4-[2-chloro-1,2-diphenylethenyl]phenoxy]-N,N-diethylethanamine
-
-
?
clozapine + NADPH + H+ + O2
?
-
-
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
clozapine + NADPH + O2
?
-
-
-
-
?
contezolid + NADPH + H+ + O2
contezolid N-oxide + NADP+ + H2O
-
substrate of isoform FMO5
-
-
?
cysteamine + NADPH + H+ + O2
?
-
-
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
-
-
-
-
?
danusertib + NADPH + H+ + O2
danusertib N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
dasatinib + NADPH + H+ + O2
4-(6-((5-((2-chloro-6-methylphenyl)carbamoyl)thiazol-2-yl)amino)-2-methylpyrimidin-4-yl)-1-(2-hydroxyethyl)piperazine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
deprenyl + NADPH + H+ + O2
?
a monoamine oxidase type B inhibitor, is converted to the hydroxylamine
-
-
?
deprenyl + NADPH + H+ + O2
deprenyl N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
disulfoton + NADPH + H+ + O2
?
E-7016 + NADPH + H+ + O2
?
-
substrate of isoform FMO5, Bayer Villiger oxidation
-
-
?
esonarimod + NADPH + H+ + O2
S-methyl esonarimod + NADP+ + H2O
a antirheumatic drug, is converted to the S-oxide
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
ethionamide + NADPH + H+ + O2
ethionamide N-oxide + NADP+ + H2O
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
ethylene thiourea + NADPH + H+ + O2
?
-
-
-
-
?
ethylenethiourea + NADPH + O2
ethylenethiourea S-oxide + NADP+ + H2O
-
-
-
-
?
etionamide + NADPH + H+ + O2
etionamide S-oxide + NADP+ + H2O
substrate of FMO1, FMO3, and FMO2.1
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+
-
-
74% (+)-sulfoxide
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
GSK5182 + NADPH + H+ + O2
(Z)-2-(4-(5-hydroxy-1-(4-hydroxyphenyl)-2-phenylpent-1-en-1-yl)phenoxy)-N,N-dimethylethan-1-amine oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
hypotaurine + NADH + H+ + O2
taurine + NAD+ + H2O
S-oxygenation
-
-
?
hypotaurine + NADPH + H+ + O2
taurine + NADP+ + H2O
S-oxygenation
-
-
?
hypotaurine + O2 + NADH + H+
taurine + NAD+ + H2O
-
-
-
?
hypotaurine + O2 + NADPH + H+
taurine + NADP+ + H2O
-
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
imipramine + NADPH + O2
?
-
-
-
-
?
imipramine + NADPH + O2
imipramine N-oxide + NADP+ + H2O
-
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
itopride + NADPH + O2
?
-
-
-
-
?
K11777 + NADPH + H+ + O2
K11777 N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
L-775,606 + NADPH + H+ + O2
4-(3-(5-(4H-1,2,4-triazol-4-yl)-1H-indol-3-yl)propyl)-1-(3-fluorophenethyl)piperazine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
L-Met-Phe + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
-
isozymes FMO1-FMO4
-
-
?
L-Met-Val + NADPH + O2
(L-Met-S-oxide)-Val + NADP+ + H2O
-
isozymes FMO1-FMO4, low activity by isozyme FMO1
-
-
?
L-methionine + NADPH + H+ + O2
?
-
-
-
?
L-methionine + NADPH + H+ + O2
L-methionine S-oxide + NADP+ + H2O
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
lipoic acid + NADPH + O2
?
-
-
-
-
?
lorcaserin + NADPH + H+ + O2
lorcaserin N-oxide + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
loxapine + NADPH + H+ + O2
4-(2-chlorodibenzo[b,f][1,4]oxazepin-11-yl)-1-methylpiperazine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
mercaptoimidazole + NADPH + O2
mercaptoimidazole S-oxide + NADP+ + H2O
-
-
-
-
?
methamphetamine + NADPH + H+ + O2
methamphetamine N-oxide + NADP+ + H2O
a psychostimulant, is converted to the hydroxylamine
-
-
?
methimazole + NADH + H+
?
-
-
-
?
methimazole + NADPH + H+
?
-
-
-
?
methimazole + NADPH + H+ + O2
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
methimazole + NADPH + O2
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl p-tolyl sulfide + NADPH + H+ + O2
?
-
-
-
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl-4-tolyl sulfide + NADPH + H+ + O2
?
-
-
-
-
?
methylmercaptan + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
MK-0457 + NADPH + H+ + O2
MK-0457 N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
MK-0767 methyl sulfide + NADPH + H+ + O2
?
-
substrate of isoforms FMO1 and FMO3
-
-
?
moclobemide + NADPH + H+ + O2
moclobemide N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
?
N,N-diallyltryptamine + NADPH + H+ + O2
N,N-diallyltryptamine N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
N,N-dimethylamphetamine + NADPH + H+ + O2
N,N-dimethylamphetamine N-oxide + NADP+ + H2O
N-oxygenation mainly by isozyme FMO1, low activity with isozyme FMO3
-
-
?
N,N-dimethylaniline + NADH + H+ + O2
N,N-dimethylaniline N-oxide + NAD+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N-(3R)-1-azabicyclo[2.2.2]oct-3-ylfuro[2,3-c]pyridine-5-carboxamide + NADPH + H+ + O2
(R)-3-(furo[2,3-c]pyridine-5-carboxamido)quinuclidine 1-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
N-methyl-tamoxifen + NADPH + O2
N-methyl-tamoxifen N-oxide + NADP+ + H2O
-
recombinant isozymes FMO1 and FMO3
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
-
recombinant protein expressed in E. coli
-
-
?
naphthylthiourea + NADPH + O2
naphthylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
nicotine + NADPH + H+ + O2
(S)-nicotine N1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
nomifensine + NADPH + H+ + O2
?
-
substrate of isoforms FMO3 and FMO5
-
-
?
NSC645809 + NADPH + H+ + O2
N,N-diethyl-2-((8-hydroxy-6-oxo-6H-imidazo[4,5,1-de]acridin-5-yl)amino)ethan-1-amine oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
olanzapine + NADPH + H+ + O2
1-methyl-4-(2-methyl-10H-benzo[b]thieno[2,3-e][1,4]diazepin-4-yl)piperazine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
orphenadrine + NADPH + H+ + O2
orphenadrine N-oxide + NADP+ + H2O
an anticholinergic drug
-
-
?
p-tolyl sulfide + NADPH + O2
p-tolyl sulfoxide + NADP+ + H2O
-
S-oxidase activity
-
-
?
pargyline + NADPH + H+ + O2
pargyline N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
-
isozyme FMO3
-
-
?
phenylthiourea + NADPH + O2
phenylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
phorate + NADPH + H+ + O2
?
a thioether-containing organophosphate insecticide
-
-
?
phospho-sulindac + NADPH + H+ + O2
?
-
substrate of isoforms FMO1, FMO3, and FMO5
-
-
?
primaquine + NADPH + H+ + O2
?
-
substrate of isoform FMO3
-
-
?
pyrazolacridine + NADPH + H+ + O2
pyrazolacridine N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
pyrazoloacridine + NADPH + O2
pyrazoloacridine N-oxide + NADP+ + H2O
-
-
-
-
?
quazepam + NADPH + H+ + O2
7-chloro-5-(2-fluorophenyl)-1-(2,2,2-trifluoroethyl)-1,3-dihydro-2H-benzo[e][1,4]diazepin-2-one + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
ranitidine + NADPH + H+ + O2
?
-
substrate of isoforms FMO3 and FMO5, S-oxygenation and N-oxygenation
-
-
?
ranitidine + NADPH + O2
?
-
-
-
-
?
S-allyl-L-cysteine + NADPH + H+ + O2
?
-
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
S-methyl esonarimod S-oxide + NADP+ + H2O
S-methyl N,N-diethyldithiocarbamate + NADPH + H+ + O2
(diethylnitroryl)(methylsulfanyl)methanethione + NADP+ + H2O
-
substrate of isoform FMO1 and FMO3
-
-
?
selegiline + NADPH + H+ + O2
?
-
i.e. (2R)-N-methyl-1-phenyl-N-prop-2-ynylpropan-2-amine
-
-
?
selenomethionine + NADPH + H+ + O2
seleno-L-methionine Se-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
SNI-2011 + NADPH + H+ + O2
?
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
SNI-2011 + NADPH + H+ + O2
SNI-2011 N-oxide + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
sulfamethoxazole + NADPH + O2
?
sulindac sulfide + NADPH + H+ + O2
?
-
substrate of isoforms FMO1 and FMO3
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
S-oxidation
-
-
?
sulindac sulfide + NADPH + O2
(S,R)-sulindac + NADP+ + H2O
-
-
-
-
?
tamoxifen + NADPH + H+ + O2
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
tazarotenic acid + NADPH + H+ + O2
tazarotenate N-oxide + NADP+ + H2O
TG100435 + NADPH + H+ + O2
1-(2-(4-((7-(2,6-dichlorophenyl)-5-methylbenzo[e][1,2,4]triazin-3-yl)amino)phenoxy)ethyl)pyrrolidine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
TG100435 + NADPH + H+ + O2
?
-
substrate of isoform FMO1
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
thiacetazone + NADPH + H+ + O2
?
thiacetazone + NADPH + H+ + O2
thiacetazone N-oxide + NADP+ + H2O
thiacetazone + NADPH + H+ + O2
thiacetazone S-oxide + NADP+ + H2O
thiobenzamide + NADPH + H+ + O2
thiobenzamide N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
thiourea + NADPH + O2
thiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
tozasertib + NADPH + H+ + O2
?
triethylamine + NADPH + H+ + O2
triethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trifluoroperazine + NADPH + H+ + O2
2,3,4-trifluoropyridine 1-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
trimethylamine + NADPH + H+ + O2
?
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
trimethylamine + NADPH + O2
?
