Information on EC 1.14.13.8 - flavin-containing monooxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.14.13.8
-
RECOMMENDED NAME
GeneOntology No.
flavin-containing monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
reaction mechanism of S-oxygenation of N-substituted thioureas
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
catalytic reaction mechanism via 4alpha-hydroperoxyflavin transient intermediate
Q9HFE4
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
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
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
catalytic cycle, reaction mechanism and structure-function relationship, overview
-
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
catalytic cycle, reaction mechanism via C4a-hydroperoxyflavin intermediate and structure-function relationship, overview
Methylophaga aminisulfidivorans SK1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Drug metabolism - cytochrome P450
-
-
Microbial metabolism in diverse environments
-
-
nicotine degradation IV
-
-
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]
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethylaniline monooxygenase (N-oxide-forming)
-
-
-
-
dimethylaniline N-oxidase
-
-
-
-
dimethylaniline oxidase
-
-
-
-
DMA oxidase
-
-
-
-
FAD-containing monooxygenase
-
-
-
-
flavin monooxygenase
-
-
-
-
flavin-containing monooxygenase
-
-
-
-
FMO
-
-
-
-
FMO 1A1
-
-
-
-
FMO 1B1
-
-
-
-
FMO 1C1
-
-
-
-
FMO 1D1
-
-
-
-
FMO 1E1
-
-
-
-
FMO-I
-
-
-
-
FMO-II
-
-
-
-
FMO1
-
-
-
-
FMO2
-
-
-
-
FMO3
-
-
-
-
FMO5
-
-
-
-
mixed-function amine oxidase
-
-
-
-
N,N-dimethylaniline monooxygenase
-
-
-
-
oxygenase, dimethylaniline mono- (N-oxide-forming)
-
-
-
-
oxygenase, methylphenyltetrahydropyridine N-mono-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
117910-56-2
-
148848-55-9
-
37256-73-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme FMO1
SwissProt
Manually annotated by BRENDA team
female and male beagle dogs
-
-
Manually annotated by BRENDA team
diet of Brussels sprouts
-
-
Manually annotated by BRENDA team
Europian-, Latin-, African-, and Asian-American schizophrenia patients
UniProt
Manually annotated by BRENDA team
FMO multigene family
-
-
Manually annotated by BRENDA team
FMO1; gene FMO1
UniProt
Manually annotated by BRENDA team
FMO3; gene FMO3
UniProt
Manually annotated by BRENDA team
FMO4
UniProt
Manually annotated by BRENDA team
FMO5
UniProt
Manually annotated by BRENDA team
genes FMO1-FMO6, FMO6 is a pseudogene
-
-
Manually annotated by BRENDA team
isozyme FMO1
UniProt
Manually annotated by BRENDA team
isozyme FMO1-FMO5
-
-
Manually annotated by BRENDA team
isozyme FMO3
-
-
Manually annotated by BRENDA team
isozyme FMO5
UniProt
Manually annotated by BRENDA team
isozymes FMO1 and FMO3
-
-
Manually annotated by BRENDA team
isozymes FMO1-FMO5
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
isozymes FMO1FMO6
-
-
Manually annotated by BRENDA team
isoform FMO1
KC734478
GenBank
Manually annotated by BRENDA team
isoform FMO2
KC734481
GenBank
Manually annotated by BRENDA team
isoform FMO3
KC734482
GenBank
Manually annotated by BRENDA team
isoform FMO5
KC734486
GenBank
Manually annotated by BRENDA team
Methylophaga aminisulfidivorans SK1
-
Uniprot
Manually annotated by BRENDA team
Methylophaga aminisulfidivorans SK1
strain SK1
-
-
Manually annotated by BRENDA team
Methylophaga sp.
-
-
-
Manually annotated by BRENDA team
Methylophaga sp. SK1
-
-
-
Manually annotated by BRENDA team
8-weeks-old female C57BL/6N mice
-
-
Manually annotated by BRENDA team
female C3H/HeOuJ and C57BL/6 mice
-
-
Manually annotated by BRENDA team
FMO1; gene FMO1
UniProt
Manually annotated by BRENDA team
FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
Manually annotated by BRENDA team
gene Fmo3; gene FMO3
UniProt
Manually annotated by BRENDA team
isoform FMO5
UniProt
Manually annotated by BRENDA team
isozyme Fmo1, gene FMO1
UniProt
Manually annotated by BRENDA team
isozyme Fmo2, gene FMO2
UniProt
Manually annotated by BRENDA team
isozyme Fmo3, gene FMO3
UniProt
Manually annotated by BRENDA team
isozyme Fmo4, gene FMO4
UniProt
Manually annotated by BRENDA team
isozyme Fmo5, gene FMO5
UniProt
Manually annotated by BRENDA team
male C57BL6 mice, isozymes FMO1, FMO3, and FMO5
-
-
Manually annotated by BRENDA team
several strains, overview, genes fmo1, fmo2, fmo3, and fmo5
-
-
Manually annotated by BRENDA team
strain C-57 BL
-
-
Manually annotated by BRENDA team
Swiss/Webster mice
-
-
Manually annotated by BRENDA team
Mus musculus C-57 BL
strain C-57 BL
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
isozyme Fmo1, gene FMO1
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6J
isozyme Fmo2, gene FMO2
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6J
isozyme Fmo3, gene FMO3
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6J
isozyme Fmo4, gene FMO4
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6J
isozyme Fmo5, gene FMO5
UniProt
Manually annotated by BRENDA team
gene etaA or RV3854c
-
-
Manually annotated by BRENDA team
isozyme FMO1-FMO5
-
-
Manually annotated by BRENDA team
isozyme FMO2
Uniprot
Manually annotated by BRENDA team
tissue-specific isozymes
-
-
Manually annotated by BRENDA team
7-9-months-old Akkaraman sheep, isozyme FMO3
-
-
Manually annotated by BRENDA team
FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
Manually annotated by BRENDA team
healthy and streptozotocin-induced diabetic rats
-
-
Manually annotated by BRENDA team
isozyme FMO1-FMO5
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
UniProt
Manually annotated by BRENDA team
male sprague-dawley rats
UniProt
Manually annotated by BRENDA team
dogfish shark
-
-
Manually annotated by BRENDA team
FMOs exist as a multi-gene family consisting of individual members that are expressed in a tissue-, developmental-, and sex-specific fashion
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P50285, Q8K2I3
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
physiological function
-
FMO catalyzes the oxidation at nucleophilic, heteroatom centers and is important for drug, xenobiotic, and endogenous substrate metabolism
physiological function
-
FMO3 plays an important role in kidney metabolism of xenobiotics containing sulfur and selenium atoms
physiological function
-
the flavin-containing monooxygenase family of enzymes oxygenates nucleophilic xenobiotics and endogenous substances
metabolism
Q01740, Q9HA79
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
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
P97501
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
show the reaction diagram
-
(S)-nicotine N-1'-oxygenation
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
show the reaction diagram
-
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
show the reaction diagram
-
possibly, and other 1,1-disubstituted hydrazines
-
?
