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Enzyme Nomenclature
Information on EC 1.14.13.8 - flavin-containing monooxygenase
Word Map on EC 1.14.13.8
- 1.14.13.8
- hepatic
- methimazole
-
xenobiotics
- trimethylamine
-
n-oxygenation
- sulfoxide
-
s-oxidation
-
trimethylaminuria
-
nadph-dependent
-
n-demethylation
- phenobarbital
- n-octylamine
- thioureas
-
cdna-expressed
- cyp3a4
- thiobenzamide
- metyrapone
-
drug-metabolizing
-
odor
- cyp2d6
- benzydamine
- imipramine
-
p-450-dependent
- cyp2c19
-
detoxication
- 3-methylcholanthrene
- 1-aminobenzotriazole
-
baeyer-villiger
-
nitrone
-
monooxygenation
- benzphetamine
-
prochiral
- yucca
-
n-hydroxylation
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.13.8
-
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RECOMMENDED NAME
GeneOntology No.
flavin-containing monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
ordered ter-bi mechanism with an irreversible step between the second and third substrate, NADPH is added first, followed by O2 and the oxidizable organic substrate last
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
reaction mechanism of S-oxygenation of N-substituted thioureas
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
reaction mechanism of S-oxygenation of N-substituted thioureas
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic reaction mechanism, structure-function relationship, FMO oxygenates soft nucleophiles, and converts lipophilic compounds into more hydrophilic metabolites, the first step for FMO is reduction of the FAD by NADPH, the next step is formation of a C4a-hydroperoxy flavin by addition of molecular oxygen to the reduced FAD, when the substrate is accepted by FMO the enzyme is already in an active form, the protein environment of FMO apparently protects the hydroperoxy flavin from decomposing, conserving NADPH, and affording an effcient two-electron oxygenating agent for nucleophiles with the appropriate size and shape
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N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic reaction mechanism via 4alpha-hydroperoxyflavin transient intermediate
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle, reaction mechanism via C4a-hydroperoxyflavin intermediate and structure-function relationship, overview
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle, reaction mechanism and structure-function relationship, overview; catalytic cycle, reaction mechanism and structure-function relationship, overview; catalytic cycle, reaction mechanism and structure-function relationship, overview
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
catalytic cycle, reaction mechanism via C4a-hydroperoxyflavin intermediate and structure-function relationship, overview
-
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
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CAS REGISTRY NUMBER
COMMENTARY
117910-56-2
-
148848-55-9
-
37256-73-8
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
348504, 348508, 348510, 348511, 348512, 658461, 659823, 659829, 659969, 660547, 684678, 686355, 686357, 703320, 703411, 705314, 706824, 710837, 711741, 711837
-
-
Europian-, Latin-, African-, and Asian-American schizophrenia patients
UniProt
isozymes FMO1-FMO5, FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
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FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
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348485, 348486, 348487, 348488, 348490, 348491, 348492, 348494, 348497, 348498, 348499, 348500, 348505, 348507, 659828, 676315, 703320, 712902
-
-
FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
-
FMOs are involved in Phase I metabolism catalyzing the NADPH-dependent oxygenation of drugs, xenobiotics and endogenous compounds containing a soft nucleophilic heteroatom, typically nitrogen or sulfur, but in some cases also selenium or phosphorous
metabolism
-
the enzyme is involved in metabolism of the anti-tuberculosis drug ethionamide in lung and liver, overview
metabolism
the enzyme is involved in metabolism of the anti-tuberculosis drug ethionamide in lung and liver, overview
metabolism
the flavin monooxygenase FMO1 contributes to metabolism of anti-tumor triazoloacridinone, C-1305 (5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one), in liver microsomes and Hep-G2 cells
metabolism
-
the flavin monooxygenase FMO1 contributes to metabolism of anti-tumor triazoloacridinone C-1305 (5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one) in liver microsomes
physiological function
-
FMO3 plays an important role in kidney metabolism of xenobiotics containing sulfur and selenium atoms
physiological function
-
FMO catalyzes the oxidation at nucleophilic, heteroatom centers and is important for drug, xenobiotic, and endogenous substrate metabolism
physiological function
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FMO catalyzes the oxidation at nucleophilic, heteroatom centers and is important for drug, xenobiotic, and endogenous substrate metabolism
physiological function
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the flavin-containing monooxygenase family of enzymes oxygenates nucleophilic xenobiotics and endogenous substances
additional information
-
although maltose-binding-protein-FMO enzymes afford lower rates of turnover than the corresponding commercial recombinant FMOs, both types of FMO show identical substrate dependencies and similar responses to changes in assay conditions. Comparison of commercial recombinant enzymes with recombinant MBP-FMOs expressed in Escherichia coli, overview
additional information
chromatin immunoprecipitation assays do not detect recruitment of aryl hydrocarbon receptor or ARNT to Fmo3 regulatory elements after exposure to 3-methylcholanthrene in liver or in Hepa-1 cells. However, in Hepa-1, 3-methylcholanthrene and benzo[a]pyrene , but not 2,3,7,8-tetrachlorodibenzo-p-dioxin, cause recruitment of p53 protein to a p53 response element in the 5'-flanking region of the Fmo3 gene. Although FMO3 mRNA is highly induced by 3-methylcholanthrene or 2,3,7,8-tetrachlorodibenzo-p-dioxin in mouse liver and in Hepa-1 cells, FMO protein levels and FMO catalytic function show only modest elevation
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
-
(S)-nicotine N-1'-oxygenation
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
1-[4-(methylsulfanyl)phenyl]ethanone + NADPH + H+ + O2
(R,S)-1-[4-(methylsulfanyl)phenyl]ethanone S-oxide + NADP+ + H2O
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
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
-
-
?
2-(methylsulfanyl)pyridine + NADPH + H+ + O2
2-(methylsulfanyl)pyridine S-oxide + NADP+ + H2O
2-(methylsulfanyl)thiophene + NADPH + H+ + O2
2-(methylsulfanyl)thiophene S-oxide + NADP+ + H2O
2-acetylsulfanylmethyl-4-(4-methoxyphenyl)-4-oxobutyric acid + NADPH + H+ + O2
?
-
-
-
-
?
2-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-2-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
2-[(methylsulfanyl)methyl]furan + NADPH + H+ + O2
2-[(methylsulfanyl)methyl]furan S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-[2-(4-methoxyphenyl)-2-oxoethyl]-acrylic acid + NADPH + H+ + O2
?
-
a synthetic 10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl)phenothiazine analogue
-
-
?
3-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-3-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 15% R-enantiomer as product
-
-
?
4-(4-methoxyphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid + NADPH + H+ + O2
?
-
FMO1, poor activity with FMO3 and FMO5
-
-
?
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid + NADPH + H+ + O2
?
-
FMO1 and FMO5, no activity with FMO3
-
-
?
4-(methylsulfanyl)benzonitrile + NADPH + H+ + O2
(R,S)-4-(methylsulfanyl)benzonitrile S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 22% S-enantiomer as product
-
-
?
4-(methylsulfanyl)phenol + NADPH + H+ + O2
(R,S)-4-(methylsulfanyl)phenol S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 81% S-enantiomer as product
-
-
?
4-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-4-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 95% S-enantiomer as product
-
-
?