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
tyramine + NADPH + O2
tyramine N-oxide + NADP+ + H2O
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
[7-(2,6-dichloro-phenyl)-5-methyl-benzo[1,2,4]triazin-3-yl]-[4-(2-pyrrolidin-1-yl-ethoxy)-phenyl]-amine + NADPH + H+ + O2
[7-(2,6-dichlorophenyl)-5-methyl-benzo[1,2,4]triazin-3-yl]-(4-[2-(1-oxy-pyrrolidin-1-yl)-ethoxy]-phenyl)-amine + NADP+ + H2O
-
i.e. TG100435, a multitargeted Src family kinase inhibitor with anticancer activity, FMO3 is the primary enzyme responsible for TG100855 formation, enzyme-mediated retroreduction of TG100855 back to TG100435 is observed catalyzed by a cytochrome P450 reductase, overview
i.e. TG100855, the N-oxide product is also a multitargeted Src family kinase inhibitor with anticancer activity
-
?
additional information
?
-
amphetamine + NADPH + H+ + O2
?
an antipsychotic agent, is converted to the hydroxylamine
-
-
?
amphetamine + NADPH + H+ + O2
?
an antipsychotic agent, is converted to the hydroxylamine
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
high activity
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
a nonsteroidal antiinflammatory drug, is converted to the N-oxide
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
N-oxygenation of benzydamine by the wild-type and N61S mutant variant of FMO3
-
-
?
clomiphene + NADPH + H+ + O2
clomiphene N-oxide + NADP+ + H2O
-
-
-
?
clomiphene + NADPH + H+ + O2
clomiphene N-oxide + NADP+ + H2O
clomiphene is used in infertility medication
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
-
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
an antipsychotic agent, is converted to the N-oxide
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
an antipsychotic agent, is converted to the N-oxide
-
-
?
deprenyl + NADPH + H+ + O2
?
a monoamine oxidase type B inhibitor, is converted to the hydroxylamine
-
-
?
deprenyl + NADPH + H+ + O2
?
a monoamine oxidase type B inhibitor, is converted to the hydroxylamine
-
-
?
ethionamide + NADPH + H+ + O2
?
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
?
an antibiotic agent
-
-
?
GSK5182 + NADPH + H+ + O2
GSK5182 N-oxide + NADP+ + H2O
-
-
-
?
GSK5182 + NADPH + H+ + O2
GSK5182 N-oxide + NADP+ + H2O
an antidiabetic lead molecule
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
-
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
a dopamine D2 receptor antagonist, is converted to the N-oxide
-
-
?
methamphetamine + NADPH + H+ + O2
?
a psychostimulant, is converted to the hydroxylamine
-
-
?
methamphetamine + NADPH + H+ + O2
?
a psychostimulant, is converted to the hydroxylamine
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
-
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
tamoxifen is used in breast cancer medication
-
-
?
thiacetazone + NADPH + H+ + O2
?
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
?
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
-
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
-
-
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
-
isozyme FMO3
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
-
-
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
-
formation of the cis-oxime
-
-
?
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
i.e. C-1299
-
-
?
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
i.e. C-1305
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
a nonsteroidal antiinflammatory drug, is converted to the N-oxide
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
a dopemaine D2 antagonist
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
a dopemaine D2 antagonist
-
-
?
cimetidine + NADPH + H+ + O2
cimetidine S-oxide + NADP+ + H2O
-
S-oxygenation of cimetidine, i.e. CIM, a histamine H2-receptor antagonist of therapeutic utility in the treatment of peptic ulcer disease and gastric hypersecretory syndromes. Development of in-line screening and an off-line chiral CE method for determination of the stereoselectivity of flavin-containing monooxygenase isoforms FMO1, FMO3, and FMO5 using chiral specific selectors, overview
-
-
?
cimetidine + NADPH + H+ + O2
cimetidine S-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
dapsone + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
dapsone + NADPH + O2
?
isozyme FMO3, not FMO1
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
-
-
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
-
i.e. O,O-diethyl O-2-ethylthioethyl phosphorothioate, isozymes FMO1 and FMO3, higher activity by FMO1
-
-
?
disulfoton + NADPH + H+ + O2
?
-
-
-
-
?
disulfoton + NADPH + H+ + O2
?
a thioether-containing organophosphate insecticide
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
-
-
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
-
i.e. alpha-ethylthio-o-tolyl methylcarbamate, isozymes FMO1 and FMO3, higher activity by FMO1
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
i.e. ETA, S-oxygenation by isozymes FMO1, FMO2, and FMO3
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
-
substrate of isoforms FMO1, FMO2, and FMO3
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
-
bioactivation by isozymes FMO1 and FMO3
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
-
a thioamide-containing second line antitubercular prodrug
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
-
-
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
-
-
more than 95% (+)-sulfoxide
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
-
i.e. O,O-dimethyl O-4-methylthio-m-tolyl phosphorothioate, isozymes FMO1 and FMO3, stereospecifc product formation, overview
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
an antidepressant, is converted to the N-oxide
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
an antidepressant, is converted to the N-oxide
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
a dopamine D2 receptor antagonist, is converted to the N-oxide
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
a dopamine D2 receptor antagonist, is converted to the N-oxide
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
-
free and N-terminally peptide-bound L-methionine, no activity with modified peptide-bound methionine and with N-acetyl-L-methionine, isozymes FMO1-FMO4
stereospecificity for formation of the D-isomer, especially by isozyme FMO3
-
?
methimazole + NADPH + H+ + O2
?
a thyroperoxidase inhibitor
-
-
?
methimazole + NADPH + H+ + O2
?
an thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
an thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
low activity with FMO2.1, moderate activity with FMO3, high activity with FMO1
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
-
substrate of isoforms FMO1, FMO2, and FMO3
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
S-oxygenation
-
-
?
methimazole + NADPH + O2
?
-
-
-
-
?
methimazole + NADPH + O2
?
-
-
-
?
methimazole + NADPH + O2
?
-
isozyme FMO3
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
recombinant protein expressed in E. coli
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
FMO3 5000 times more efficient than FMO5
-
-
?
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
-
-
-
-
?
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
-
i.e. 4-methylthio-3,5-xylyl methylcarbamate, isozyme FMO1 acts stereospecifically, no activity by isozyme FMO3
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
an antifungal agent, is converted to the N-hydroxyl
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
-
substrate of isoform FMO1
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
an antihistamininc drug, is converted to the N-oxide
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
an antihistamininc drug, is converted to the N-oxide
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
S-methyl esonarimod S-oxide + NADP+ + H2O
an cytokine production inhibitor, is converted to the S-oxide
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
S-methyl esonarimod S-oxide + NADP+ + H2O
-
substrate of isoforms FMO1, FMO3, and FMO5
-
-
?
sulfamethoxazole + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
sulfamethoxazole + NADPH + O2
?
isozyme FMO3, not FMO1
-
-
?
tamoxifen + NADPH + H+ + O2
?
-
-
-
-
?
tamoxifen + NADPH + H+ + O2
?
-
i.e. (Z)-2-[4-(1,2-diphenylbut-1-enyl)phenoxy]-N,N-dimethylethanamine
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen metabolism pathways involving FMOs and CYP450s, tamoxifen N-oxide is reconverted into tamoxifen by reduced hemoglobin and NADPH-P450 oxidoreductase, a metabolic cycle in vivo, overview
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway, low level of tamoxifen N-oxide production in human liver microsomes may be explained by the kinetics of FMO1 versus FMO3
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
i.e. (Z)-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene), a drug used in breast cancer therapy, isozymes FMO1 and FMO3
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tazarotenic acid + NADPH + H+ + O2
tazarotenate N-oxide + NADP+ + H2O
an retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
tazarotenic acid + NADPH + H+ + O2
tazarotenate N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
-
bioactivation by isozymes FMO1 and FMO3, two-step process
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
-
a thiourea-containing second line antitubercular prodrug
-
-
?
thiacetazone + NADPH + H+ + O2
?
-
-
-
-
?
thiacetazone + NADPH + H+ + O2
?
a anti-tubercular drug, high activity
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone N-oxide + NADP+ + H2O
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone N-oxide + NADP+ + H2O
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone S-oxide + NADP+ + H2O
low activity with FMO1 and FMO3, high activity with FMO2.1
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone S-oxide + NADP+ + H2O
-
substrate of isoforms FMO1, FMO2, and FMO3
-
-
?
tozasertib + NADPH + H+ + O2
?
-
-
-
-
?
tozasertib + NADPH + H+ + O2
?
-
i.e. N-[4-[4-(4-methylpiperazin-1-yl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]pyrimidin2yl]sulfanylphenyl]cyclopropane carboxamide
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
substrate of isoform FMO3
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
-
isozyme FMO3
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
-
preferred substrate of isozyme FMO3
-
-
?
voriconazole + NADPH + H+ + O2
?
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
-
liver microsomes, a potent second-generation triazole antifungal agent with broad-spectrum activity against clinically important fungi
-
-
?
voriconazole + NADPH + H+ + O2
?
-
recombinant FMO1 and FMO3, no activity with FMO5, N-oxidation of the fluoropyrimidine ring, its hydroxylation, and hydroxylation of the adjacent methyl group
-
-
?
voriconazole + NADPH + H+ + O2
?
-
substrate of isoforms FMO1 and FMO3
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
-
substrate of isoforms FMO1 and FMO3
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
human FMO3 regulatory elements, overview
-
-
?
additional information
?
-
-
human FMO3 regulatory elements, overview
-
-
?
additional information
?
-
comparison of in vivo activity of FMO enzyme with P450 enzme in N-oxygenation of drugs at different pH values, overview
-
-
-
additional information
?
-
-
comparison of in vivo activity of FMO enzyme with P450 enzme in N-oxygenation of drugs at different pH values, overview
-
-
-
additional information
?
-
analysis of the uncoupling reactions in the catalytic cycle of enzyme FMO3, overview. The level of uncoupling varies between 50% and 70% (wild-type) and 90-98% (mutant N61S) for incubations with NADPH and benzydamine over a period of 5 or 20 min, respectively. The substrate lowers the level of uncoupling only related to the H2O2 and not the superoxide radical. In the absence of the substrate benzydamine (BZD), mutant N61S produces higher amounts of H2O2 compared to wild-type
-
-
-
additional information
?