1,2,3,4-tetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1,2,3,4-tetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1,2-dimethylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1,2-dimethylphenylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-butanethiol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-methyl-1-phenylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-methyl-2-benzylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-methyl-2-thioimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
one of the predominant enzmyes responsible for the oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
?
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
show the reaction diagram
Mus musculus C-57 BL
-
-
-
?
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
show the reaction diagram
Mus musculus C-57 BL
-
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 + O2
?
show the reaction diagram
-
-
-
-
?
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-methyl-6,7-dihydroxytetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
1-[4-(methylsulfanyl)phenyl]ethanone + NADPH + H+ + O2
(R,S)-1-[4-(methylsulfanyl)phenyl]ethanone S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp., Methylophaga sp. SK1
-
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
?
show the reaction diagram
-
with the alkyl side chain varying in length from 2 to 7 carbons, liver isozyme FMO1
-
-
?
10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl) phenothiazines + NADPH + O2
?
show the reaction diagram
-
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-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
P49326
-
-
-
?
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
P97872
-
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
show the reaction diagram
-
isozyme FMO3
-
-
?
10-([N,N-dimethylaminopentyl]-2-trifluoromethyl)phenothiazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
show the reaction diagram
-
formation of the cis-oxime
-
-
?
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine + NADPH + H+ + O2
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine + NADPH + O2
?
show the reaction diagram
-
i.e. 5-DPT or diethylenetriaminepentaacetic acid
-
-
?
2-(methylsulfanyl)pyridine + NADPH + H+ + O2
2-(methylsulfanyl)pyridine S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp., Methylophaga sp. SK1
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-(methylsulfanyl)thiophene + NADPH + H+ + O2
2-(methylsulfanyl)thiophene S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp., Methylophaga sp. SK1
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-acetylsulfanylmethyl-4-(4-methoxyphenyl)-4-oxobutyric acid + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
2-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-2-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp., Methylophaga sp. SK1
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 75% R-enantiomer as product
-
-
?
2-mercaptobenzimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-mercaptobenzimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-mercaptobenzimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-[(methylsulfanyl)methyl]furan + NADPH + H+ + O2
2-[(methylsulfanyl)methyl]furan S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
2-[2-(4-methoxyphenyl)-2-oxoethyl]-acrylic acid + NADPH + H+ + O2
?
show the reaction diagram
-
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
show the reaction diagram
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
?
show the reaction diagram
-
FMO1, poor activity with FMO3 and FMO5
-
-
?
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1 and FMO5, no activity with FMO3
-
-
?
4-(methylsulfanyl)benzonitrile + NADPH + H+ + O2
(R,S)-4-(methylsulfanyl)benzonitrile S-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 81% S-enantiomer as product
-
-
?
4-aminobenzoic acid hydrazide + NADPH + O2
?
show the reaction diagram
Q01740
-
-
-
?
4-chlorophenyl methyl sulfide + NADPH + H+ + O2
(R,S)-4-chlorophenyl methyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
Q01740, Q9HA79
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
show the reaction diagram
-
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
show the reaction diagram
Q01740, Q9HA79
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
show the reaction diagram
Q01740, Q9HA79
i.e. C-1305
-
-
?
aldicarb + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
alpha-naphthylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
aminopyrine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
ammonia + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
amphetamine + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antipsychotic agent, is converted to the hydroxylamine
-
-
?
amphetamine + NADPH + H+ + O2
?
show the reaction diagram
-
an antipsychotic agent, is converted to the hydroxylamine
-
-
?
amphetamine + NADPH + O2
amphetamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a nonsteroidal antiinflammatory drug, is converted to the N-oxide
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
N-oxidation
-
-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
KC734478, KC734481, KC734482, KC734486
-
-
-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
KC734478, KC734481, KC734482, KC734486
highest activity of all isoforms tested
-
-
?