5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-[[3-(dimethylnitroryl)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-[[3-(dimethylnitroryl)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
benzyl ethyl sulfide + NADPH + H+ + O2
benzyl ethyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
benzyl methyl sulfide + NADPH + H+ + O2
benzyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
butyl ethyl sulfide + NADPH + H+ + O2
butyl ethyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
butyl methyl sulfide + NADPH + H+ + O2
butyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
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
-
-
?
cyclohexyl methyl sulfide + NADPH + H+ + O2
cyclohexyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
disulfoton + NADPH + H+ + O2
?
a thioether-containing organophosphate insecticide
-
-
?
esonarimod + NADPH + H+ + O2
S-methyl esonarimod + NADP+ + H2O
a antirheumatic drug, is converted to the S-oxide
-
-
?
ethyl phenyl sulfide + NADPH + H+ + O2
ethyl phenyl sulfoxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
etionamide + NADPH + H+ + O2
etionamide S-oxide + NADP+ + H2O
-
substrate of FMO1, FMO3, and FMO2.1
-
-
?
K11777 + NADPH + H+ + O2
K11777 N-oxide + NADP+ + H2O
a cysteine protease inhibitor against Trypanosoma cruzi, is converted to the N-oxide
-
-
?
L-methionine + NADPH + H+ + O2
methionine S-oxide + NADP+ + H2O
stereochemistry, overview
formation of 80% D-isomer
-
?
L-Phe-Met + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
-
liver microsomes
-
-
?
mercaptoimidazole + NADPH + H+ + O2
?
-
FMO1 and FMO3, no activity with FMO5
-
-
?
mercaptoimidazole + NADPH + O2
mercaptoimidazole S-oxide + NADP+ + H2O
-
-
-
-
?
methamphetamine + NADPH + H+ + O2
methamphetamine N-oxide + NADP+ + H2O
a psychostimulant, is converted to the hydroxylamine
-
-
?
methyl 2-phenylethyl sulfide + NADPH + H+ + O2
methyl 2-phenylethyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
methyl 4-(methylsulfanyl)phenyl ether + NADPH + H+ + O2
(R,S)-methyl 4-(methylsulfanyl)phenyl ether S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 70% S-enantiomer as product
-
-
?
methyl 4-methylphenyl sulfide + NADPH + H+ + O2
(R,S)-methyl 4-methylphenyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 92% S-enantiomer as product
-
-
?
methyl 4-nitrophenyl sulfide + NADPH + H+ + O2
(R,S)-methyl 4-nitrophenyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 37% S-enantiomer as product
-
-
?
methyl phenyl sulfide + NADPH + H+ + O2
(R,S)-methyl phenyl sulfoxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 35% S-enantiomer as product
-
-
?
MK-0767 methyl sulfide + NADPH + H+ + O2
?
a peroxisome proliferator receptor activator, is converted to the S-oxide
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethyl-3-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]propan-1-amine + NADPH + H+ + O2
?
-
3-DPT, a phenothiazine analogue, N-oxygenation by FMO1 and FMO3, no activity with FMO5
-
-
?
N,N-dimethyl-5-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]pentan-1-amine + NADPH + H+ + O2
?
-
5-DPT, a phenothiazine analogue, N-oxygenation by FMO1, FMO3, and FMO5
-
-
?
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine + NADPH + H+ + O2
?
-
8-DPT, a phenothiazine analogue, N-oxygenation by FMO1, FMO3, and FMO5
-
-
?
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-deacetyl ketoconazole + NADPH + H+ + O2
?
an antifungal agent, is converted to the N-hydroxyl
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
an antifungal agent, is converted to the N-hydroxyl
-
-
?
N-methyl-tamoxifen + NADPH + O2
N-methyl-tamoxifen N-oxide + NADP+ + H2O
-
recombinant isozymes FMO1 and FMO3
-
-
?
orphenadrine + NADPH + H+ + O2
orphenadrine N-oxide + NADP+ + H2O
an anticholinergic drug
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
-
isozyme FMO3
-
-
?
phenyl propyl sulfide + NADPH + H+ + O2
phenyl propyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
phorate + NADPH + H+ + O2
?
a thioether-containing organophosphate insecticide
-
-
?
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-allyl-L-cysteine + NADPH + H+ + O2
?
-
-
-
?
S-allyl-L-cysteine + NADPH + H+ + O2
? + NADP+ + H2O
stereochemmistry, overview
-
-
?
S-benzyl-L-cysteine + NADPH + O2
S-benzyl-L-cysteine S-oxide + NADP+ + H2O
-
isozyme FMO1
-
-
?
S-farnesylcysteine + NADPH + O2
S-farnesylcysteine S-oxide + NADP+ + H2O
-
-
-
-
?
S-farnesylcysteine methyl ester + NADPH + O2
S-farnesylcysteine S-oxide methyl ester + NADP+ + H2O
-
-
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
S-methyl esonarimod S-oxide + NADP+ + H2O
an cytokine production inhbitor, 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
-
-
?
secondary amine + NADPH + O2
secondary nitrone + NADP+ + H2O
-
-
first oxidation to the N-hydroxy amine and then to the corresponding nitrone
?
seleno-L-methionine + NADPH + H+ + O2
seleno-L-methionine Se-oxide + NADP+ + H2O
-
-
-
?
SNI-2011 + NADPH + H+ + O2
?
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
tazarotenic acid + NADPH + H+ + O2
?
a retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
tazarotenic acid + NADPH + H+ + O2
tazarotenate N-oxide + NADP+ + H2O
an retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
thiacetazone + 2 NADPH + 2 O2
(E)-{(2E)-[4-(acetylamino)benzylidene]hydrazinylidene}(amino)methanesulfinic acid + 2 NADP+ + H2O
-
bioactivation by EtaA
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone S-oxide + NADP+ + H2O
-
low activity with FMO1 and FMO3, high activity with FMO2.1
-
-
?
thiobenzamide + NADPH + H+ + O2
thiobenzamide N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
[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
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
reaction in microsomal detoxification pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, a neurotoxin to nigrostriatal dopaminergic neurons
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
reaction in microsomal detoxification pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, a neurotoxin to nigrostriatal dopaminergic neurons
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
-
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
one of the predominant enzmyes responsible for the oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
?
1-[4-(methylsulfanyl)phenyl]ethanone + NADPH + H+ + O2
(R,S)-1-[4-(methylsulfanyl)phenyl]ethanone S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 21% R-enantiomer as product
-
-
?
1-[4-(methylsulfanyl)phenyl]ethanone + NADPH + H+ + O2
(R,S)-1-[4-(methylsulfanyl)phenyl]ethanone S-oxide + NADP+ + H2O
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 21% R-enantiomer as product
-
-
?
10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl) phenothiazines + NADPH + O2
?
-
with the alkyl side chain varying in length from 5 to 7 carbons, no activity with shorter side chains by isozyme FMO2
-
-
?
10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl) phenothiazines + NADPH + O2
?
-
with the alkyl side chain varying in length from 2 to 7 carbons, liver isozyme FMO1
-
-
?
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
?
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
?
-
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
-
-
?
2-(methylsulfanyl)pyridine + NADPH + H+ + O2
2-(methylsulfanyl)pyridine S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-(methylsulfanyl)pyridine + NADPH + H+ + O2
2-(methylsulfanyl)pyridine S-oxide + NADP+ + H2O
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-(methylsulfanyl)thiophene + NADPH + H+ + O2
2-(methylsulfanyl)thiophene S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-(methylsulfanyl)thiophene + NADPH + H+ + O2
2-(methylsulfanyl)thiophene S-oxide + NADP+ + H2O
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-2-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 75% R-enantiomer as product
-
-
?
2-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-2-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 75% R-enantiomer as product
-
-
?
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-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
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
-
-
?
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
-
-
?
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
-
N-oxidation
-
-
?
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
-
-
-
-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
KC734478, KC734481, KC734482, KC734486
-
-
-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
KC734478, KC734481, KC734482, KC734486
highest activity of all isoforms tested
-
-
?
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
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
-
N-oxidation
-
-
?