-
-
analysis of the uncoupling reactions in the catalytic cycle of enzyme FMO3, overview. The level of uncoupling varies between 50% and 70% (wild-type) and 90-98% (mutant N61S) for incubations with NADPH and benzydamine over a period of 5 or 20 min, respectively. The substrate lowers the level of uncoupling only related to the H2O2 and not the superoxide radical. In the absence of the substrate benzydamine (BZD), mutant N61S produces higher amounts of H2O2 compared to wild-type
-
-
-
additional information
?
-
identification of GSK5182 N-oxide products by mass spectrometry
-
-
-
additional information
?
-
-
identification of GSK5182 N-oxide products by mass spectrometry
-
-
-
additional information
?
-
N- and S-oxygenation activity of truncated wild-type human flavin-containing monooxygenase 3 and its common polymorphic variants, overview. The enzyme binds noncovalently one molecule of FAD and is reduced by NADPH before exerting its catalysis
-
-
-
additional information
?
-
-
N- and S-oxygenation activity of truncated wild-type human flavin-containing monooxygenase 3 and its common polymorphic variants, overview. The enzyme binds noncovalently one molecule of FAD and is reduced by NADPH before exerting its catalysis
-
-
-
additional information
?
-
-
comparison of FMO3 and FMO5
-
-
?
additional information
?
-
-
modulation of activity by site directed mutagenesis
-
-
?
additional information
?
-
-
overview on substrate specifities and requirements of FMO1, FMO3
-
-
?
additional information
?
-
-
enzyme regulation, overview
-
-
?
additional information
?
-
arylamine compounds, such as sulfamethoxazole and dapsone, are metabolized in epidermal keratinocytes to arylhydroxylamine metabolites that autooxidize to arylnitroso derivatives, which in turn bind to cellular proteins and can act as antigens/immunogens, methimazole and 4-aminobenzoic acid hydrazide attenuate the protein haptenation, overview
-
-
?
additional information
?
-
-
effects of genetic variants of isozyme FMO3 on N- and S-oxygenation activities, FMO3 polymorphisms are responsible for the genetic disorder trimethylaminuria, or fish-like odor syndrome, overview
-
-
?
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, isozymes FMO1-FMO3 are involved in detoxication and drug metabolism, FMO3 deficiency causes the disease trimethylaminuria
-
-
?
additional information
?
-
-
FMOs are, together with cytochrome P450 monooxygenases, the major oxidative enzymes in phase I metabolism, extrahepatic metabolism of carbamate and organophosphate thioether compounds, isozyme FMO1 shows higher turnover numbers than isozyme FMO3 for all pesticides studies, overview
-
-
?
additional information
?
-
-
FMOs catalyze NADPH-dependent monooxygenation of soft-nucleophilic nitrogen, sulfur, and phosphorous atoms contained within various drugs, pesticides, and xenobiotics, isozyme FMO3 is responsible for the majority of FMO-mediated xenobiotic metabolism in the adult human liver, FMO3 mutations causing defects in trimethylamine N-oxygenation, result in the disorder known as trimethylaminuria, TMAU, or fish-odour syndrome, overview, interindividual variability in the expression of FMO3 affect drug and exogenous chemical metabolism in the liver and other tissues
-
-
?
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, FMO is not induced by xenobiotics, isozyme FMO3 mutant alleles contribute to the disease known as trimethylaminuria, the enzyme is involved in detoxification and drug metabolism, overview, expression of FMO5 is markedly down-regulated in the liver of humans with type II diabetes, patients diagnosed with atrial fibrillation document a significant increase in the expression of FMO1, FMO may be associated with sideroblastic anemia, FMO3 mutations lead to trimethylaminuria, detailed overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the NADPH-dependent N-and S-oxidation of a variety of therapeutics, environmental toxicants, carcinogens, and nutrients
-
-
?
additional information
?
-
-
carbophenothion, i.e. S-4-chlorophenylthiomethyl O,O-diethyl phosphorodithioate, and fonofos, i.e. O-ethyl S-phenyl (RS)-ethylphosphonodithioate, are poor substrates
-
-
?
additional information
?
-
-
FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, isozyme substrate specificity, detailed overview, no activity with 1,3-diphenylthiourea
-
-
?
additional information
?
-
-
FMO oxygenates soft nucleophiles, and converts lipophilic compounds into more hydrophilic metabolites, potential adverse drug-drug interactions are minimized for drugs prominently metabolized by FMO, substrate specificities of isozmes, overview
-
-
?
additional information
?
-
-
stereoselectivity of male and female liver microsomes, and of recombinant isozymes FMO1, FMO3, and FMO4, overview
-
-
?
additional information
?
-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
-
-
?
additional information
?
-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
-
-
?
additional information
?
-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
-
-
?
additional information
?
-
-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
-
-
?
additional information
?
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
-
-
?
additional information
?
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
-
-
?
additional information
?
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
-
-
?
additional information
?
-
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
-
-
?
additional information
?
-
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
?
additional information
?
-
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
?
additional information
?
-
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
?
additional information
?
-
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
?
additional information
?
-
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
?
additional information
?
-
-
the enzyme is regulated by hormones, e.g. testosterone
-
-
?
additional information
?
-
-
FMO1 mediates the formation of a reactive intermediate of 4-fluoro-N-methylaniline. FMO1 catalyzes a carbon oxidation reaction coupled with defluorination that leads to the formation of 4-N-methylaminophenol, mechanism, overview. A labile 1-fluoro-4-(methylimino)cyclohexa-2,5-dienol intermediate is formed leading to an electrophilic quinoneimine intermediate
-
-
?
additional information
?
-
isoform FMO5 exhibits a low catalytic activity only for sulfoxidation of methyl 4-tolyl sulfide
-
-
?
additional information
?
-
-
isoform FMO5 exhibits a low catalytic activity only for sulfoxidation of methyl 4-tolyl sulfide
-
-
?
additional information
?
-
isozyme FMO5 does not metabolize C-1305
-
-
?
additional information
?
-
isozyme FMO5 does not metabolize C-1305
-
-
?
additional information
?
-
-
isozyme FMO5 does not metabolize C-1305
-
-
?
additional information
?
-
formation of a highly stable C4a-hydroperoxyflavin intermediate of hFMO1 upon reduction by NADPH in presence of O2, the intermediate is not fully re-oxidized after 30 min at 15°C in the absence of substrate. The enzyme is below 1% uncoupled in the presence of substrate. Higher stability of the hFMO1 intermediate compared to the stability of the intermediate of isozyme hFMO3
-
-
-
additional information
?
-
-
formation of a highly stable C4a-hydroperoxyflavin intermediate of hFMO1 upon reduction by NADPH in presence of O2, the intermediate is not fully re-oxidized after 30 min at 15°C in the absence of substrate. The enzyme is below 1% uncoupled in the presence of substrate. Higher stability of the hFMO1 intermediate compared to the stability of the intermediate of isozyme hFMO3
-
-
-
additional information
?
-
-
human FMO1 catalyzes the oxygenation of hypotaurine in vitro. Ability of hypotaurine to act as a competitor substrate of FMO1 is assessed by measuring the effect of various concentrations of hypotaurine on FMO1-catalyzed S-oxygenation of methimazole
-
-
-
additional information
?
-
human FMO1 catalyzes the oxygenation of hypotaurine in vitro. Ability of hypotaurine to act as a competitor substrate of FMO1 is assessed by measuring the effect of various concentrations of hypotaurine on FMO1-catalyzed S-oxygenation of methimazole
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
-
-
-
?
clomiphene + NADPH + H+ + O2
clomiphene N-oxide + NADP+ + H2O
clomiphene is used in infertility medication
-
-
?
clomipramine + NADPH + H+ + O2
clomipramine N-oxide + NADP+ + H2O
-
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
-
-
-
?
dasatinib + NADPH + H+ + O2
dasatinib N-oxide + NADP+ + H2O
-
-
-
?
GSK5182 + NADPH + H+ + O2
GSK5182 N-oxide + NADP+ + H2O
an antidiabetic lead molecule
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
loxapine + NADPH + H+ + O2
loxapine N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
tozasertib + NADPH + H+ + O2
tozasertib N-oxide + NADP+ + H2O
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
-
-
-
?
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
-
(S)-nicotine N-1'-oxygenation
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
-
-
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
-
-
-
-
?
3-hydroxy-nabumetone + NADPH + H+ + O2
? + NADP+ + H2O
activation reaction
-
-
?
4-aminobenzoic acid hydrazide + NADPH + O2
?
-
-
-
?
amphetamine + NADPH + O2
amphetamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzylamine + [reduced NADPH-hemoprotein reductase] + O2
benzylamine N-oxide + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cimetidine + NADPH + O2
cimetidine S-oxide + NADP+ + H2O
-
-
-
-
?
clozapine + NADPH + O2
?
-
-
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
-
-
-
-
?
dapsone + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
-
-
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
-
bioactivation by isozymes FMO1 and FMO3
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
-
-
-
-
?
hypotaurine + NADH + H+ + O2
taurine + NAD+ + H2O
S-oxygenation
-
-
?
hypotaurine + NADPH + H+ + O2
taurine + NADP+ + H2O
S-oxygenation
-
-
?
imipramine + NADPH + O2
?
-
-
-
-
?
itopride + NADPH + O2
?
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
-
-
-
-
?
lipoic acid + NADPH + O2
?
-
-
-
-
?
methimazole + NADPH + O2
?
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylamphetamine + NADPH + H+ + O2
N,N-dimethylamphetamine N-oxide + NADP+ + H2O
N-oxygenation mainly by isozyme FMO1, low activity with isozyme FMO3
-
-
?
N,N-dimethylaniline + NADH + H+ + O2
N,N-dimethylaniline N-oxide + NAD+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
-
isozyme FMO3
-
-
?
ranitidine + NADPH + O2
?