benzyl ethyl sulfide + NADPH + H+ + O2
benzyl ethyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
benzyl methyl sulfide + NADPH + H+ + O2
benzyl methyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
benzylamine + NADPH + O2
benzylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
beta-ethylphenylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
bupivacaine + NADPH + O2
bupivacaine-oxide + NADP+
show the reaction diagram
-
-
-
-
?
butyl ethyl sulfide + NADPH + H+ + O2
butyl ethyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
butyl methyl sulfide + NADPH + H+ + O2
butyl methyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
butylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a dopemaine D2 antagonist
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine N-oxide + NADP+ + H2O
show the reaction diagram
-
a dopemaine D2 antagonist
-
-
?
chlorpromazine + NADPH + H+ + O2
chlorpromazine oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
chlorpromazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
chlorpromazine + NADPH + O2
?
show the reaction diagram
-
liver isozyme FMO1
-
-
?
chlorpromazine + NADPH + O2
?
show the reaction diagram
-
liver microsomes
-
-
?
chlorpromazine + NADPH + O2
chlorpromazine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
cimetidine + NADPH + H+ + O2
cimetidine S-oxide + NADP+ + H2O
show the reaction diagram
-
S-oxygenation of cimetidine, i.e. CIM, a histamine H2-receptor antagonist of therapeutic utility in the treatment of peptic ulcer disease and gastric hypersecretory syndromes. Development of in-line screening and an off-line chiral CE method for determination of the stereoselectivity of flavin-containing monooxygenase isoforms FMO1, FMO3, and FMO5 using chiral specific selectors, overview
-
-
?
cimetidine + NADPH + O2
cimetidine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antipsychotic agent, is converted to the N-oxide
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
show the reaction diagram
-
an antipsychotic agent, is converted to the N-oxide
-
-
?
clozapine + NADPH + H+ + O2
clozapine N-oxide + NADP+ + H2O
show the reaction diagram
-
N-oxidation
-
-
?
clozapine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cyclohexyl methyl sulfide + NADPH + H+ + O2
cyclohexyl methyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
cysteamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
dapsone + NADPH + O2
?
show the reaction diagram
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation, isozyme FMO3, not FMO1
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
show the reaction diagram
-
i.e. O,O-diethyl O-2-ethylthioethyl phosphorothioate, isozymes FMO1 and FMO3, higher activity by FMO1
-
-
?
deprenyl + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
-
deprenyl + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a monoamine oxidase type B inhibitor, is converted to the hydroxylamine
-
-
?
deprenyl + NADPH + H+ + O2
?
show the reaction diagram
-
a monoamine oxidase type B inhibitor, is converted to the hydroxylamine
-
-
?
dibenzylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
dihydrolipoic acid + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
disulfoton + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a thioether-containing organophosphate insecticide
-
-
?
esonarimod + NADPH + H+ + O2
S-methyl esonarimod + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a antirheumatic drug, is converted to the S-oxide
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
show the reaction diagram
-
i.e. alpha-ethylthio-o-tolyl methylcarbamate, isozymes FMO1 and FMO3, higher activity by FMO1
-
-
?
ethionamide + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
?
show the reaction diagram
-
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide N-oxide + NADP+ + H2O
show the reaction diagram
P97501
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antibiotic agent
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
P50285, Q8K2I3
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
P50285, Q8K2I3
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
P50285, Q8K2I3
i.e. ETA, S-oxygenation by isozymes FMO1, FMO2, and FMO3
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
i.e. ETA, S-oxygenation by isozymes FMO1, FMO2, and FMO3
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
show the reaction diagram
-
bioactivation by isozymes FMO1 and FMO3, a thioamide-containing second line antitubercular prodrug
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
show the reaction diagram
-
a thioamide-containing second line antitubercular prodrug
-
-
?
ethyl phenyl sulfide + NADPH + H+ + O2
ethyl phenyl sulfoxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
ethylene sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
ethylenethiourea + NADPH + O2
ethylenethiourea S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethylenthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
etionamide + NADPH + H+ + O2
etionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
substrate of FMO1, FMO3, and FMO2.1
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+
show the reaction diagram
-
-
74% (+)-sulfoxide
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
more than 95% (+)-sulfoxide
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antidepressant, is converted to the N-oxide
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
show the reaction diagram
-
an antidepressant, is converted to the N-oxide
-
-
?
imipramine + NADPH + H+ + O2
imipramine oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
liver isozyme FMO1
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
liver microsomes
-
-
?
imipramine + NADPH + O2
imipramine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
imipramine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
show the reaction diagram
Q83XK4
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga aminisulfidivorans SK1
-
-
-
-
?
indole + NADPH + H+ + O2
indole N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga aminisulfidivorans SK1
Q83XK4
-
-
-
?
isopropylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a dopamine D2 receptor antagonist, is converted to the N-oxide
-
-
?
itopride + NADPH + H+ + O2
itopride N-oxide + NADP+ + H2O
show the reaction diagram
-
a dopamine D2 receptor antagonist, is converted to the N-oxide
-
-
?
itopride + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
K11777 + NADPH + H+ + O2
K11777 N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a cysteine protease inhibitor against Trypanosoma cruzi, is converted to the N-oxide
-
-
?
L-Met-Phe + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
show the reaction diagram
-
isozymes FMO1-FMO4
-
-
?
L-Met-Phe + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
show the reaction diagram
-
liver microsomes
-
-
?
L-Met-Val + NADPH + O2
(L-Met-S-oxide)-Val + NADP+ + H2O
show the reaction diagram
-
isozymes FMO1-FMO4, low activity by isozyme FMO1
-
-
?