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
-
-
?
dapsone + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
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
-
-
?
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
-
-
?
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
?
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide N-oxide + NADP+ + H2O
an antibiotic agent
-
-
?
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
-
-
-
?
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 + 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
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
-
bioactivation by EtaA
-
-
?
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
-
-
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
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
-
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
-
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
-
-
-
?
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
-
-
?
L-Met-Phe + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
-
isozymes FMO1-FMO4
-
-
?
L-Met-Phe + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
-
liver microsomes
-
-
?
L-Met-Val + NADPH + O2
(L-Met-S-oxide)-Val + NADP+ + H2O
-
isozymes FMO1-FMO4, low activity by isozyme FMO1
-
-
?
L-Met-Val + NADPH + O2
(L-Met-S-oxide)-Val + NADP+ + H2O
-
liver microsomes
-
-
?
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
-
?
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
-
?
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
-
?
L-seleno-methionine + NADPH + O2
L-methionine seleno-oxide + NADP+ + H2O
-
liver microsomes
-
-
?
L-seleno-methionine + NADPH + O2
L-methionine seleno-oxide + NADP+ + H2O
-
purified liver isozymes FMO1 and FMO3
-
-
?
methamphetamine + NADPH + H+ + O2
?
a psychostimulant, is converted to the hydroxylamine
-
-
?
methamphetamine + NADPH + H+ + O2
?
-
a psychostimulant, is converted to the hydroxylamine
-
-
?
methimazole + NADPH + H+ + O2
?
a thyroperoxidase inhibitor
-
-
?
methimazole + NADPH + H+ + O2
?
a thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
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 N-oxide + NADP+ + H2O
KC734478, KC734481, KC734482, KC734486
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
KC734478, KC734481, KC734482, KC734486
about 25% of the activityy with substrate benzydamine
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-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
i.e. N-methyl-2-mercaptoimidazole
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
-
?
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
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + 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
-
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl p-tolyl sulfide + NADPH + H+ + O2
?
-
FMO1, FMO2, but poor substrate of FMO3
-
-
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
-
-
stereochemistry: product 49% R-enantiomer
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
-
-
26% R
-
?
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 + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
348485, 348486, 348487, 348488, 348490, 348491, 348492, 348494, 348497, 348498, 348499, 348505, 676315
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
-
-
-
?
n-decylamine + NADPH + O2
1-nitrosodecane + NADP+ + H2O
-
lung enzyme active, liver enzyme not
-
-
?
n-decylamine + NADPH + O2
1-nitrosodecane + NADP+ + H2O
-
lung enzyme active, liver enzyme not
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
-
recombinant protein expressed in E. coli
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
-
recombinant protein expressed in E. coli
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
-
lung enzyme active, liver enzyme not
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
-
lung enzyme active, liver enzyme not
-
-
?
naphthylthiourea + NADPH + O2
naphthylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
naphthylthiourea + NADPH + O2
naphthylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
a stimulant, is converted to the trans-N-oxide
-
-
?
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
-
-
-
-
?
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
-
-
?
p-tolyl sulfide + NADPH + O2
p-tolyl sulfoxide + NADP+ + H2O
-
S-oxidase activity
-
-
?
p-tolyl sulfide + NADPH + O2
p-tolyl sulfoxide + NADP+ + H2O
-
S-oxidase activity
-
-
?
phenylthiourea + NADPH + O2
phenylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
phenylthiourea + NADPH + O2
phenylthiourea S-oxide + NADP+ + H2O
-
isozyme FMO2
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
?
a cytokine production inhbitor, is converted to the S-oxide
-
-
?
sulfamethoxazole + NADPH + O2
?
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
S-oxidation, low activity
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
a nonsteroidal antiinflammatory drug, is converted to the S-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
-
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
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)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway, high activity by isozyme FMO1
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
i.e. (Z)-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
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 + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
-
bioactivation by EtaA
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
-
a thiourea-containing second line antitubercular prodrug
-
-
?
thiacetazone + NADPH + H+ + O2
?
a anti-tubercular drug, high activity
-
-
?
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
-
-
?
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
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
-
detoxification, the organism is resistant against the antibiotic
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
-
a glycylcycline derivative containing a 9-tert-butylglycylamido group belonging to the tetracyline antibiotic compounds
product identification by LC-MS
-
?
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
KC734478, KC734481, KC734482, KC734486
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
Methylophaga sp.
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
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
?
-
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
-
-
?
additional information
?
-
-
enhanced disease susceptibility1, EDS1, controls defense activation and programmed cell death conditioned by intracellular Toll-related immune receptors that recognize specific pathogen effectors in Arabidopsis thaliana, EDS1 is also needed for basal resistance to invasive pathogens by restricting the progression of disease, EDS1 with phytoalexin-deficient 4, PAD4, regulates accumulation of the phenolic defense molecule salicylic acid, EDS1 is regulated by FMO and the Nudix hydrolase NUDT7
-
-
-
additional information
?
-
enhanced disease susceptibility1, EDS1, controls defense activation and programmed cell death conditioned by intracellular Toll-related immune receptors that recognize specific pathogen effectors in Arabidopsis thaliana, EDS1 is also needed for basal resistance to invasive pathogens by restricting the progression of disease, EDS1 with phytoalexin-deficient 4, PAD4, regulates accumulation of the phenolic defense molecule salicylic acid, EDS1 is regulated by FMO and the Nudix hydrolase NUDT7
-
-
-
additional information
?
-
-
isozyme FMO1 is an essential component of biologically induced systemic acquired resistance, e.g. versus the bacterial pathogen Pseudomonas syringae pv maculicola, resistance is accompanied by accumulation of salicylic acid, overview
-
-
-
additional information
?
-
-
the enzyme is important for pathogen defense and resistance participating in the detoxification of virulence factors produced by pathogens, overview
-
-
-
additional information
?
-
-
tigecycline displays a broad spectrum of antibacterial activity and circumvents the efflux and ribosomal protection resistance mechanisms, Mg2+-complexing is required for ribosome binding, 11a-hydroxytigecycline forms a weaker complex with magnesium than tigecycline, structure, overview
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
additional information
?
-
-
modulation of activity by site directed mutagenesis
-
-
-
additional information
?
-
-
overview on substrate specifities and requirements of FMO1, FMO3
-
-
-
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, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, 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, 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
?
-
human FMO3 regulatory elements, overview
-
-
-
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
?
-
-
S-oxygenation of N-substituted thioureas
-
-
-
additional information
?
-
-
substrate specificity, the ability to stabilize the hydroperoxyflavin intermediate in substrate oxygenation is crucial involving NADP(H), overview
-
-
-
additional information
?
-
-
substrate specificity, the ability to stabilize the hydroperoxyflavin intermediate in substrate oxygenation is crucial involving NADP(H), overview
-
-
-
additional information
?
-
Methylophaga sp.
-
substrate specificity of the recombinant PTDH-mFMO fusion enzyme, overview
-
-
-
additional information
?
-
-
substrate specificity of the recombinant PTDH-mFMO fusion enzyme, overview
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview, hepatic total FMO activity is enhanced in mouse models of type I and type II diabetes
-
-
-
additional information
?
-
-
the enzyme is involved in fatty acid oxidation in the liver, as well as in drug detoxification
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
regulation of the enzyme expression by hypersaline conditions and the osmoregulatory hormonecortisol, overview
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
additional information
?
-
the enzyme is involved in oxidative metabolism of drugs and other chemicals
-
-
-
additional information
?
-
-
stereoselectivity of recombinant isozymes FMO1, FMO2, and FMO3
-
-
-
additional information
?