-
-
-
-
?
sulfamethoxazole + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
sulindac sulfide + NADPH + O2
(S,R)-sulindac + NADP+ + H2O
-
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
-
bioactivation by isozymes FMO1 and FMO3, two-step process
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
tyramine + NADPH + O2
tyramine N-oxide + NADP+ + H2O
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
-
liver microsomes, a potent second-generation triazole antifungal agent with broad-spectrum activity against clinically important fungi
-
-
?
[7-(2,6-dichloro-phenyl)-5-methyl-benzo[1,2,4]triazin-3-yl]-[4-(2-pyrrolidin-1-yl-ethoxy)-phenyl]-amine + NADPH + H+ + O2
[7-(2,6-dichlorophenyl)-5-methyl-benzo[1,2,4]triazin-3-yl]-(4-[2-(1-oxy-pyrrolidin-1-yl)-ethoxy]-phenyl)-amine + NADP+ + H2O
-
i.e. TG100435, a multitargeted Src family kinase inhibitor with anticancer activity, FMO3 is the primary enzyme responsible for TG100855 formation, enzyme-mediated retroreduction of TG100855 back to TG100435 is observed catalyzed by a cytochrome P450 reductase, overview
i.e. TG100855, the N-oxide product is also a multitargeted Src family kinase inhibitor with anticancer activity
-
?
additional information
?
-
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
tamoxifen is used in breast cancer medication
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + O2
?
-
-
-
-
?
methimazole + NADPH + O2
?
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen metabolism pathways involving FMOs and CYP450s, tamoxifen N-oxide is reconverted into tamoxifen by reduced hemoglobin and NADPH-P450 oxidoreductase, a metabolic cycle in vivo, overview
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway, low level of tamoxifen N-oxide production in human liver microsomes may be explained by the kinetics of FMO1 versus FMO3
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
-
preferred substrate of isozyme FMO3
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview
-
-
?
additional information
?
-
human FMO3 regulatory elements, overview
-
-
?
additional information
?
-
-
human FMO3 regulatory elements, overview
-
-
?
additional information
?
-
comparison of in vivo activity of FMO enzyme with P450 enzme in N-oxygenation of drugs at different pH values, overview
-
-
-
additional information
?
-
-
comparison of in vivo activity of FMO enzyme with P450 enzme in N-oxygenation of drugs at different pH values, overview
-
-
-
additional information
?
-
-
enzyme regulation, overview
-
-
?
additional information
?
-
arylamine compounds, such as sulfamethoxazole and dapsone, are metabolized in epidermal keratinocytes to arylhydroxylamine metabolites that autooxidize to arylnitroso derivatives, which in turn bind to cellular proteins and can act as antigens/immunogens, methimazole and 4-aminobenzoic acid hydrazide attenuate the protein haptenation, overview
-
-
?
additional information
?
-
-
effects of genetic variants of isozyme FMO3 on N- and S-oxygenation activities, FMO3 polymorphisms are responsible for the genetic disorder trimethylaminuria, or fish-like odor syndrome, overview
-
-
?
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, isozymes FMO1-FMO3 are involved in detoxication and drug metabolism, FMO3 deficiency causes the disease trimethylaminuria
-
-
?
additional information
?
-
-
FMOs are, together with cytochrome P450 monooxygenases, the major oxidative enzymes in phase I metabolism, extrahepatic metabolism of carbamate and organophosphate thioether compounds, isozyme FMO1 shows higher turnover numbers than isozyme FMO3 for all pesticides studies, overview
-
-
?
additional information
?
-
-
FMOs catalyze NADPH-dependent monooxygenation of soft-nucleophilic nitrogen, sulfur, and phosphorous atoms contained within various drugs, pesticides, and xenobiotics, isozyme FMO3 is responsible for the majority of FMO-mediated xenobiotic metabolism in the adult human liver, FMO3 mutations causing defects in trimethylamine N-oxygenation, result in the disorder known as trimethylaminuria, TMAU, or fish-odour syndrome, overview, interindividual variability in the expression of FMO3 affect drug and exogenous chemical metabolism in the liver and other tissues
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additional information
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nitrogen- and sulfur-containing endogenous substrates and physiologic functions, FMO is not induced by xenobiotics, isozyme FMO3 mutant alleles contribute to the disease known as trimethylaminuria, the enzyme is involved in detoxification and drug metabolism, overview, expression of FMO5 is markedly down-regulated in the liver of humans with type II diabetes, patients diagnosed with atrial fibrillation document a significant increase in the expression of FMO1, FMO may be associated with sideroblastic anemia, FMO3 mutations lead to trimethylaminuria, detailed overview
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additional information
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-
-
the enzyme catalyzes the NADPH-dependent N-and S-oxidation of a variety of therapeutics, environmental toxicants, carcinogens, and nutrients
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?
additional information
?
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drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
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additional information
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drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
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?
additional information
?
-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
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?
additional information
?
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-
drug metabolism, overview, most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
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?
additional information
?
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
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additional information
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drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
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additional information
?
-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
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additional information
?
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-
drug metabolism, overview, the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis, but is upregulated in the myocardial tissue of patients with atrial fibrillation
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?
additional information
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FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
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?
additional information
?
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FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
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?
additional information
?
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FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
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?
additional information
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FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
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?
additional information
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FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
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additional information
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the enzyme is regulated by hormones, e.g. testosterone
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0.0345 - 0.0659
Benzydamine
0.0183 - 0.0444
clomiphene
0.0101 - 0.0163
sulindac sulfide
0.00134 - 0.0081
tamoxifen
15 - 38
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
0.0229
5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO1, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.05903 - 0.4314
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
0.0426 - 0.056
Benzydamine
0.022 - 0.08
chlorpromazine
0.018
clomiphene
-
pH and temperature not specified in the publication
0.101 - 1.45
ethiofencarb
0.105 - 0.336
Ethionamide
0.0502 - 0.0761
ethylenethiourea
0.018 - 0.046
mercaptoimidazole
0.007 - 0.5758
Methimazole
0.079
methiocarb
-
pH 9.0, isozyme FMO1
0.0048 - 0.3
methyl p-tolyl sulfide
0.0445 - 0.261
N,N-dimethylamphetamine
0.0871
p-tolyl sulfide
-
37°C
0.147
pyrazoloacridine
-
-
0.314
selegiline
-
pH and temperature not specified in the publication
0.0058 - 0.007
thiacetazone
0.023
tozasertib
-
pH and temperature not specified in the publication
0.0209 - 0.0373
trimethylamine
additional information
additional information
-
0.0345
Benzydamine
recombinant His-tagged full-length mutant E308G, pH 7.4, 37°C
0.0373
Benzydamine
recombinant His-tagged full-length mutant V257M, pH 7.4, 37°C
0.038
Benzydamine
recombinant His-tagged truncated mutant V257M, pH 7.4, 37°C
0.0397
Benzydamine
recombinant His-tagged truncated mutant E308G, pH 7.4, 37°C
0.052
Benzydamine
recombinant His-tagged full-length wild-type enzyme, pH 7.4, 37°C
0.053
Benzydamine
recombinant His-tagged truncated wild-type enzyme, pH 7.4, 37°C
0.0593
Benzydamine
recombinant His-tagged full-length mutant E158K, pH 7.4, 37°C
0.0659
Benzydamine
recombinant His-tagged truncated mutant E158K, pH 7.4, 37°C
0.0183
clomiphene
recombinant wild-type enzyme, pH 7.4, 37°C
0.0205
clomiphene
recombinant mutant E158K, pH 7.4, 37°C
0.0332
clomiphene
recombinant mutant V257M, pH 7.4, 37°C
0.0444
clomiphene
recombinant mutant E308G, pH 7.4, 37°C
0.00457
GSK5182
recombinant mutant E158K, pH 7.4, 37°C
0.00982
GSK5182
recombinant wild-type enzyme, pH 7.4, 37°C
0.0285
GSK5182
recombinant mutant V257M, pH 7.4, 37°C
0.0587
GSK5182
recombinant mutant E308G, pH 7.4, 37°C
0.0101
sulindac sulfide
recombinant His-tagged full-length mutant E308G, pH 7.4, 37°C
0.0103
sulindac sulfide
recombinant His-tagged truncated mutant E308G, pH 7.4, 37°C
0.0103
sulindac sulfide
recombinant His-tagged truncated mutant V257M, pH 7.4, 37°C
0.0127
sulindac sulfide
recombinant His-tagged truncated wild-type enzyme, pH 7.4, 37°C
0.0143
sulindac sulfide
recombinant His-tagged full-length mutant V257M, pH 7.4, 37°C
0.0151
sulindac sulfide
recombinant His-tagged full-length mutant E158K, pH 7.4, 37°C
0.0156
sulindac sulfide
recombinant His-tagged full-length wild-type enzyme, pH 7.4, 37°C
0.0163
sulindac sulfide
recombinant His-tagged truncated mutant E158K, pH 7.4, 37°C
0.00134
tamoxifen
recombinant His-tagged truncated mutant E158K, pH 7.4, 37°C
0.00156
tamoxifen
recombinant mutant E158K, pH 7.4, 37°C
0.0016
tamoxifen
recombinant His-tagged full-length mutant E158K, pH 7.4, 37°C
0.0025
tamoxifen
recombinant His-tagged full-length mutant E308G, pH 7.4, 37°C
0.0025
tamoxifen
recombinant mutant E308G, pH 7.4, 37°C
0.0029
tamoxifen
recombinant His-tagged truncated mutant E308G, pH 7.4, 37°C
0.0056
tamoxifen
recombinant His-tagged truncated wild-type enzyme, pH 7.4, 37°C
0.0064
tamoxifen
recombinant wild-type enzyme, pH 7.4, 37°C
0.0064
tamoxifen
recombinant His-tagged full-length wild-type enzyme, pH 7.4, 37°C
0.0071
tamoxifen
recombinant His-tagged truncated mutant V257M, pH 7.4, 37°C
0.0081
tamoxifen
recombinant His-tagged full-length mutant V257M, pH 7.4, 37°C
0.0081
tamoxifen
recombinant mutant V257M, pH 7.4, 37°C
15