L-Met-Val + NADPH + O2
(L-Met-S-oxide)-Val + NADP+ + H2O
show the reaction diagram
-
liver microsomes
-
-
?
L-methionine + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
-
-
-
?
L-methionine + NADPH + H+ + O2
methionine S-oxide + NADP+ + H2O
show the reaction diagram
Q9EQ76
stereochemistry, overview
formation of 80% D-isomer
-
?
L-methionine + NADPH + H+ + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
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-Phe-Met + NADPH + O2
(L-Met-S-oxide)-Phe + NADP+ + H2O
show the reaction diagram
-
liver microsomes
-
-
?
L-seleno-methionine + NADPH + O2
L-methionine seleno-oxide + NADP+ + H2O
show the reaction diagram
-
liver microsomes
-
-
?
L-seleno-methionine + NADPH + O2
L-methionine seleno-oxide + NADP+ + H2O
show the reaction diagram
-
purified liver isozymes FMO1 and FMO3
-
-
?
lidocaine + NADPH + O2
lidocaine-oxide + NADP+
show the reaction diagram
-
-
-
-
?
lipoic acid + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
mercaptoimidazole + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1 and FMO3, no activity with FMO5
-
-
?
mercaptoimidazole + NADPH + O2
mercaptoimidazole S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methamphetamine + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a psychostimulant, is converted to the hydroxylamine
-
-
?
methamphetamine + NADPH + H+ + O2
?
show the reaction diagram
-
a psychostimulant, is converted to the hydroxylamine
-
-
?
methamphetamine + NADPH + H+ + O2
methamphetamine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a psychostimulant, is converted to the hydroxylamine
-
-
?
methamphetamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methamphetamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a thyroperoxidase inhibitor
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1, FMO2, and FMO3
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
Methylophaga aminisulfidivorans SK1
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
KC734478, KC734481, KC734482, KC734486
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an thyroperoxidase inhibitor, is converted to the S-oxide
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
-
N-oxidation
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
KC734478, KC734481, KC734482, KC734486
about 25% of the activityy with substrate benzydamine
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp. SK1
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
show the reaction diagram
Q9EQ76
i.e. N-methyl-2-mercaptoimidazole
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
show the reaction diagram
-
low activity with FMO2.1, moderate activity with FMO3, high activity with FMO1
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
recombinant protein expressed in E. coli
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
recombinant protein expressed in E. coli
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
-
FMO3 5000 times more efficient than FMO5
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
Q01740
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
Q9HFE4
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
isozyme FMO3
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
liver microsomes
-
-
?
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
show the reaction diagram
-
i.e. 4-methylthio-3,5-xylyl methylcarbamate, isozyme FMO1 acts stereospecifically, no activity by isozyme FMO3
-
-
?
methyl 2-phenylethyl sulfide + NADPH + H+ + O2
methyl 2-phenylethyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 37% S-enantiomer as product
-
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methyl p-tolyl sulfide + NADPH + H+ + O2
?
show the reaction diagram
Q99518
-
-
-
?
methyl p-tolyl sulfide + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1, FMO2, but poor substrate of FMO3
-
-
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
stereochemistry: product 49% R-enantiomer
?
methyl p-tolyl sulfide + NADPH + O2
methyl p-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
26% R
-
?
methyl phenyl sulfide + NADPH + H+ + O2
(R,S)-methyl phenyl sulfoxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation of the thioanisole derivative by recombinant PTDH-mFMO fusion protein. Enantiomeric reaction with 35% S-enantiomer as product
-
-
?
methylmercaptan + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
methylphenylsulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-3-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]propan-1-amine + NADPH + H+ + O2
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
N-oxygenation mainly by isozyme FMO1, low activity with isozyme FMO3
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga aminisulfidivorans, Methylophaga aminisulfidivorans SK1
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N-aminohomopiperidine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N-aminomorpholine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
?
N-aminopiperidine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N-aminopyrrolidone + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antifungal agent, is converted to the N-hydroxyl
-
-
?
N-deacetyl ketoconazole + NADPH + H+ + O2
N-deacetyl ketoconazole N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antifungal agent, is converted to the N-hydroxyl
-
-
?
n-decylamine + NADPH + O2
1-nitrosodecane + NADP+ + H2O
show the reaction diagram
-
lung enzyme active, liver enzyme not
-
-
?
N-methyl-1,2,3,4-tetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
N-methyl-tamoxifen + NADPH + O2
N-methyl-tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
recombinant isozymes FMO1 and FMO3
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
show the reaction diagram
-
lung enzyme active, liver enzyme not
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
show the reaction diagram
-
recombinant protein expressed in E. coli
-
-
?
naphthylthiourea + NADPH + O2
naphthylthiourea S-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO2
-
-
?