-
-
the lung isozyme is distinct from the liver isozyme in having high activity toward primary alkyl amines, restricted substrate specificity related to steric properties, resistance to detergent inhibition and enhanced thermal stability, and restricted substrate access, no activity of the lung isozyme with 1,3-diphenylthiourea, chlorpromazine and imipramine by isozyme FMO2, isozyme substrate specificity, detailed overview
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
additional information
?
-
-
the enzyme is involved in detoxification, generally, metabolites produced by FMO-catalysed reactions are more hydrophilic and less toxic, and are easily excreted from the body
-
-
-
additional information
?
-
-
substrates are a wide range of nucleophilic nitrogen-, sulfur-, phosphorus-, and selenium heteroatom-containing chemicals, drugs, and agricultural agents
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
the enzyme plays an important role in drug metabolism, insulin itself has no effect on FMO1 activity in non-diabetic animals, but hepatic isozyme FMO1 and intestinal CYP3A activity are correlated with average blood glucose concentration in untreated diabetic rats, and insulin reduces CYP3A activity, thus also regulates FMO1 indirectly
-
-
-
additional information
?
-
-
stereoselectivity of purified isozymes FMO1 and FMO3, overview
-
-
-
additional information
?
-
-
isozyme FMO5 does not metabolize 5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one (C-1305)
-
-
-
additional information
?
-
-
the substrate specificity of Saccharomyces cerevisiae FMO is more restricted than that of mammalian FMOs, reflecting its role in maintaining redox balance in the cell
-
-
-
additional information
?
-
-
reaction can be functionally separated into 2 partial reactions: 1. a reduced pyridine nucleotide and oxygen-dependent N-oxide synthase, 2. an N-oxide dealkylase
-
-
-
additional information
?
-
-
catalyzes NADPH- and O2-dependent N-oxidation of N-substituted amines and hydrazines and the S-oxidation of thioureylenes and thiols
-
-
-
additional information
?
-
-
catalyzes NADPH- and O2-dependent N-oxidation of N-substituted amines and hydrazines and the S-oxidation of thioureylenes and thiols
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
additional information
?
-
-
FMO oxygenates oxygenates a wide range of sulfur- and nitrogen-containing xenobiotics and, in some cases, also oxygenates selenium, iodine, boron, phosphorus and even carbon, it oxidizes drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, liver isozyme FMO1 shows a very promiscuous substrate specificity, isozyme substrate specificity, detailed overview
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
-
(S)-nicotine N-1'-oxygenation
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
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
-
-
-
-
?
dapsone + NADPH + O2
?
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
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
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
-
isozyme FMO3
-
-
?
S-farnesylcysteine + NADPH + O2
S-farnesylcysteine S-oxide + NADP+ + H2O
-
-
-
-
?
sulfamethoxazole + NADPH + O2
?
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
thiacetazone + 2 NADPH + 2 O2
(E)-{(2E)-[4-(acetylamino)benzylidene]hydrazinylidene}(amino)methanesulfinic acid + 2 NADP+ + H2O
-
bioactivation by EtaA
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
-
detoxification, the organism is resistant against the antibiotic
-
-
?
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
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
reaction in microsomal detoxification pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, a neurotoxin to nigrostriatal dopaminergic neurons
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
reaction in microsomal detoxification pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, a neurotoxin to nigrostriatal dopaminergic neurons
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + H+ + O2
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide + NADP+ + H2O
-
one of the predominant enzmyes responsible for the oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-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
P50285, Q8K2I3
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
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
-
bioactivation by EtaA
-
-
?
L-methionine + NADPH + O2
L-methionine S-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 + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + 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
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway, high activity by isozyme FMO1
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
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
-
bioactivation by EtaA
-
-
?
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
?
-
-
enhanced disease susceptibility1, EDS1, controls defense activation and programmed cell death conditioned by intracellular Toll-related immune receptors that recognize specific pathogen effectors in Arabidopsis thaliana, EDS1 is also needed for basal resistance to invasive pathogens by restricting the progression of disease, EDS1 with phytoalexin-deficient 4, PAD4, regulates accumulation of the phenolic defense molecule salicylic acid, EDS1 is regulated by FMO and the Nudix hydrolase NUDT7
-
-
-
additional information
?
-
Q9LMA1
enhanced disease susceptibility1, EDS1, controls defense activation and programmed cell death conditioned by intracellular Toll-related immune receptors that recognize specific pathogen effectors in Arabidopsis thaliana, EDS1 is also needed for basal resistance to invasive pathogens by restricting the progression of disease, EDS1 with phytoalexin-deficient 4, PAD4, regulates accumulation of the phenolic defense molecule salicylic acid, EDS1 is regulated by FMO and the Nudix hydrolase NUDT7
-
-
-
additional information
?
-
-
isozyme FMO1 is an essential component of biologically induced systemic acquired resistance, e.g. versus the bacterial pathogen Pseudomonas syringae pv maculicola, resistance is accompanied by accumulation of salicylic acid, overview
-
-
-
additional information
?
-
-
the enzyme is important for pathogen defense and resistance participating in the detoxification of virulence factors produced by pathogens, overview
-
-
-
additional information
?
-
-
tigecycline displays a broad spectrum of antibacterial activity and circumvents the efflux and ribosomal protection resistance mechanisms, Mg2+-complexing is required for ribosome binding, 11a-hydroxytigecycline forms a weaker complex with magnesium than tigecycline, structure, overview
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
additional information
?
-
Q01740
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
?
-
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, 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, 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
?
-
P31512
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
P31513
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
P49326
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
Q01740
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
Q99518
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
P31513
human FMO3 regulatory elements, overview
-
-
-
additional information
?
-
-
the enzyme is regulated by hormones, e.g. testosterone
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview, hepatic total FMO activity is enhanced in mouse models of type I and type II diabetes
-
-
-
additional information
?
-
-
the enzyme is involved in fatty acid oxidation in the liver, as well as in drug detoxification
-
-
-
additional information
?
-
P50285
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
P97501
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
P97872
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
Q8K2I3
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
Q8VHG0
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
P50285
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
P97501
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
P97872
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
Q8K2I3
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
Q8VHG0
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
additional information
?
-
A0SZ82
regulation of the enzyme expression by hypersaline conditions and the osmoregulatory hormonecortisol, overview
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
additional information
?
-
P17635
the enzyme is involved in oxidative metabolism of drugs and other chemicals
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
additional information
?
-
-
the enzyme is involved in detoxification, generally, metabolites produced by FMO-catalysed reactions are more hydrophilic and less toxic, and are easily excreted from the body
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
the enzyme plays an important role in drug metabolism, insulin itself has no effect on FMO1 activity in non-diabetic animals, but hepatic isozyme FMO1 and intestinal CYP3A activity are correlated with average blood glucose concentration in untreated diabetic rats, and insulin reduces CYP3A activity, thus also regulates FMO1 indirectly
-
-
-
additional information
?
-
-
the substrate specificity of Saccharomyces cerevisiae FMO is more restricted than that of mammalian FMOs, reflecting its role in maintaining redox balance in the cell
-
-
-
additional information
?
-
-
FMO oxygenates a number of drugs and xenobiotics containing a soft-nucleophile heteroatom, mostly sulfur- and nitrogen-containing xenobiotics, and is involved in detoxication
-
-
-
additional information
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
additional information
?