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3
25
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3
32
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3
35
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3
38
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3
0.05903
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO1, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.4314
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO5, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.0426
Benzydamine
-
pH 7.4, 37°C
0.056
Benzydamine
-
pH and temperature not specified in the publication
0.022
chlorpromazine
-
pH 8.4, 37°C, recombinant mutant H360P His6-tagged MBT-fusion-FMO1
0.026
chlorpromazine
-
pH 8.4, 37°C, recombinant mutant L360P His6-tagged MBT-fusion-FMO3
0.028
chlorpromazine
-
pH 8.4, 37°C, recombinant mutant L360H His6-tagged MBT-fusion-FMO3
0.058
chlorpromazine
-
pH 8.4, 37°C, recombinant wild-type His6-tagged MBT-fusion-FMO1
0.061
chlorpromazine
-
pH 8.4, 37°C, recombinant wild-type His6-tagged MBT-fusion-FMO3
0.076
chlorpromazine
-
pH 8.4, 37°C, recombinant mutant L360Q His6-tagged MBT-fusion-FMO3
0.08
chlorpromazine
-
pH 8.4, 37°C, recombinant mutant L360A His6-tagged MBT-fusion-FMO3
4.31
cimetidine
-
pH 8.3, S-oxygenation with (+)-enantiomer formation by isozyme FMO1
4.56
cimetidine
-
pH 8.3, S-oxygenation with (-)-enantiomer formation by isozyme FMO1
0.013
demeton-O
-
pH 9.0, isozyme FMO1
0.25
demeton-O
-
pH 9.0, isozyme FMO3
0.101
ethiofencarb
-
pH 9.0, isozyme FMO1
1.45
ethiofencarb
-
pH 9.0, isozyme FMO3
0.105
Ethionamide
37°C, isozyme FMO1
0.105
Ethionamide
isozyme FMO1, at pH 9.5 and 37°C
0.261
Ethionamide
37°C, isozyme FMO2
0.261
Ethionamide
isozyme FMO2, at pH 9.5 and 37°C
0.336
Ethionamide
37°C, isozyme FMO3
0.0502
ethylenethiourea
-
recombinant mutant K416N, pH 8.5
0.0557
ethylenethiourea
-
recombinant wild-type enzyme, pH 8.5
0.0761
ethylenethiourea
-
recombinant mutant E24D, pH 8.5
0.145
fenthion
-
wild-type enzyme, FMO3
0.15
fenthion
-
mutant enzyme D132H, FMO3
0.2
fenthion
-
mutant enzyme K158L, FMO3
0.22
fenthion
-
mutant enzyme K158L/D132H, FMO3
0.24
fenthion
-
mutant enzyme I303T, FMO1
0.3
fenthion
-
mutant enzyme R502X, FMO1
0.32
fenthion
-
mutant enzyme H97Q, FMO1
0.34
fenthion
-
wild-type enzyme, FMO1
0.351
fenthion
-
mutant enzyme I303V, FMO1
0.0078
imipramine
-
37°C
0.014
imipramine
-
mutant enzyme I303T, FMO1
0.014
imipramine
-
wild-type enzyme, FMO1
0.015
imipramine
-
mutant enzyme H97Q, FMO1
0.016
imipramine
-
mutant enzyme R502X, FMO1
0.02
imipramine
-
mutant enzyme I303V, FMO1
6.5
L-methionine
-
recombinant FMO3, pH 7.4, 37°C
10
L-methionine
-
above, recombinant FMO4, pH 7.4, 37°C
0.018
mercaptoimidazole
-
pH 8.4, 37°C, recombinant wild-type His6-tagged MBT-fusion-FMO3
0.02
mercaptoimidazole
-
pH 8.4, 37°C, recombinant mutant H360P His6-tagged MBT-fusion-FMO1
0.022
mercaptoimidazole
-
pH 8.4, 37°C, recombinant mutant L360Q His6-tagged MBT-fusion-FMO3
0.03
mercaptoimidazole
-
pH 8.4, 37°C, recombinant wild-type His6-tagged MBT-fusion-FMO1
0.034
mercaptoimidazole
-
pH 8.4, 37°C, recombinant mutant L360P His6-tagged MBT-fusion-FMO3
0.038
mercaptoimidazole
-
pH 8.4, 37°C, recombinant mutant L360H His6-tagged MBT-fusion-FMO3
0.046
mercaptoimidazole
-
pH 8.4, 37°C, recombinant mutant L360A His6-tagged MBT-fusion-FMO3
0.007
Methimazole
-
mutant enzyme I303V, FMO1
0.007
Methimazole
-
wild-type enzyme, FMO1
0.0081
Methimazole
9.5, 37°C, FMO1
0.014
Methimazole
-
mutant enzyme H97Q, FMO1
0.016
Methimazole
-
mutant enzyme I303T, FMO1
0.0293
Methimazole
9.5, 37°C, FMO3
0.0718
Methimazole
-
recombinant wild-type enzyme, pH 8.5
0.0773
Methimazole
-
recombinant mutant K416N, pH 8.5
0.0854
Methimazole
-
recombinant mutant E24D, pH 8.5
0.1233
Methimazole
-
recombinant mutant N61K, pH 8.5
0.5758
Methimazole
9.5, 37°C, FMO2.1
0.0048
methyl p-tolyl sulfide
pH 9.0, 37°C, mutant N413K
0.005
methyl p-tolyl sulfide
pH 9.0, 37°C, mutant S195L
0.0135
methyl p-tolyl sulfide
pH 9.0, 37°C, wild-type FMO2.1
0.2
methyl p-tolyl sulfide
-
mutant enzyme R502X, FMO1
0.245
methyl p-tolyl sulfide
-
mutant enzyme I303T, FMO1
0.251
methyl p-tolyl sulfide
-
mutant enzyme H97Q, FMO1
0.284
methyl p-tolyl sulfide
-
wild-type enzyme, FMO1
0.3
methyl p-tolyl sulfide
-
mutant enzyme I303V, FMO1
0.0445
N,N-dimethylamphetamine
pH 7.4, 37°C, FMO1
0.261
N,N-dimethylamphetamine
pH 7.4, 37°C, FMO3
0.0068
NADPH
pH 9.0, 37°C, mutant N413K
0.0115
NADPH
pH 9.0, 37°C, wild-type FMO2.1
0.132
NADPH
pH 9.0, 37°C, mutant S195L
0.0665
sulindac
-
recombinant mutant K416N, pH 8.5
0.0693
sulindac
-
pH 9.0, 37°C
0.1208
sulindac
-
recombinant mutant E24D, pH 8.5
0.1501
sulindac
-
recombinant wild-type enzyme, pH 8.5
0.2071
sulindac
-
recombinant mutant N61K, pH 8.5
0.005
tamoxifen
-
pH and temperature not specified in the publication
0.043
tamoxifen
-
pH 8.5, 37°C, recombinant isozyme FMO1 and recombinant mutant isozyme FMO3 E158K
0.121
tamoxifen
-
pH 8.5, 37°C, recombinant wild-type isozyme FMO3
0.0058
thiacetazone
9.5, 37°C, FMO2.1
0.0063
thiacetazone
9.5, 37°C, FMO1
0.007
thiacetazone
9.5, 37°C, FMO3
0.0209
trimethylamine
-
recombinant wild-type enzyme, pH 8.5
0.0228
trimethylamine
-
recombinant mutant E24D, pH 8.5
0.0373
trimethylamine
-
recombinant mutant K416N, pH 8.5
3
voriconazole
-
pH 7.4, 37°C, recombinant FMO1
3.4
voriconazole
-
pH 7.4, 37°C, recombinant FMO3
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten kinetics, potentiometric titrations of the flavin cofactor of FMO3 and the calculated reduction potentials for full-length wild-type and polymorphic variants of FMO3 and that of the truncated form of the wild-type
-
additional information
additional information
-
Michaelis-Menten kinetics, potentiometric titrations of the flavin cofactor of FMO3 and the calculated reduction potentials for full-length wild-type and polymorphic variants of FMO3 and that of the truncated form of the wild-type
-
additional information
additional information
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
comparison of kinetics of recombinant isozymes FMO1 and FMO3
-
additional information
additional information
-
kinetics of wild-type and mutant structural variants
-
additional information
additional information
MichaelisMenten kinetics
-
additional information
additional information
-
MichaelisMenten kinetics
-
additional information
additional information
-
the recombinant enzyme exhibuts Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic analysis of commercial recombinant enzymes and recombinant MBP-FMOs expressed in Escherichia coli, overview
-
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A52T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
D132H
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows substrate-dependent reduced activity
D198E
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E24D
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
E305X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E314X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E32K
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E362Q
naturally occuring single nucleotide polymorphism of FMO3
G148X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
G180V
naturally occuring single nucleotide polymorphism of FMO3, the mutant is similar to the wild-type enzyme
G475D
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
G503R
naturally occuring single nucleotide polymorphism of FMO3
I199T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
I37T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
I468M
naturally occuring single nucleotide polymorphism of FMO3
K416N
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
M260V
naturally occuring single nucleotide polymorphism of FMO3
M434I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
M66I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
M82T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
N114S
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
Q470X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R223Q
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R238P
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R378L
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R500X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R51G
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
T201K
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
V143E
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
V277A
naturally occuring single nucleotide polymorphism of FMO3
V58I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
W388X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
C530L
naturally occuring single nucleotide polymorphism of FMO2
D227K
pKa value 7.3 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
D36G
naturally occuring single nucleotide polymorphism of FMO2
down
-
FMO5 is downregulated in type II diabetes in liver. FMO1 downregulation and inhibition by 3,3'-diindolylmethane
E132H
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E132H/E158K
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K/T201K/E308G
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K/V257M
-
the naturally occuring polymorphisms reduce the oxidation and clearance of FMO3 substrates such as tyramine, and TMA in vitro, and mutations are highly likely to eliminate the enzyme function in vivo
E24D
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview, the mutant shows altered substrate specificity compared to the wild-type mutant
E314G
naturally occuring single nucleotide polymorphism of FMO2
E339Q
naturally occuring single nucleotide polymorphism of FMO4
F182S
naturally occuring single nucleotide polymorphism of FMO2
F510X
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
F69Y
naturally occuring single nucleotide polymorphism of FMO2
F81S
naturally occuring single nucleotide polymorphism of FMO2
G182E
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
H360P
-
site-directed mutagenesis of isozyme FMO1, the mutant shows altered thermal stability and highly increased activity with mercaptoimidazole and chlorpromazine compared to the wild-type FMO1
I37T
naturally occuring single nucleotide polymorphism of FMO4
K158L
-
Km-value for fenthion is 1.4fold higher than the wild-type value, Vmax for fenthion is nearly identical to the wild-type value, mutant of FMO3
K158L/D132H
-
Km-value for fenthion is 1.5fold higher than the wild-type value, Vmax for fenthion is 1.5fold higher than the wild-type value, mutant of FMO3
K416N
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview, the mutant shows altered substrate specificity compared to the wild-type mutant
L360A
-
site-directed mutagenesis of isozyme FMO3, the mutant shows altered thermal stability and reduced activity with mercaptoimidazole, chlorpromazine, and 10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine compared to the wild-type FMO3
L360H
-
site-directed mutagenesis of isozyme FMO3, the mutant shows altered thermal stability and reduced activity with mercaptoimidazole, chlorpromazine, and 10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine compared to the wild-type FMO3
L360Q
-
site-directed mutagenesis of isozyme FMO3, the mutant shows altered thermal stability and reduced activity with mercaptoimidazole, chlorpromazine, and 10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine compared to the wild-type FMO3
M66I
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
N61K
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview, the mutant shows altered substrate specificity compared to the wild-type mutant