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a stimulant, is converted to the trans-N-oxide
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antihistamininc drug, is converted to the N-oxide
-
-
?
olopatadine + NADPH + H+ + O2
olopatadine N-oxide + NADP+ + H2O
show the reaction diagram
-
an antihistamininc drug, is converted to the N-oxide
-
-
?
orphenadrine + NADPH + H+ + O2
orphenadrine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an anticholinergic drug
-
-
?
p-chloro-N-methylaniline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
p-tolyl sulfide + NADPH + O2
p-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
S-oxidase activity
-
-
?
pargyline + NADPH + O2
?
show the reaction diagram
-
inhibitor of monoaminoxidase B
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO3
-
-
?
phenyl propyl sulfide + NADPH + H+ + O2
phenyl propyl sulfide S-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
sulfoxidation by recombinant PTDH-mFMO fusion protein
-
-
?
phenylhydrazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
phenylthiourea + NADPH + O2
phenylthiourea S-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO2
-
-
?
phorate + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a thioether-containing organophosphate insecticide
-
-
?
procarbazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
propranolol + NADPH + O2
propranolol-hydroxylamine + NADP+
show the reaction diagram
-
-
-
-
?
pyrazolacridine + NADPH + H+ + O2
pyrazolacridine N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antitumor drug, is converted to the N-oxide
-
-
?
pyrazoloacridine + NADPH + O2
pyrazoloacridine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
R(-)-deprenyl + NADPH + O2
?
show the reaction diagram
-
inhibitor of monoaminoxidase B
-
-
?
ranitidine + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antihistamininc drug, is converted to the N-oxide and/or S-oxide
-
-
?
ranitidine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
S-allyl-L-cysteine + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
-
-
-
?
S-allyl-L-cysteine + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
Q9EQ76
stereochemmistry, overview
-
-
?
S-benzyl-L-cysteine + NADPH + O2
S-benzyl-L-cysteine S-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO1
-
-
?
S-farnesylcysteine + NADPH + O2
S-farnesylcysteine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
S-farnesylcysteine methyl ester + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
S-farnesylcysteine methyl ester + NADPH + O2
S-farnesylcysteine S-oxide methyl ester + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a cytokine production inhbitor, is converted to the S-oxide
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
S-methyl esonarimod S-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an cytokine production inhbitor, is converted to the S-oxide
-
-
?
S16020 + NADPH + H+ + O2
S16020 N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a topoisomerase II inhibitor and antitumor drug, is converted to the N-oxide
-
-
?
secondary amine + NADPH + O2
secondary nitrone + NADP+ + H2O
show the reaction diagram
-
-
first oxidation to the N-hydroxy amine and then to the corresponding nitrone
?
selegiline + NADPH + O2
selegiline N-oxide + NADP+
show the reaction diagram
-
-
-
-
?
seleno-L-methionine + NADPH + H+ + O2
seleno-L-methionine Se-oxide + NADP+ + H2O
show the reaction diagram
Q9EQ76
-
-
-
?
SNI-2011 + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a muscarinic receptor antagonist, is converted to the N-oxide
-
-
?
sulfamethoxazole + NADPH + O2
?
show the reaction diagram
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation, isozyme FMO3, not FMO1
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
show the reaction diagram
P97501
-
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a nonsteroidal antiinflammatory drug, is converted to the S-oxide
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
show the reaction diagram
-
S-oxidation
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
show the reaction diagram
-
S-oxidation, low activity
-
-
?
sulindac sulfide + NADPH + O2
(S,R)-sulindac + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
sulindac sulfide + NADPH + O2
sulindac + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + H+ + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
an estrogen receptor modulator, is converted to the N-oxide
-
-
?
tamoxifen + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway, high activity by isozyme FMO1
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
i.e. (Z)-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
i.e. Z-(1-[4-(2-dimethyl-aminoethoxy)phenyl]-1,2-diphenyl-1-butene)
-
-
?
tazarotenic acid + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
tazarotenic acid + NADPH + H+ + O2
tazarotenate N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an retinoic acid receptor modulator, is converted to the S-oxide
-
-
?
tertiary amine + NADPH + O2
tertiary N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
show the reaction diagram
-
bioactivation by isozymes FMO1 and FMO3, two-step process, a thiourea-containing second line antitubercular prodrug
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
show the reaction diagram
-
a thiourea-containing second line antitubercular prodrug
-
-
?
thiacetazone + 2 NADPH + 2 O2
(E)-{(2E)-[4-(acetylamino)benzylidene]hydrazinylidene}(amino)methanesulfinic acid + 2 NADP+ + H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
thiacetazone + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a anti-tubercular drug, high activity
-
-
?
thiacetazone + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
?
show the reaction diagram
-
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone N-oxide + NADP+ + H2O
show the reaction diagram
-
an antibiotic agent, is converted to the sulfinic acid/carbodiimide
-
-
?
thiacetazone + NADPH + H+ + O2
thiacetazone S-oxide + NADP+ + H2O
show the reaction diagram
-
low activity with FMO1 and FMO3, high activity with FMO2.1
-
-
?
thioacetamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thioacetamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thioacetamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiobenzamide + NADPH + H+ + O2
thiobenzamide N-oxide + NADP+ + H2O
show the reaction diagram
-
N-oxidation
-
-
?
thiobenzamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiocarbanilide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
thiourea S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
thiourea S-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO2
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
show the reaction diagram
-
detoxification, the organism is resistant against the antibiotic
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
show the reaction diagram
-
a glycylcycline derivative containing a 9-tert-butylglycylamido group belonging to the tetracyline antibiotic compounds
product identification by LC-MS
-
?
triethylamine + NADPH + H+ + O2
triethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trifluoperazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trifluoroperazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp.
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
KC734478, KC734481, KC734482, KC734486
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
Methylophaga aminisulfidivorans SK1
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga sp. SK1
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1, no activity with FMO3 and FMO5
-
-
?
trimethylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO3
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
preferred substrate of isozyme FMO3
-
-
?
tyramine + NADPH + O2
tyramine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
show the reaction diagram
-
liver microsomes, a potent second-generation triazole antifungal agent with broad-spectrum activity against clinically important fungi, recombinant FMO1 and FMO3, no activity with FMO5, N-oxidation of the fluoropyrimidine ring, its hydroxylation, and hydroxylation of the adjacent methyl group
-
-
?
xanomeline + NADPH + H+ + O2
xanomeline N-oxide + NADP+ + H2O
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
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
show the reaction diagram
-
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
-
?