-
-
benzydamine is a weak base and an indazole derivative with analgesic and antipyretic properties used in human and veterinary medicine, it is metabolized to a wide range of metabolites. One of the main metabolites, benzydamine N-oxide is produced in the liver and brain by flavin-containing monooxygenases
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the prosthetic group FAD is an integral part of the protein, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview
FAD
binding site structure containing a GXGXXG motif, overview; binding site structure containing a GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview
FAD
-
binding structure, one molecule of noncovalently tightly bound FAD per enzyme monomer, overview
FAD
-
content determination, overview. Molar ratio of FAD to MBP-FMO3 varies from 0.5 to 0.9, and the FAD content of MBP-FMO5 has molar ratios of 0.6 and 0.7
FAD
-
-
671729, 672319, 673064, 673286, 673290, 673296, 673303, 673313, 675600, 675603, 676116, 684678, 686357, 690175, 703411, 706824, 710837, 717226
NADH
-
concentration of NADPH required for half-maximal velocity is one-tenth of that for NADH
NADPH
dependent on, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview
NADPH
binding site structure containing a GXGXXG motif, overview; binding site structure containing a GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview; binding site structure containing an GXGXXG motif, overview
NADPH
-
binding structure, the adjacent ribose of NADP+ is an integral part of the catalytic site being actively engaged in the stabilization of the oxygenating intermediate, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-2-[2-(4-(dimethylamino)phenyl)vinyl]benzoic acid
-
i.e. DS2CO, 2 mM, mechanism
(E)-3-[2-(4-(dimethylamino)phenyl)vinyl]benzoic acid
-
2 mM, 80-90% inhibition, mechansim; i.e. DS3CO
Deprenyl
-
strong, oxidative activity toward 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, MPTP
n-decyl-beta-D-maltoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-beta-D-maltoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-N,N-dimethylamine-n-oxide
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-nonyl-beta-D-glucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-glucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-thioglucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
NADPH
inhibits the binding of indole and decreases indoxyl production
NO
-
overproduced NO in liver causes the suppression of FMO3 activity directly via reversible S-nitrosylation. Overproduced NO may be responsible, at least in part, for the impairment of the detoxification or metabolism by FMOs of xenobiotics, which include a number of therapeutic drugs
Pargyline
-
strong, oxidative activity toward 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, MPTP
trans10, cis12-conjugated linoleic acid
-
reduces expression of FMO3 by 95%, and inhibits activity of hepatic microsomal FMO by 40% and of isozyme FMO3 activity by 67%, the compound has a strong effect on hepatic fatyy acid oxidation, overview
chlorpromazine
-
competitive inhibition of methimazole oxidation at high concentrations
imipramine
-
a FMO1-specific inhibitor, selectively inhibits N,N-dimethylamphetamine N-oxidation
imipramine
-
competitive inhibition of methimazole oxidation at high concentrations
Thiourea
inhibits S-oxygenation of ethionamide; thiourea reduces ethionamide oxygenation to ethionamide S-oxide by an average of 73.5% in liver and 76.9% in lung; thiourea reduces ethionamide oxygenation to ethionamide S-oxide by an average of 73.5% in liver and 76.9% in lung
trimethylamine
-
a FMO3-specific inhibitor, exhibits anegligible effect on the N,N-dimethylamphetamine N-oxide formation
additional information
-
FMO is not induced or readily inhibited by drugs in general in contrast to cytochrome P450 monooxygenases
-
additional information
-
the FMO1 gene is downregulated in the spinal cord of patients with the neurodegenerative disease amyotrophic lateral sclerosis
-
additional information
-
no inhibition of S-oxygenation of ethionamide by SKF-525A
-
additional information
-
cis9, trans11-conjugated linoleic acid reduces expression of FMO3 by 61%
-
additional information
-
lack of inhibition of S-oxygenation of ethionamide by SKF-525A
-
additional information
lack of inhibition of S-oxygenation of ethionamide by SKF-525A
-
additional information
lack of inhibition of S-oxygenation of ethionamide by SKF-525A
-
additional information
-
the lung isozyme is resistant to detergent inhibition
-
additional information
-
insulin itself has no effect on FMO1 activity in non-diabetic animals
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Guanidines
-
stimulate NADPH- and O2-dependent oxidation of tertiary amines and sulfur-containing substrates with alkyl side-chains of less than 5 carbons
-
Lipophilic primary alkylamines
-
stimulate NADPH- and O2-dependent oxidation of tertiary amines and sulfur-containing substrates with alkyl side-chain of less than 5 carbons
-
n-decyl-beta-D-maltoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-beta-D-maltoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-N,N-dimethylamine-n-oxide
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-nonyl-beta-D-glucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-glucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-thioglucoside
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octylamine
-
allosteric activation of pig liver and mouse lung enzymes, not mouse, rabbit or rat liver enzymes
n-octylamine
-
allosteric activation of pig liver and mouse lung enzymes, not mouse, rabbit or rat liver enzymes
n-octylamine
-
allosteric activation of pig liver and mouse lung enzymes, not mouse, rabbit or rat liver enzymes
Triton X-100
-
FMO3 enzymes show a 2fold activation of kcat/Km in the presence of Triton X-100. MBP-FMO3 also shows disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100
additional information
-
FMO is not induced or readily inhibited by drugs in general in contrast to cytochrome P450 monooxygenases
-
additional information
the ERalpha receptor upregulates enzyme expression, hyperforin induces the enzyme
-
additional information
the ERalpha receptor upregulates enzyme expression, hyperforin induces the enzyme
-
additional information
-
FMO1 expression is increased in the myocardial tissue of patients with atrial fibrillation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.117
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazine
pH 8.4, 37°C
0.0711
4-(4-methoxyphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37°C, recombinant FMO1
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
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
0.0032
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37°C, recombinant FMO5
0.0038
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37°C, recombinant FMO1
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
0.022
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
0.104
Ethionamide
37°C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37°C
2.131
Ethionamide
37°C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37°C
0.005
indole
wild-type, pH 8.0, temperature not specified in the publication
0.008
indole
mutant Y207S, pH 8.0, temperature not specified in the publication
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
0.0068
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37°C, recombinant FMO1
0.0245
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37°C, recombinant FMO3
0.0808
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37°C, recombinant FMO5
0.043
tamoxifen
-
pH 8.5, 37°C, recombinant isozyme FMO1 and recombinant mutant isozyme FMO3 E158K
0.131
thiacetazone
-
recombinant EtaA, pH 9.0, 37°C, thiacetazone sulfinic acid formation
0.147
thiacetazone
-
recombinant EtaA, pH 9.0, 37°C, thiacetazone carbodiimide formation
additional information
additional information
-
2 Km values for oxygenation of thiocarbamides: 1. Km1 for oxygenation to sulfenic acid, 2. Km2 for oxygenation of sulfenic acid to sulfinic acid
-
additional information
additional information
-
2 Km values for oxygenation of thiocarbamides: 1. Km1 for oxygenation to sulfenic acid, 2. Km2 for oxygenation of sulfenic acid to sulfinic acid
-
additional information
additional information
-
steady-state 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
-
kinetics for kidney and liver enzymes, overview
-
additional information
additional information
-
the recombinant enzyme exhibits Michaelis-Menten 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
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3
0.19
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3
0.22
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3
0.55
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3
0.67
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is CHAPS, commercial recombinant FMO3
0.72
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3
4.52
Ethionamide
Mus musculus
P50285, Q8K2I3
37°C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37°C
9.45
Ethionamide
Mus musculus
P50285, Q8K2I3
37°C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37°C