N61S
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
P153L
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
P457L
naturally occuring single nucleotide polymorphism of FMO4
Q170K
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
Q206H
pKa value 6.5 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
R205C
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3, and is almost substrate inhibited, wild-type FMO3 has no free cysteine residues in the native form
R223Q
naturally occuring single nucleotide polymorphism of FMO1
R238Q
naturally occuring single nucleotide polymorphism of FMO2
R249X
naturally occuring single nucleotide polymorphism of FMO2, probably inactive mutant
R391T
naturally occuring single nucleotide polymorphism of FMO2
R492W
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
R502V
-
no activity with methimazole, KM-value for methyl p-tolyl sulfide is 70% of the wild-type value, Vmax with methyl p-tolyl sulfide is 70% of the wild-type value, KM-value for imipramine is is nearly identical to the the wild-type value, Vmax with imipramine is 49% of the wild-type value, KM-value for fenthion is 88% of the wild-type value, Vmax with fenthion is 55% of wild-type value, mutant of FMO1
R506S
naturally occuring single nucleotide polymorphism of FMO4
T308S
naturally occuring single nucleotide polymorphism of FMO4
V257M/E308G
-
naturally occuring polymorphism, the substitutions do not affect enzyme activity in vitro
V257M/M260V
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
V323A
naturally occuring single nucleotide polymorphism of FMO4
Y228H
pKa value 7.9 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
E158K
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
E158K
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation slightly affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
E158K
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly affects enzyme activity, substrate-dependent reduced activity
E158K
the mutant shows moderately reduced activity
E158K
naturally occuring mutation and site-directed mutagenesis, the mutant exhibits a significant increase in all the kinetic parameters measured with substrate tamoxifen with nearly two times faster clearance. The mutation has no effect on the clearance of GSK5182
E158K
naturally occuring polymorphic variant and site-directed mutagenesis, the melting temperature and activation energy of the mutant is nearly unaltered compared to the wild-type enzyme
E158K
naturally occuring polymorphism of FMO3, the E158K variant is mostly expressed in African-American and Europeans, the mutant shows reduced activity compared to the wild-type enzyme
E158K/E308G
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
E158K/E308G
naturally occuring single nucleotide polymorphism of FMO3, the mutation affects enzyme activity, substrate-dependent reduced activity
E308G
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
E308G
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation slightly affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
E308G
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly affects enzyme activity, substrate-dependent reduced activity
E308G
the mutant shows moderately reduced activity
E308G
naturally occuring mutation and site-directed mutagenesis, the mutant exhibits a significant increase in all the kinetic parameters measured with substrate clomiphene with nearly two times faster clearance. The mutation has no effect on the clearance of GSK5182
E308G
naturally occuring polymorphic variant and site-directed mutagenesis, the mutant is unable to bind the NADP+ cofactor, it shows a significantly higher energy of unfolding (Ea) compared to wild-type
E308G
naturally occuring polymorphism of FMO3, the E308G is widely distributed in Asians and Europeans, the mutant shows reduced activity compared to the wild-type enzyme
L360P
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows increased activity
L360P
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows increased activity
L360P
the mutation increases catalytic activity
N61K
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
N61K
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
N61S
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, nuta this mutant is still active with methimazole, phenotype, overview
N61S
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, nuta this mutant is still active with methimazole, phenotype, overview
N61S
an active site polymorphic variant, the single-nucleotide polymorphism is leading to deleterious effects of oxidative stress. N-Oxygenation of benzydamine by the wild-type and N61S mutant variant of FMO3. In the absence of the substrate benzydamine (BZD), N61S produces higher amounts of H2O2 compared to wild-type
P153L
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
P153L
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R205C
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
R205C
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows highly reduced activity
R205C
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
V257M
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
V257M
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows slightly reduced activity
V257M
naturally occuring mutation and site-directed mutagenesis, residue V257 is not in the immediate vicinity of the active site and is part of the hFMO3 insert region in a loop that protrudes from the NADP+-binding domain across the FAD-binding domain, the mutant exhibits a significant increase in all the kinetic parameters measured with substrate clomiphene with nearly two times faster clearance, while the clearance with substrate tamoxifen is reduced. The mutation has no effect on the clearance of GSK5182
V257M
naturally occuring polymorphic variant and site-directed mutagenesis, the melting temperature and activation energy of the mutant is nearly unaltered compared to the wild-type enzyme
V257M
naturally occuring polymorphism of FMO3, the V257M polymorphic variant is predominantly present in Asians, the mutant shows reduced activity compared to the wild-type enzyme
D132H
-
KM-value and Vmax of fenthion are nearly identical to the wild-type values, mutant of FMO3
D132H
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K
-
major naturally occuring structural varainat of isozyme FMO3, the mutant shows increased activity with tamoxifen compared to the wild-type enzyme
E158K
-
natural genetic variant of isozymes FMO2 and FMO3, substrate specificity, overview
E158K
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E158K
-
naturally occuring mutation not involved in primary trimethylaminuria
E158K/E308G
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K/E308G
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K/E308G
-
naturally occuring polymorphism, in many cases in vivo, altered clinical responses or altered susceptibility to various chemicals due to these sequence variants are observed compared to the carriers of at least one wild-type allele
E158K/E308G
-
naturally occuring mutation not involved in primary trimethylaminuria
E308G
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E308G
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E308G
-
naturally occuring mutation not involved in primary trimethylaminuria
H97Q
-
KM-value for methimazole is 3fold higher than wild-type value, Vmax with methimazole is 1.6fold higher than the wild-type value, KM-value for methyl p-tolyl sulfide is 88% of the wild-type value, Vmax with methyl p-tolyl sulfide is 1.4fold higher than the wild-type value, KM-value for imipramine is is nearly identical to the the wild-type value, Vmax with imipramine is 1.3fold higher than the wild-type value, KM-value for fenthion is 94% of the wild-type value, Vmax with fenthion is 1.3fold higher than the wild-type value, mutant of FMO1
H97Q
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
H97Q
naturally occuring single nucleotide polymorphism of FMO1, the mutant enzyme is similar to the wild-type enzyme
I303T
-
KM-value for methimazole is 2.3fold higher than wild-type value, Vmax with methimazole is 1.8fold higher than the wild-type value, KM-value for methyl p-tolyl sulfide is 86% of the wild-type value, Vmax with methyl p-tolyl sulfide is 1.8fold higher than the wild-type value, KM-value for imipramine is identical to the the wild-type value, Vmax with imipramine is 1.4fold higher than the wild-type value, KM-value for fenthion is 94% of the wild-type value, Vmax with fenthion is 1.6fold higher than the wild-type value, mutant of FMO1
I303T
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
I303T
naturally occuring single nucleotide polymorphism of FMO1, the mutant enzyme is similar to the wild-type enzyme
I303V
-
KM-value for methimazole is identical to the wild-type value, Vmax with methimazole is nearly identical to the wild-type value, KM-value and Vmax for meth is 1,4fold higher than the the wild-type value, Vmax with imipramine is nearly identical to the wild-type value, KM-value and Vmax for fenthion are nearly identical to the wild-type values, mutant of FMO1
I303V
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
I303V
naturally occuring single nucleotide polymorphism of FMO1, the mutant enzyme is similar to the wild-type enzyme
L360P
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
L360P
-
site-directed mutagenesis of isozyme FMO3, the mutant shows altered thermal stability and increased activity with mercaptoimidazole, chlorpromazine, and 10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine compared to the wild-type FMO3
N413K
naturally occuring single nucleotide polymorphism of FMO2, the mutant is similar to the wild-type enzyme
N413K
naturally occuring mutant of the FMO2*1 allele, the mutant shows higher kcat and Vmax, and increased thermosensitivity compared to the wild-type enzyme, activity is stabilized by NADPH
N413K
-
the mutant of isoform FMO2 exhibits higher catalytic activity toward methyl-4-tolyl sulfide compared to the wild type enzyme
Q472X
naturally occuring single nucleotide polymorphism of FMO2, inactive mutant
Q472X
naturally occuring single nucleotide polymorphism of FMO2, inactive mutant
Q472X
naturally occuring mutant of the FMO2*1 allele, more frequent in the sub-Sahara African population
R502X
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
R502X
naturally occuring single nucleotide polymorphism of FMO1, the mutant shows substrate-dependent reduced activity compared to the wild-type enzyme
R502X
naturally occuring single nucleotide polymorphism of FMO1, the mutant shows substrate-dependent reduced activity compared to the wild-type enzyme
S195L
naturally occuring single nucleotide polymorphism of FMO2, inactive mutant
S195L
naturally occuring mutant of the FMO2*1 allele, the mutant shows reduced activity and increased pH sensitivity and thermosensitivity compared to the wild-type enzyme, activity is stabilized by NADPH
S195L
-
the mutant of isoform FMO2 exhibits lower catalytic activity toward methyl-4-tolyl sulfide and ethylene thiourea compared to the wild type enzyme
V257M
-
variant with 13.21% allele frequency. Mutation causes a transformation of the secondary structure. The presence of this mutant allele correlates significantly with a reduction in caffeine N-1-demethylating activity
V257M
-
natural genetic variant of isozyme FMO3, substrate specificity, overview
V257M
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
V257M
-