MK-0767 methyl sulfide + NADPH + H+ + O2
?
show the reaction diagram
P31512, P31513, P49326, Q01740, Q99518
a peroxisome proliferator receptor activator, is converted to the S-oxide
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
comparison of FMO3 and FMO5
-
-
-
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
?
-
-
modulation of activity by site directed mutagenesis
-
-
-
additional information
?
-
-
overview on substrate specifities and requirements of FMO1, FMO3
-
-
-
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
?
-
-
overview on specificity
-
-
-
additional information
?
-
-
S-oxygenation of N-substituted thioureas
-
-
-
additional information
?
-
-
study of oxidative half-reaction
-
-
-
additional information
?
-
-
study of reductive half-reaction
-
-
-
additional information
?
-
-
specificity of FMO-I and FMO-II
-
-
-
additional information
?
-
-
enzyme regulation, overview
-
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
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 catalyzes the NADPH-dependent N-and S-oxidation of a variety of therapeutics, environmental toxicants, carcinogens, and nutrients
-
-
-
additional information
?
-
-
the enzyme is important for pathogen defense and resistance participating in the detoxification of virulence factors produced by pathogens, overview
-
-
-
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
?
-
-
the enzyme is involved in fatty acid oxidation in the liver, as well as in drug detoxification
-
-
-
additional information
?
-
P17635
the enzyme is involved in oxidative metabolism of drugs and other chemicals
-
-
-
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
?
-
-
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
?
-
-
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 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
?
-
-
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
?
-
-
stereoselectivity of purified isozymes FMO1 and FMO3, overview
-
-
-
additional information
?
-
-
stereoselectivity of recombinant isozymes FMO1, FMO2, and FMO3
-
-
-
additional information
?
-
-
substrates are a wide range of nucleophilic nitrogen-, sulfur-, phosphorus-, and selenium heteroatom-containing chemicals, drugs, and agricultural agents
-
-
-
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
?
-
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview, 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, 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, P31513, P49326, Q01740, Q99518
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
P31513
human FMO3 regulatory elements, overview
-
-
-
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
?
-
-
substrate specificity, the ability to stabilize the hydroperoxyflavin intermediate in substrate oxygenation is crucial involving NADP(H), overview
-
-
-
additional information
?
-
-
regulation of hepatic Fmo isozymes, overview
-
-
-
additional information
?
-
A0SZ82
regulation of the enzyme expression by hypersaline conditions and the osmoregulatory hormonecortisol, overview
-
-
-
additional information
?
-
-
the enzyme is regulated by hormones, e.g. testosterone
-
-
-
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 monooxigenases
-
-
-
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
?
-
P50285, P97501, P97872, Q8K2I3, 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
?
-
-
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
?
-
Methylophaga sp.
-
substrate specificity of the recombinant PTDH-mFMO fusion enzyme, overview
-
-
-
additional information
?
-
-
isoform FMO5 exhibits a low catalytic activity only for sulfoxidation of methyl 4-tolyl sulfide
-
-
-
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
?
-
Q01740, Q9HA79
isozyme FMO5 does not metabolize C-1305
-
-
-
additional information
?
-
Methylophaga aminisulfidivorans SK1
-
substrate specificity, the ability to stabilize the hydroperoxyflavin intermediate in substrate oxygenation is crucial involving NADP(H), overview
-
-
-
additional information
?
-
Mus musculus C57BL/6J
P50285, P97501, P97872, Q8K2I3, 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
?
-
Methylophaga sp. SK1
-
substrate specificity of the recombinant PTDH-mFMO fusion enzyme, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-nicotine + NADPH + O2
(S)-nicotine N1-oxide + NADP+ + H2O
show the reaction diagram
-
(S)-nicotine N-1'-oxygenation
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
one of the predominant enzmyes responsible for the oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
?
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
show the reaction diagram
Mus musculus C-57 BL
-
reaction in microsomal detoxification pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, a neurotoxin to nigrostriatal dopaminergic neurons
-
-
?
10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
4-aminobenzoic acid hydrazide + NADPH + O2
?
show the reaction diagram
Q01740
-
-
-
?
amphetamine + NADPH + O2
amphetamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
benzylamine + NADPH + O2
benzylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
cimetidine + NADPH + O2
cimetidine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
clozapine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
dapsone + NADPH + O2
?
show the reaction diagram
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
demeton-O + NADPH + O2
demeton-O sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
dihydrolipoic acid + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
ethiofencarb + NADPH + O2
ethiofencarb sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
P50285, Q8K2I3
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
ethionamide + NADPH + O2 + H+
2-ethyl-N-hydroxypyridine-4-carbothioamide + NADP+ + H2O
show the reaction diagram
-
bioactivation by isozymes FMO1 and FMO3
-
-
?
fenthion + NADPH + O2
fenthion sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
itopride + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lipoic acid + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
Q01740
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + O2
?
show the reaction diagram
Q9HFE4
-
-
-
?
methiocarb + NADPH + O2
methiocarb sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylamphetamine + NADPH + H+ + O2
N,N-dimethylamphetamine N-oxide + NADP+ + H2O
show the reaction diagram
-
N-oxygenation mainly by isozyme FMO1, low activity with isozyme FMO3
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
Methylophaga aminisulfidivorans, Methylophaga aminisulfidivorans SK1
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
phenethylamine + NADPH + O2
phenethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
isozyme FMO3
-
-
?