0.048
thiacetazone
Mycobacterium tuberculosis
-
recombinant EtaA, pH 9.0, 37°C, thiacetazone carbodiimide formation
0.085
thiacetazone
Mycobacterium tuberculosis
-
recombinant EtaA, pH 9.0, 37°C, thiacetazone sulfinic acid formation
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3
6382
0.0057
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3
6382
0.0143
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3
6382
0.0152
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3
6382
0.027
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
Homo sapiens
-
pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3
6382
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
Deprenyl
-
oxidative activity toward 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, MPTP
0.009
Pargyline
-
oxidative activity toward 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, MPTP
additional information
additional information
-
inhibition kinetics, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
substrate specificity of recombinant wild-type and mutant His6-tagged MBT-fusion-FMO3s, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 9
7.4
7.6
8.4
8.5
8.5
9.5
9.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
7.4 - 8.4
7.5 - 9
-
pH 7.5: about 40% of activity maximum, pH 9.0: about 95% of activity maximum
7.6 - 9
7.6 - 9.6
8.4 - 10.4
additional information
7.4 - 8.4
the activity is approximately twice as high at pH 8.4 as at pH 7.4; the activity is approximately twice as high at pH 8.4 as at pH 7.4
7.4 - 8.4
-
the activity is approximately twice as high at pH 8.4 as at pH 7.4
7.6 - 9
-
pH 7.6: about 70% of maximal activity, pH 9.0: about 65% of maximal activity, p-tolyl sulfide S-oxidase activity
7.6 - 9.6
-
about 50% of activity maximum at pH 7.6 and 9.6, liver, thiobenzamide S-oxidation
7.6 - 9.6
-
about 50% of activity maximum at pH 7.6 and 9.6, liver, thiobenzamide S-oxidation
8.4 - 10.4
-
about 50% of activity maximum at pH 8.4 and 10.4, lung, thiobenzamide S-oxidation
8.4 - 10.4
-
about 50% of activity maximum at pH 8.4 and 10.4, lung, thiobenzamide S-oxidation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
37
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
FMO1, expression profiling in tissue from patients with atrial fibrillation
additional information
KC734478, KC734481, KC734482, KC734486
most abundantly expressed; most abundantly expressed
expression of the FMO1 gene is not silenced postnatally in liver and kidney
FMO1 shows low expression; FMO3 is expressed in the renal collecting tubules, in renal medulla, and in renal glomerulus; FMO4 is expressed in the renal collecting tubules, in renal medulla, and in renal glomerulus
-
low level of tamoxifen N-oxide production in human liver microsomes may be explained by the kinetics of FMO1 versus FMO3, isozyme expression pattern, overview, fetal liver expresses only isozyme FMO1
birth is necessary but not sufficient for FMO3 onset in the liver, it occurs between week 3 and 10 after birth; fetal and adult; fetal and adult; fetal and adult; high level expression in adult liver
-
-
348504, 348508, 348510, 348512, 658461, 659823, 671729, 673286, 673290, 676116, 685038, 686355, 686357, 703411, 706921
KC734478, KC734481, KC734482, KC734486
most abundantly expressed; most abundantly expressed
-
expression analysis of FMO3 in liver and after treatment with conjugated linoleic acid isomers
expression of the FMO1 gene is not silenced postnatally in liver and kidney
-
-
FMO4 occurs in lobular distribution; highest expression of FMO1 in the perivenous region; highest expression of FMO3 in the perivenous region
-
-
348485, 348486, 348487, 348488, 348490, 348491, 348492, 348494, 348497, 348498, 348500, 348505, 348507, 659828, 673313, 703320, 712902
additional information
-
no expression of FMO3 in Hep-G2 cells, decreased hepatic nuclear factor HNF4alpha levels and DNA hypermethylation are the mechanisms suppressing Hep-G2 FMO3 expression
additional information
broad tissue distribution, overview; tissue-specific and devlopmental expression of FMO3, overview; tissue-specific expression of FMO1, overview; tissue-specific expression of FMO2, overview; tissue-specific expression of FMO5, overview, the enzyme is increased in ERalpha-positive tumors
additional information
broad tissue distribution, overview; tissue-specific and devlopmental expression of FMO3, overview; tissue-specific expression of FMO1, overview; tissue-specific expression of FMO2, overview; tissue-specific expression of FMO5, overview, the enzyme is increased in ERalpha-positive tumors
additional information
-
no activity in fetal human liver, intestine, and kidney
additional information
-
tissue-specific expression of FMO isozymes, quantitative expression analysis, overview
additional information
-
differential expression of isozymes in tissues
additional information
-
the lung isozyme FMO2 is distinct from the liver isozyme in having high activity toward primary alkyl amines, restricted substrate specificity related to steric properties, resistance to detergent inhibition and enhanced thermal stability
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the highly hydrophobic FMO shows multiple internal sites of membrane association
-
-
-
-
658461, 672319, 673286, 673290, 673313, 675600, 675603, 676116, 676315, 686276, 686355, 686357, 690175, 703320, 703408, 703411, 706824, 706921, 717226
-
-
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
54000
56000 - 59000
56000
60000
65000
100000
-
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation
102000
-
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation
104000
-
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
x * 60047, sequence calcualtion; x * 63338, sequence calculation
?
-
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation
?
-
x * 64000, SDS-PAGE, active enzyme exists as aggregating units of the monomer, amino acid composition
additional information
-
structure homology model for FMO3 based on the crystal structure for yeast FMO with N61 in close proximity to the FAD catalytic center, in contrast to residues M66, P153, R492, E158, V257, and E308, overview
additional information
-
structure comparison of wild-type and mutant enzymes, crystal structure analysis, overview
additional information
-
MBP-FMO3 shows disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100. MBP-FMO3 solubilized in 0.5% CHAPS and MBP-FMO5 solubilized in 0.01% DDM or minimal detergent conditions contain hexameric and larger aggregates of protein
additional information
-
structure motifs, overview, structural modeling
additional information
the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor
additional information
-
the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
FMO1 is selectively N-glycosylated at Asn120, N-glycosylation is not essential for functional activity
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of enzyme and enzyme in complex with NADP+, and a mutant Y207S, which lacks indole oxygenation activity, with and without indole. The crystal structures reveal overlapping binding sites for NADP+ and indole, suggestive of a double-displacement reaction mechanism. NADPH induces conformational changes in two active site motifs. One of the motifs contains Arg229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding to NADPH rather than NADH. The second motif contains Tyr207
mutant E158A/E159A, ligand-free or in complex with NADP+, microbatch technique at 4°C by mixing equal volumes of 8 mg of protein/ml in 25 mM Tris-HCl, pH 8.0, 250 mM NaCl, 1 mM NADP+, and of crystallization solution containing PEG 4000 20% w/v in 0.1 M Na/HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution, molecular replacement
-
purified recombinant enzyme in complex with FAD, and NADPH or methimazole, sitting drop vapor diffusion method, purified protein in 10 mM HEPES, pH 7.0, and 150 mM NaCl, versus reservoir solution containing 20% PEG 4000, 0.1 M sodium citrate buffer, pH 5.8, and 1,6-diaminohexane, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38
-
pH 7.6, half-life of free enzyme: 10 min, half-life of immobilized enzyme 5 h
40
50
additional information
40
-
in absence of NADPH, residue 360 is important for thermal stability, half-lives of wild-type and mutant isozymes FMO1 and FMO3, overview
40
-
purified recombinant FMO1, FMO3, and FMO5, the isozymes display similar thermal sensitivity, with activity decreased to 76% to 83% after 1 min preincubation at 40°C, 61% to 71% after 2 min preincubation, and 41% to 55% after 5 min preincubation
50
-
10 min, elimination of most Fmo1 and Fmo3 activity, while 94% of Fmo2 activity remains
additional information
-
loss of about 30% of activity after heat treatment of mutant enzyme N413K, activity is preservable by NADPH
additional information
-
the lung isozyme shows high thermal stability as the liver isozyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
glass-bead immobilized enzyme: 0-4°C, 0.025 M phosphate buffer, several months with little or no loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
one-step purification of the recombinant PTDH-mFMO from Escherichia coli by nickel affinity chromatography
Methylophaga sp.