naturally occuring mutation not involved in primary trimethylaminuria
additional information
FMO3 is highly polymorphic, with as many as 15 nonsynonymous single nucleotide polymorphisms identified, many of which are present at relatively high frequency, several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
FMO3 is highly polymorphic, with as many as 15 nonsynonymous single nucleotide polymorphisms identified, many of which are present at relatively high frequency, several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
FMO3 is highly polymorphic, with as many as 15 nonsynonymous single nucleotide polymorphisms identified, many of which are present at relatively high frequency, several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
-
FMO3 is highly polymorphic, with as many as 15 nonsynonymous single nucleotide polymorphisms identified, many of which are present at relatively high frequency, several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
genotyping of FMO3 in a Japanese cohort, missense and nonsense mutations, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
-
several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
the HepG2 model is suitable for the study of FMO3 regulation, deletion analysis of FMO3/luciferase reporter constructs, domains A-I, and specific transcription factor responsive elements identified by DNA-protein binding reactions and site-directed mutagenesis of FMO3 reporter constructs, functional analysis of the FMO3 HNF3, and C/EBP elements, FMO3 promoter analysis, overview
additional information
-
the HepG2 model is suitable for the study of FMO3 regulation, deletion analysis of FMO3/luciferase reporter constructs, domains A-I, and specific transcription factor responsive elements identified by DNA-protein binding reactions and site-directed mutagenesis of FMO3 reporter constructs, functional analysis of the FMO3 HNF3, and C/EBP elements, FMO3 promoter analysis, overview
additional information
generation of humanized-liver TK-NOG mice, chimeric mice, in which more than 90% of liver cells are estimated to have been replaced with human hepatocytes, interactions between FMO substrates in humanized-liver mice, overview. Administered itopride (10 mg/kg) is extensively oxygenated to its N-oxide in humanized-liver mouse plasma. The area under the concentration-time curve of itopride N-oxide is 15fold that of itopride in humanize-liver mice
additional information
generation of truncated forms of wild-type and mutant enzymes, the 17 amino acid truncation at the C-terminal of FMO3 results in a more soluble protein, the truncated enzymes are better catalysts than the full-length proteins. The truncated enzymes are not only fully active, but also have a higher vmax compared to their full-length counterparts, the latter observation might be the result of their higher solubility. The mutations have no major effect on the interaction of the FAD cofactor with the protein
additional information
-
generation of truncated forms of wild-type and mutant enzymes, the 17 amino acid truncation at the C-terminal of FMO3 results in a more soluble protein, the truncated enzymes are better catalysts than the full-length proteins. The truncated enzymes are not only fully active, but also have a higher vmax compared to their full-length counterparts, the latter observation might be the result of their higher solubility. The mutations have no major effect on the interaction of the FAD cofactor with the protein
additional information
unfolding process of a phase I drug metabolizing enzyme, human flavin-containing monooxygenase 3 (hFMO3) and its single nucleotide polymorphic variants (SNPs) V257M, E158K and E308G are analyzed by differential scanning calorimetry (DSC) indicating that the thermal denaturation of the enzyme is irreversible. The melting temperature (Tm) for the wild-type enzyme and its polymorphic variants is in a range from 46°C to 50°C. Also the activation energies of unfolding (Ea) show no significant differences among all proteins investigated (290-328 KJ/mol), except for the E308G variant that shows a significantly higher Ea of 412 KJ/mol. The presence of the bound NADP+ cofactor stabilizes all the variants by shifting the main Tm by 4-5°C for all the proteins, exception made for E308G where no changes are observed
additional information
-
unfolding process of a phase I drug metabolizing enzyme, human flavin-containing monooxygenase 3 (hFMO3) and its single nucleotide polymorphic variants (SNPs) V257M, E158K and E308G are analyzed by differential scanning calorimetry (DSC) indicating that the thermal denaturation of the enzyme is irreversible. The melting temperature (Tm) for the wild-type enzyme and its polymorphic variants is in a range from 46°C to 50°C. Also the activation energies of unfolding (Ea) show no significant differences among all proteins investigated (290-328 KJ/mol), except for the E308G variant that shows a significantly higher Ea of 412 KJ/mol. The presence of the bound NADP+ cofactor stabilizes all the variants by shifting the main Tm by 4-5°C for all the proteins, exception made for E308G where no changes are observed
additional information
-
determination and analysis of frequencies of 18 FMO3 single-nucleotide polymorphisms in 202 Hispanics of Mexican descent, 201 African Americans, and 200 non-Latino whites, synonymous mutations, and hypomorphic haplotypes, overview
additional information
-
effects of genetic variants of isozyme FMO3 on N- and S-oxygenation activities, genotype-phenotype studies, overview
additional information
-
identification and analysis of 18 mutations of FMO3 genes from 134 AfricanAmericans and 129 Caucasians from the United States, missense and nonsense nucleotide substitutions, and polymorphic variants of the gene, both involved in development of trimethylaminuria, TMAU, interindividual variability in the expression of FMO3 may affect drug and exogenous chemical metabolism in the liver and other tissues, clinical relevance of the polymorphisms, overview
additional information
-
occuring single nucleotide polymorphisms are associated with dramatic functional differences in selective functional enzyme activity, overview
additional information
-
three of the five expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms, overview
additional information
most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
additional information
most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
additional information
most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
additional information
-
most humans are homozygous for a nonsense mutation that inactivates FMO2. But a substantial proportion of sub-Saharan Africans express functional FMO2 and, thus, are predicted to respond differently to drugs and other foreign chemicals
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview
additional information
-
enzyme activity analysis using a simple but functional and stable enzyme-electrode system based on a glassy carbon electrode with human flavin-containing monooxygenase isoform 3 entrapped in a gel cross-linked with bovine serum albumin by glutaraldehyde, method development and evaluation, overview
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Homo sapiens
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Krueger, S.K.; Vandyke, J.E.; Williams, D.E.; Hines, R.N.
The role of flavin-containing monooxygenase (FMO) in the metabolism of tamoxifen and other tertiary amines
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Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
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Enzyme-mediated protein haptenation of dapsone and sulfamethoxazole in human keratinocytes: II. Expression and role of flavin-containing monooxygenases and peroxidases
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Homo sapiens (Q01740)
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Koukouritaki, S.B.; Poch, M.T.; Henderson, M.C.; Siddens, L.K.; Krueger, S.K.; VanDyke, J.E.; Williams, D.E.; Pajewski, N.M.; Wang, T.; Hines, R.N.
Identification and functional analysis of common human flavin-containing monooxygenase 3 genetic variants
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Homo sapiens
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Zhou, J.; Shephard, E.A.
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Homo sapiens
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Oryctolagus cuniculus, Homo sapiens, Mus musculus, Sus scrofa
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Yeung, C.K.; Adman, E.T.; Rettie, A.E.
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
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Homo sapiens
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Shephard, E.A.; Chandan, P.; Stevanovic-Walker, M.; Edwards, M.; Phillips, I.R.
Alternative promoters and repetitive DNA elements define the species-dependent tissue-specific expression of the FMO1 genes of human and mouse
Biochem. J.
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Mus musculus (P50285), Mus musculus, Homo sapiens (Q01740), Homo sapiens
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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.
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2008
Homo sapiens (P31513), Homo sapiens
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Phillips, I.R.; Francois, A.A.; Shephard, E.A.
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Curr. Pharmacogenomics
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2007
Homo sapiens (P31512), Homo sapiens (P31513), Homo sapiens (P49326), Homo sapiens (Q01740), Homo sapiens (Q99518)
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brenda
Kousba, A.; Soll, R.; Yee, S.; Martin, M.
Cyclic conversion of the novel Src kinase inhibitor [7-(2,6-dichloro-phenyl)-5-methyl-benzo[1,2,4]triazin-3-yl]-[4-(2-pyrrolidin-1-yl-ethoxy)-phenyl]-amine (TG100435) and Its N-oxide metabolite by flavin-containing monoxygenases and cytochrome P450 reduct
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Homo sapiens
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Yanni, S.B.; Annaert, P.P.; Augustijns, P.; Bridges, A.; Gao, Y.; Benjamin, D.K.; Thakker, D.R.
Role of flavin-containing monooxygenase in oxidative metabolism of voriconazole by human liver microsomes
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Homo sapiens
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Shimizu, M.; Tomioka, S.; Murayama, N.; Yamazaki, H.
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2007
Homo sapiens (P31513)
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Allerston, C.K.; Shimizu, M.; Fujieda, M.; Shephard, E.A.; Yamazaki, H.; Phillips, I.R.
Molecular evolution and balancing selection in the flavin-containing monooxygenase 3 gene (FMO3)
Pharmacogenet. Genomics
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2007
Homo sapiens (P31513), Homo sapiens
brenda
Phillips, I.R.; Shephard, E.A.
Flavin-containing monooxygenases: mutations, disease and drug response
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2008
Saccharomyces cerevisiae, Homo sapiens (P31513), Homo sapiens (Q01740), Homo sapiens (Q99518), Homo sapiens
brenda
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Flavin mono-oxygenase (FMO) - The other oxidase
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2008
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Francois, A.A.; Nishida, C.R.; de Montellano, P.R.; Phillips, I.R.; Shephard, E.A.