ranitidine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
S-farnesylcysteine + NADPH + O2
S-farnesylcysteine S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
S-farnesylcysteine methyl ester + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
selegiline + NADPH + O2
selegiline N-oxide + NADP+
show the reaction diagram
-
-
-
-
?
sulfamethoxazole + NADPH + O2
?
show the reaction diagram
Q01740
bioactivation by isozyme FMO3, not FMO1, results in covalent adduct formation
-
-
?
sulindac sulfide + NADPH + O2
(S,R)-sulindac + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway, high activity by isozyme FMO1
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
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
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
thiacetazone + 2 NADPH + 2 H+ + 2 O2
thiacetazone carbodiimide + 2 NADP+ + 2 H2O
show the reaction diagram
-
bioactivation by isozymes FMO1 and FMO3, two-step process
-
-
?
thiacetazone + 2 NADPH + 2 O2
(E)-{(2E)-[4-(acetylamino)benzylidene]hydrazinylidene}(amino)methanesulfinic acid + 2 NADP+ + H2O
show the reaction diagram
-
bioactivation by EtaA
-
-
?
tigecycline + NADPH + O2
11a-hydroxytigecycline + NADP+ + H2O
show the reaction diagram
-
detoxification, the organism is resistant against the antibiotic
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + H+ + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
preferred substrate of isozyme FMO3
-
-
?
tyramine + NADPH + O2
tyramine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
show the reaction diagram
-
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
show the reaction diagram
-
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
-
?
methyl 4-tolyl sulfide + NADPH + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme regulation, overview
-
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview
-
-
-
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 catalyzes the NADPH-dependent N-and S-oxidation of a variety of therapeutics, environmental toxicants, carcinogens, and nutrients
-
-
-
additional information
?
-
-
the enzyme is important for pathogen defense and resistance participating in the detoxification of virulence factors produced by pathogens, overview
-
-
-
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
?
-
-
the enzyme is involved in fatty acid oxidation in the liver, as well as in drug detoxification
-
-
-
additional information
?
-
P17635
the enzyme is involved in oxidative metabolism of drugs and other chemicals
-
-
-
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
?
-
-
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
?
-
-
drug metabolism, overview, enzyme mutations are involved in development of trimethylaminuria or fish-odor-syndrome, overview, 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, 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, P31513, P49326, Q01740, Q99518
FMO2 catalyzes the S-oxygenation of organophosphates representing a detoxification pathway
-
-
-
additional information
?
-
P31513
human FMO3 regulatory elements, overview
-
-
-
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
?
-
-
regulation of hepatic Fmo isozymes, overview
-
-
-
additional information
?
-
A0SZ82
regulation of the enzyme expression by hypersaline conditions and the osmoregulatory hormonecortisol, overview
-
-
-
additional information
?
-
-
the enzyme is regulated by hormones, e.g. testosterone
-
-
-
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 monooxigenases
-
-
-
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
?
-
P50285, P97501, P97872, Q8K2I3, 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
?
-
Mus musculus C57BL/6J
P50285, P97501, P97872, Q8K2I3, Q8VHG0
flavin-containing monooxygenases catalyze the addition of oxygen to many sulfur-, nitrogen-, phosphorus-, and selenium-containing compounds including pesticides, therapeutics, and dietary substances
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
FAD binding domain; flavoprotein
FAD
-
1 FAD per enzyme; flavoprotein
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
FAD binding domain
FAD
-
enzyme-bound
FAD
-
enzyme-bound
FAD
-
one molecule per enzyme molecule, binding motif
FAD
Q9HFE4
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
P31512, P49326
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
-
consensus binding sequence is Gly-Xaa-Gly-Xaa-Xaa-Gly
FAD
Q93Y23
-
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
Q01740, Q9HA79
;
flavin
-
flavoprotein
flavin
-
flavoprotein
NADH
-
can partially replace NADPH
NADH
-
concentration of NADPH required for half-maximal velocity is one-tenth of that for NADH
NADH
-
-
NADPH
-
NADP+ binding domain
NADPH
-
NADP+ binding domain
NADPH
-
required
NADPH
-
-
NADPH
Q9HFE4
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
P31512, P49326
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
NADPH
-
consensus binding sequence is Gly-Leu-Gly-Asn-Ser-Gly
NADPH
Q93Y23
-
NADPH
-
; required for activity; required for activity
NADPH
P50285, Q8K2I3
; required for activity; required for activity
NADPH
Methylophaga sp.