-
partial
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant His-tagged EtaA from Escherichia coli strain DH5alpha by nickel affinity chromatography
-
recombinant maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 from Escherichia coli by amylose affinity chromatography
-
recombinant MBP-fusion FMO3 and FMO5 from Escherichia coli strain DH5alpha to about 90% purity by amylose affinity chromatography, and for FMO3 also further by anion exchange chromatography
-
recombinant protein
recombinant wild-type and mutant FMO3 from Escherichia coli strain JM109 in a multistep process
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA data
cDNA from liver, DNA and amino acid sequence determination and analysis, genomic structure and sequence comparison, expression analysis
DNA and amino acid sequence determination and analysis of multiple samples of gene FMO3, expression of clones in Spodoptera frugiperda Sf9 insect cell microsomes via baculovirus transfection system, the FMO multigene family consists of a five-gene cluster at 1q24.3, comprising FMO1-4 and FMO6p, and a second cluster of five genes at 1q24.2, comprising FMO7p-11p, and a single gene, FMO5, at 1q21.1, encoding a total of five active proteins in humans
-
expressed in Sf9 insect cells; expressed in Sf9 insect cells
expressed in Trichoplusia ni cells using a baculovirus expression vector system
-
expression analysis of FMO3 in liver and after treatment with conjugated linoleic acid isomers
-
expression as maltose-binding fusion proteins in Escherichia coli
expression in Escherichia coli
expression of FMO1, FMO2.1, and FMO3 in Spodoptera frugiperda Sf9 cell microsomes
-
expression of FMO3 and FMO5 as N-terminal maltose-binding protein fusion proteins, MBP-FMOs, in Escherichia coli strain DH5alpha
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of His-tagged EtaA in Escherichia coli strain DH5alpha
-
expression of isozyme FMO genetic variants in Spodoptera frugiperda Sf9 insect cell microsomes via baculovirus transfection system
-
expression of isozymes FMO1-FMO5, optimized for heterologous expression, in Escherichia coli, isozymes FMO1-FMO4 are active with peptide-bound methionine, while FMO5 is inactive
-
expression of maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 in Escherichia coli
-
expression of N-terminally His6-tagged truncation mutant in Escherichia coli as soluble enzyme, and expression of the mutant in Spodoptera frugiperda Sf9 insect cells
expression of wild-type and mutant isozymes FMO1 and FMO3 as N-terminally maltose-binding-protein fusion and C-terminally His6-tagged proteins in Escherichia coli strain JM109
-
expression of wild-type enzyme and mutants M66I and R492W in Spodoptera frugiperda Sf9 cell membranes
-
five genes encoding isozymes FMO1-FMO5 and 1 pseudogene organized in a gene cluster
-
FMO isozyme expression patterns, expression analysis; FMO isozyme expression patterns, expression analysis
FMO isozyme expression patterns, expression analysis; FMO isozyme expression patterns, expression analysis; FMO isozyme expression patterns, expression analysis
FMO, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21 (DE3)
FMO1, DNA and amino acid sequence determination and analysis, phylogenetic analysis; FMO2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; FMO3, DNA and amino acid sequence determination and analysis, the gene maps to the long arm of chromosome 1, phylogenetic analysis; FMO4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, the gene maps to the long arm of chromosome 1, genotyping and alternative splicing variants, overview; FMO5, the gene encoding the enzyme is located at 1q21.1, not in the FMO gene cluster at 1q24.3, DNA and amino acid sequence determination and analysis, phylogenetic analysis
FMO3 cDNA from liver, DNA and amino acid sequence determination and analysis, expression in Spodoptera frugiperda Sf9 insect cells
-
FMO3, genotyping in relation to gender, age, race/ethnic, and FMO3 expression in response to administration of the anti-schizophrenia drug olanzapine
gene FMO1, DNA and amino acid sequence determination and analysis, the gene contains five long interspersed nuclear element-1-like elements, i.e. LINE elements, expression analysis, silencing of FMO1 in adult human liver is due apparently to the presence upstream of the proximal P0 of LINE-1 elements rather than the absence of retrotransposons, expression in Hep-G2 cells
gene FMO1, DNA and amino acid sequence determination and analysis, the gene contains polyA region, an 80 bp direct repeat, an long terminal, LTR, repeat, a short-interspersed nuclear element, i.e. SINE element, and a poly T tract, expression analysis, expression in Hep-G2 cells
gene FMO1, genes FMO1 to FMO4 are clustered on chromosome 1 at q24.3, along with a pseudogene FMO6P; gene FMO2, genes FMO1 to FMO4 are clustered on chromosome 1 at q24.3, along with a pseudogene FMO6P; gene FMO3, genes FMO1 to FMO4 are clustered on chromosome 1 at q24.3, along with a pseudogene FMO6P
-
gene fMO3, DNA and amino acid sequence determination and analysis of wild-type and natural mutant enzymes, overview
-
gene FMO3, DNA and amino acid sequence determination and analysis, transient expression in Hep-G2 cells
-
gene tetX, expression in Escherichia coli confers antibiotic resistance
-
genes fmo1, fmo2, fmo3, quantitative expression analysis in different tissues, expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
genes FMO1-FMO6, FMO6 is a pseudogene, the genes are organized in two clusters chromosome 1, one of which resides on the long arm of chromosome 1 at q23 25, the second cluster is composed of 3 genes, that are not pseudogenes
-
genes FMO1-FMO6, FMO6 is a pseudogene, the genes are organized in two clusters chromosome 1, one of which resides on the long arm of chromosome 1 at q23 25, the second cluster is composed of 5 pseudogenes
-
independent expression of isozymes FMO1 and FMO3 in Spodoptera frugiperda Sf9 insect cell microsomes via baculovirus transfection system
-
overexpression of the FMO1 cDNA under control of the 35S CaMV promoter in independent transgenic Col-0 lines
-
quantitative Fmo isozyme expression analysis in female C3H/HeOuJ and C57BL/6 mice
-
using a baculovuirus expression system in Sf-9 insect cells, dFMO1 is expressed to protein levels of 0.4 nM/mg
whole genome microarrays to examine the EDS1 regulatory node in disease resistance and correlation of FMO1 expression, overview
using a baculovuirus expression system in Sf-9 insect cells, dFMO1 is expressed to protein levels of 0.4 nM/mg
-
using a baculovuirus expression system in Sf-9 insect cells, dFMO1 is expressed to protein levels of 0.4 nM/mg
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
8fold induction of FMO3 in liver by 3-methylcholanthrene. In Hepa-1 cells, 3-methylcholanthrene and benzo[a]pyrene induce FMO3 mRNA by about 30fold in an aryl hydrocarbon receptor-dependent manner. Aryl hydrocarbon receptor, AHR, dependent induction of FMO mRNAs in liver by 2,3,7,8-tetrachlorodibenzo-p-dioxin, but the potent AHR agonist, TCDD, does not induce FMO3 mRNA in Hepa-1 cells. Mechanism of FMO3 mRNA induction, overview
bacterial lipopolysaccharides lead to enzyme downregulation in the liver, as well as posttranslationally S-nitrosylation by nitric oxide
-
FMO3 expression in response to administration of the anti-schizophrenia drug olanzapine, allele frequencies and phenotypes, overview
induction by treatement of cells with cortisol and NaCl for 24 h, consistent with the reoccurrence cis-osmoregulatory and glucocorticoid response elements in the 5'-upstream sequence
isozyme expressions, especially of Fmo3, are downregulated by lipopolysaccharides or infection with Citrobacter rodentium in inflammation female C3H/HeOuJ mouse models, which is independent of Toll-like receptor 4, TLR4, overview
-
isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview; isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively; isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively; isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
no induction of FMO3 in Hepa-1 cells by 2,3,7,8-tetrachlorodibenzo-p-dioxin, DMSO, beta-naphthoflavon, 3,3',4,4',5-pentachlorobiphenyl, butylated hydroxyanisole, menadione, sulphoraphane, and tert-butylhydroquinone
isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview; isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview
isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview; isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview
-
-
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively; isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively; isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively; isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively; isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A52T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
D132H
D198E
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
D227K
pKa value 7.3 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
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
E158K/E308G
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
E305X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E308G
E314X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E32K
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
F510X
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
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
G182E
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
G475D
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
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
H97Q
I199T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
I303T
I303V
I37T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome; 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
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
L360P
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
M434I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
M66I
M82T
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
N114S
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
N413K
N61K
N61S
P153L
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
Q470X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
Q472X
R205C
R223Q
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome; naturally occuring single nucleotide polymorphism of FMO1
R238P
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R249X
naturally occuring single nucleotide polymorphism of FMO2, probably inactive mutant
R378L
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R492W
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
R500X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
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
R502X
R51G
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
S195L
T201K
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
V143E
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
V257M
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
V58I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
W388X
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
Y228H
pKa value 7.9 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
E158A/E159A
-
the mutant shows similar activity with trimethylamine compared to the wild-type enzyme
Y207S
mutant exhibits very little indoxyl producing activity but the NADPH oxidase activity of the mutant is higher than that of the wild-type enzyme
E158A/E159A
-
the mutant shows similar activity with trimethylamine compared to the wild-type enzyme
-
Y207S
-
mutant exhibits very little indoxyl producing activity but the NADPH oxidase activity of the mutant is higher than that of the wild-type enzyme
-
W47F
Methylophaga sp.