Human flavin-containing monooxygenase 2.1 catalyzes oxygenation of the antitubercular drugs thiacetazone and ethionamide
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2009
Homo sapiens (Q01740), Homo sapiens
brenda
Krueger, S.K.; Henderson, M.C.; Siddens, L.K.; VanDyke, J.E.; Benninghoff, A.D.; Karplus, P.A.; Furnes, B.; Schlenk, D.; Williams, D.E.
Characterization of sulfoxygenation and structural implications of human flavin-containing monooxygenase isoform 2 (FMO2.1) variants S195L and N413K
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2009
Homo sapiens (Q99518), 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
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1987-1990
2009
Canis lupus familiaris, Homo sapiens
brenda
Cashman, J.R.; Zhang, J.; Nelson, M.R.; Braun, A.
Analysis of flavin-containing monooxygenase 3 genotype data in populations administered the anti-schizophrenia agent olanzapine
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2008
Homo sapiens (P31513), Homo sapiens
brenda
Hai, X.; Adams, E.; Hoogmartens, J.; Van Schepdael, A.
Enantioselective in-line and off-line CE methods for the kinetic study on cimetidine and its chiral metabolites with reference to flavin-containing monooxygenase genetic isoforms
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2009
Homo sapiens
brenda
Novick, R.M.; Mitzey, A.M.; Brownfield, M.S.; Elfarra, A.A.
Differential localization of flavin-containing monooxygenase (FMO) isoforms 1, 3, and 4 in rat liver and kidney and evidence for expression of FMO4 in mouse, rat, and human liver and kidney microsomes
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Homo sapiens, Homo sapiens (P31512), Mus musculus, Rattus norvegicus (P36365), Rattus norvegicus (Q8K4B7), Rattus norvegicus (Q9EQ76)
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
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2008
Homo sapiens, Homo sapiens (Q01740), Homo sapiens (Q99518), Mus musculus, Mus musculus (P50285), Mus musculus (Q8K2I3)
brenda
Lee, S.K.; Kang, M.J.; Jin, C.; In, M.K.; Kim, D.H.; Yoo, H.H.
Flavin-containing monooxygenase 1-catalysed N,N-dimethylamphetamine N-oxidation
Xenobiotica
39
680-686
2009
Homo sapiens (Q01740), Homo sapiens
brenda
Castrignano, S.; Sadeghi, S.J.; Gilardi, G.
Electro-catalysis by immobilised human flavin-containing monooxygenase isoform 3 (hFMO3)
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Homo sapiens
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Driscoll, J.P.; Aliagas, I.; Harris, J.J.; Halladay, J.S.; Khatib-Shahidi, S.; Deese, A.; Segraves, N.; Khojasteh-Bakht, S.C.
Formation of a quinoneimine intermediate of 4-fluoro-N-methylaniline by FMO1: carbon oxidation plus defluorination
Chem. Res. Toxicol.
23
861-863
2010
Homo sapiens
brenda
Reddy, R.R.; Ralph, E.C.; Motika, M.S.; Zhang, J.; Cashman, J.R.
Characterization of human flavin-containing monooxygenase (FMO) 3 and FMO5 expressed as maltose-binding protein fusions
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2010
Homo sapiens
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.
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Homo sapiens (Q01740), 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
Rattus norvegicus, Homo sapiens (Q01740), Homo sapiens (Q9HA79), Homo sapiens
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Motika, M.S.; Zhang, J.; Ralph, E.C.; Dwyer, M.A.; Cashman, J.R.
pH dependence on functional activity of human and mouse flavin-containing monooxygenase 5
Biochem. Pharmacol.
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2012
Homo sapiens (P49326), Homo sapiens, Mus musculus (P97872), Mus musculus
brenda
Catucci, G.; Polignano, I.; Cusumano, D.; Medana, C.; Gilardi, G.; Sadeghi, S.J.
Identification of human flavin-containing monooxygenase 3 substrates by a colorimetric screening assay
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Homo sapiens
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Huijbers, M.; Montersino, S.; Westphal, A.; Tischler, D.; Van Berkel, W.
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2014
Homo sapiens
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Siddens, L.K.; Krueger, S.K.; Henderson, M.C.; Williams, D.E.
Mammalian flavin-containing monooxygenase (FMO) as a source of hydrogen peroxide
Biochem. Pharmacol.
89
141-147
2014
Homo sapiens
brenda
Phillips, I.R.; Francois, A.A.; Shephard, E.A.
The flavin-containing monooxygenases (FMOs) genetic variation and its consequences for the metabolism of therapeutic drugs
Curr. Pharmacogenomics
5
292-313
2007
Homo sapiens
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brenda
Fennema, D.; Phillips, I.R.; Shephard, E.A.
Trimethylamine and trimethylamine N-oxide, a flavin-containing monooxygenase 3 (FMO3)-mediated host-microbiome metabolic axis implicated in health and disease
Drug Metab. Dispos.
44
1839-1850
2016
Homo sapiens (P31513)
brenda
Taniguchi-Takizawa, T.; Shimizu, M.; Kume, T.; Yamazaki, H.
Benzydamine N-oxygenation as an index for flavin-containing monooxygenase activity and benzydamine N-demethylation by cytochrome P450 enzymes in liver microsomes from rats, dogs, monkeys, and humans
Drug Metab. Pharmacokinet.
30
64-69
2015
Canis lupus familiaris, Macaca fascicularis, Homo sapiens, Rattus norvegicus
brenda
Phillips, I.R.; Shephard, E.A.
Drug metabolism by flavin-containing monooxygenases of human and mouse
Expert. Opin. Drug Metab. Toxicol.
13
167-181
2017
Homo sapiens, Mus musculus
brenda
Liao, B.M.; McManus, S.A.; Hughes, W.E.; Schmitz-Peiffer, C.
Flavin-containing monooxygenase 3 reduces endoplasmic reticulum stress in lipid-treated hepatocytes
Mol. Endocrinol.
30
417-428
2016
Homo sapiens, Mus musculus
brenda
Fu, C.W.; Lin, T.H.
Predicting the metabolic sites by flavin-containing monooxygenase on drug molecules using SVM classification on computed quantum mechanics and circular fingerprints molecular descriptors
PLoS ONE
12
e0169910
2017
Homo sapiens
brenda
El-Serafi, I.; Terelius, Y.; Abedi-Valugerdi, M.; Naughton, S.; Saghafian, M.; Moshfegh, A.; Mattsson, J.; Potacova, Z.; Hassan, M.
Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway
PLoS ONE
12
e0187294
2017
Homo sapiens, Mus musculus
brenda
Bortolussi, S.; Catucci, G.; Gilardi, G.; Sadeghi, S.J.
N- and S-oxygenation activity of truncated human flavin-containing monooxygenase 3 and its common polymorphic variants
Arch. Biochem. Biophys.
697
108663
2021
Homo sapiens (P31513), Homo sapiens
brenda
Catucci, G.; Bortolussi, S.; Rampolla, G.; Cusumano, D.; Gilardi, G.; Sadeghi, S.J.
Flavin-containing monooxygenase 3 polymorphic variants significantly affect clearance of tamoxifen and clomiphene
Basic Clin. Pharmacol. Toxicol.
123
687-691
2018
Homo sapiens (P31513), Homo sapiens
brenda
Cheropkina, H.; Catucci, G.; Marucco, A.; Fenoglio, I.; Gilardi, G.; Sadeghi, S.
Human flavin-containing monooxygenase 1 and its long-sought hydroperoxyflavin intermediate
Biochem. Pharmacol.
193
114763
2021
Homo sapiens (Q01740), Homo sapiens
brenda
Veeravalli, S.; Phillips, I.R.; Freire, R.T.; Varshavi, D.; Everett, J.R.; Shephard, E.A.
Flavin-containing monooxygenase 1 catalyzes the production of taurine from hypotaurine
Drug Metab. Dispos.
48
378-385
2020
Homo sapiens, Homo sapiens (Q01740), Mus musculus (P50285)
brenda
Shimizu, M.; Uehara, S.; Suemizu, H.; Yamazaki, H.
In vivo drug interactions of itopride and trimethylamine mediated by flavin-containing monooxygenase 3 in humanized-liver mice
Drug Metab. Pharmacokinet.
37
100369
2021
Homo sapiens (P31513)
brenda
Taniguchi-Takizawa, T.; Kato, N.; Shimizu, M.; Kume, T.; Yamazaki, H.
Different substrate elimination rates of model drugs pH-dependently mediated by flavin-containing monooxygenases and cytochromes P450 in human liver microsomes
Drug Metab. Pharmacokinet.
40
100412
2021
Homo sapiens (P31513), Homo sapiens
brenda
Catucci, G.; Gao, C.; Rampolla, G.; Gilardi, G.; Sadeghi, S.J.
Uncoupled human flavin-containing monooxygenase 3 releases superoxide radical in addition to hydrogen peroxide
Free Radic. Biol. Med.
145
250-255
2019
Homo sapiens (P31513), Homo sapiens
brenda
Kim, J.; Lee, H.; Roh, Y.J.; Kim, H.U.; Shin, D.; Kim, S.; Son, J.; Lee, A.; Kim, M.; Park, J.; Hwang, S.Y.; Kim, K.; Lee, Y.K.; Jung, H.S.; Hwang, K.Y.; Lee, B.C.
Structural and kinetic insights into flavin-containing monooxygenase and calponin-homology domains in human MICAL3
IUCrJ
7
90-99
2020
Homo sapiens (P31513), Homo sapiens
brenda
Matsumoto, K.; Hasegawa, T.; Ohara, K.; Kamei, T.; Koyanagi, J.; Akimoto, M.
Role of human flavin-containing monooxygenase (FMO) 5 in the metabolism of nabumetone Baeyer-Villiger oxidation in the activation of the intermediate metabolite, 3-hydroxy nabumetone, to the active metabolite, 6-methoxy-2-naphthylacetic acid in vitro
Xenobiotica
51
155-166
2021
Homo sapiens (P49326), Homo sapiens
brenda