-
soluble and active protein. The spectrum of the flavin displays a redshift, the kcat values for NADPH, trimethylamine, and methimazole, show a 5-8fold decrease, and primary kinetic isotope effect values are higher than in wild-type. Mutant displays reduced flexibility in active site residues and, in particular, the nicotinamide moiety of NADP+
W47F
-
soluble and active protein. The spectrum of the flavin displays a redshift, the kcat values for NADPH, trimethylamine, and methimazole, show a 5-8fold decrease, and primary kinetic isotope effect values are higher than in wild-type. Mutant displays reduced flexibility in active site residues and, in particular, the nicotinamide moiety of NADP+
-
H228Y
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
K227D
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
additional information
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
D132H
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows substrate-dependent reduced activity
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
-
major naturally occuring structural varainat of isozyme FMO3, the mutant shows increased activity with tamoxifen compared to the wild-type enzyme
E158K
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E158K
-
natural genetic variant of isozymes FMO2 and FMO3, substrate specificity, overview
E158K
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly affects enzyme activity, substrate-dependent reduced activity
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/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
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K/E308G
-
naturally occuring mutation not involved in primary trimethylaminuria
E158K/E308G
naturally occuring single nucleotide polymorphism of FMO3, the mutation affects enzyme activity, substrate-dependent reduced activity
E158K/E308G
-
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
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
E24D
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
E308G
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E308G
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E308G
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly 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
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
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
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
K416N
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
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
L360P
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
L360P
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows increased activity
M66I
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
M66I
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
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
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
N61K
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
N61S
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
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
P153L
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
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; naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
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
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
R205C
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
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
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
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
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
-
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
-
natural genetic variant of isozyme FMO3, substrate specificity, overview
V257M
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows slightly 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
additional information
-
construction of fmo1 defective mutants, FMO1 mutations specifically affects the EDS1 pathway, defects in Arabidopsis fmo1 mutants are not coupled to SA accumulation, reduced pathogen defense, phenotype, analysis of fmo1 and nudt7 mutants alone or in combination with sid2-1, a mutation that severely depletes pathogen-induced salicylic acid production, points to salicylic acid-independent functions of FMO1 and NUDT7 in EDS1-conditioned disease resistance and cell death, overview
additional information
construction of fmo1 defective mutants, FMO1 mutations specifically affects the EDS1 pathway, defects in Arabidopsis fmo1 mutants are not coupled to SA accumulation, reduced pathogen defense, phenotype, analysis of fmo1 and nudt7 mutants alone or in combination with sid2-1, a mutation that severely depletes pathogen-induced salicylic acid production, points to salicylic acid-independent functions of FMO1 and NUDT7 in EDS1-conditioned disease resistance and cell death, overview
additional information
-
isolation of a dominant, gain-of-function phenotype FMO1-3D mutant, insertion at At1g19260 and towards the At1g19250 locus, from Arabidopsis thaliana, using activation tagging in the Arabidopsis Col-0 rps2-101C background, the mutant shows virtually no symptoms after inoculation with virulent Pseudomonas syringae pv. tomato DC3000 bacteria and downy mildew-causing pathogen Hyaloperonospora parasitica due to overexpression of class 3 FMO, overview, overexpression of the FMO1 cDNA, under control of the 35S CaMV promoter in independent transgenic Col-0 lines, leads to the same phenotype, progeny from crosses of the FMO1-3D mutant with the NahG transgenic line show that the enhanced basal resistance phenotype is dependent on the accumulation of salicylic acid, the R-gene-mediated defence physiology is not compromised by FMO1 overexpression, T-DNA insertion into the FMO1 gene resulted in enhances the susceptibility to virulent Pseudomonas and Hyaloperonospora parasitica, phenotypes, overview
additional information
-
an Arabidopsis FMO1 knockout line is fully impaired in the establishment of systemic acquired resistance, SAR, triggered by virulent bacteria, loss of SAR in the FMO1 mutants is accompanied by the inability to initiate systemic accumulation of salicylic acid and systemic expression of diverse defense related genes, overview, fmo1mutation does not significantly affect local disease resistance toward virulent or avirulent bacteria in native plants
additional information
-
occuring single nucleotide polymorphisms are associated with dramatic functional differences in selective functional enzyme activity, overview
additional information
-
effects of genetic variants of isozyme FMO3 on N- and S-oxygenation activities, genotype-phenotype studies, overview
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
-
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
-
three of the five expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms, 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
naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview
additional information
naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview; naturally occuring mutations, including silent mutations, genotyping, overview
additional information
-
genotyping of FMO3 in a Japanese cohort, missense and nonsense mutations, 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
-
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; 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
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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
additional information
Methylophaga sp.
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preparation of self-sufficient monooxygenases by covalent coupling of mFMO with the soluble NADPHregenerating phosphite dehydrogenase, PTDH, from Pseudomonas stutzeri using a codon-optimized gene encoding a His-tagged and thermostable PTDH mutant as fusion partner. The bifunctional biocatalyst is able to use phosphite as a cheap and sacrificial substrate for recycling NADPH
additional information
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preparation of self-sufficient monooxygenases by covalent coupling of mFMO with the soluble NADPHregenerating phosphite dehydrogenase, PTDH, from Pseudomonas stutzeri using a codon-optimized gene encoding a His-tagged and thermostable PTDH mutant as fusion partner. The bifunctional biocatalyst is able to use phosphite as a cheap and sacrificial substrate for recycling NADPH
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additional information
C-terminal truncation of 26 amino acids and and a double Ser substitutio of isozyme FMO2 enhances the enzyme solubility and reduce hydrophobicity required for efficient enzyme crystallization, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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the enzyme is not affected by drugs in contrast to cytochrome P450 monooxgenases, EC 1.14.14.1, by incorporating FMO detoxication pathways into drug candidates, more drug-like materials may emerge
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.8)
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