-
-
NADPH
-
required for activity
NADPH
Q01740, Q9HA79
required for activity; required for activity
NADPH
-
required for activity
flavin
P97501
-
additional information
-
the enzyme contains no heme
-
additional information
-
FMO2 contains no bound FAD
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
required
Mg2+
-
-
MgCl2
-
activates activity of mutant N413K by 18%
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
1-aminobenzotriazole
-
-
2-Diethylaminoethyl-2,2-diphenylpentanoate
-
SKF-525A, inhibition of dealkylation
3,3'-diindolylmethane
-
competitive inhibition of FMO3
alpha-Naphthoflavone
-
-
alpha-naphthylthiourea
-
0.5 mM, 59.2% inhibition
Anionic detergents
-
-
-
chlorpromazine
-
competitive inhibition of methimazole oxidation at high concentrations
chlorpromazine
-
competitively inhibits oxygenation of methimazole by FMO
CO
-
inhibition of dealkylation
Deprenyl
-
strong, oxidative activity toward 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, MPTP
fatty acids
-
-
HgCl2
-
IC50: 4.7 mM, liver microsomes
imipramine
-
competitive inhibition of methimazole oxidation at high concentrations
imipramine
-
competitively inhibits oxygenation of methimazole by FMO
imipramine
-
a FMO1-specific inhibitor, selectively inhibits N,N-dimethylamphetamine N-oxidation
indole
Q83XK4
inhibits NADPH oxidase activity
indole-3-carbinol
-
and its acid condensation products, strong
indole-3-carbinol
-
competitive inhibition of FMO3
ketoconazole
-
-
Methimazole
-
not competitive; oxidation of dimethylaniline
Methimazole
-
oxidation of dimethylaniline
Methimazole
-
0.5 mM, 27.4% inhibition
Methimazole
-
-
Methimazole
-
-
Methimazole
-
inhibits N,N-dimethylamphetamine N-oxidation
MgCl2
-
100 mM, 100% inhibition within 6 min
n-decyl-beta-D-maltoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-beta-D-maltoside
P17635
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
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-nonyl-beta-D-glucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-glucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-thioglucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octylamine
-
IC50: 4 mM, liver microsomes
NADPH
Q83XK4
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
propranolol
-
competitive, reaction with lidocaine or bupivacaine
SDS
-
-
Sodium cholate
-
1%, time-dependent sensitivity, maximum 65-100% inhibition
stearate
-
-
thiobenzamide
-
oxidation of dimethylaniline, competitive
thiobenzamide
-
0.5 mM, 68% inhibition
thiobenzamide
-
-
Thiourea
-
inhibits S-oxygenation of ethionamide
Thiourea
P50285, Q8K2I3
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
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
trimethylamine
-
1 mM, oxidation of dimethylaniline, competitive
trimethylamine
-
-
trimethylamine
-
a FMO3-specific inhibitor, exhibits anegligible effect on the N,N-dimethylamphetamine N-oxide formation
MgCl2
-
IC50: 77.5 mM, liver microsomes
additional information
-
not: piperonyl butoxide
-
additional information
-
FMO is not induced or readily inhibited by drugs in general in contrast to cytochrome P450 monooxygenases
-
additional information
-
cis9, trans11-conjugated linoleic acid reduces expression of FMO3 by 61%
-
additional information
-
insulin itself has no effect on FMO1 activity in non-diabetic animals
-
additional information
-
the lung isozyme is resistant to detergent inhibition
-
additional information
P31512, P49326
FMO5 is downregulated in type 2 diabetes
-
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
P50285, Q8K2I3
lack of inhibition of S-oxygenation of ethionamide by SKF-525A
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholate
-
29% activation at 0.5% concentration
cholate
-
activates activity of mutant N413K by 23%
Emulgen 913
-
350% activation at 0.2%, 47% activation at 1.0% concentration
Guanidines
-
stimulate NADPH- and O2-dependent oxidation of tertiary amines and sulfur-containing substrates with alkyl side-chains of less than 5 carbons
-
n-decyl-beta-D-maltoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-dodecyl-beta-D-maltoside
P17635
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
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-nonyl-beta-D-glucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-glucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octyl-beta-D-thioglucoside
P17635
1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes
n-octylamine
-
stimulation of tert-amine oxidation, not sec-amine oxidation
n-octylamine
-
allosteric activation of pig liver and mouse lung enzymes, not mouse, rabbit or rat liver enzymes
n-octylamine
-
-
n-octylamine
-
thyroid enzyme only active in presence of n-octylamine
n-octylamine
-
3 mM, enhances activity by 51%
n-octylamine
-
activates
n-octylamine
-
1 mM, 2fold stimulation
tertiary amines
-
self-activation with alkyl side chains of 7 or more
Triton X-100
-
271% activation at 0.1%, 159% activation at 0.3% concentration
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
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
-
additional information
-
FMO is not induced or readily inhibited by drugs in general in contrast to cytochrome P450 monooxygenases
-
additional information
-
FMO is not induced by xenobiotics
-
additional information
P31512, P49326
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
1,1-Dimethylhydrazine
-
-
0.059
1,2,3,4-tetrahydroisoquinoline
-
-
12
1,2-dimethylhydrazine
-
-
0.08
1-Methyl-1-phenylhydrazine
-
-
2
1-methyl-2-benzylhydrazine
-
-
0.0018
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
0.006
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
0.038
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
0.117
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene
P97872
pH 8.4, 37C
-
15
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, recombinant MBP-FMO3
25
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, commercial recombinant FMO3
32
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, recombinant MBP-FMO3
35
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, commercial recombinant FMO3
38
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is CHAPS, recombinant MBP-FMO3
0.0711
4-(4-methoxyphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37C, recombinant FMO1
0.0032
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37C, recombinant FMO5
0.0038
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37C, recombinant FMO1
0.0229
5-[[3-(dimethylamino)propyl]amino]-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Q01740, Q9HA79
isozyme FMO1, in 0.1 M potassium phosphate buffer (pH 8.4) at 37C
0.05903
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Q01740, Q9HA79
isozyme FMO1, in 0.1 M potassium phosphate buffer (pH 8.4) at 37C
0.4314
5-[[3-(dimethylamino)propyl]amino]-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Q01740, Q9HA79
isozyme FMO5, in 0.1 M potassium phosphate buffer (pH 8.4) at 37C
0.0186
Benzydamine
-
pH 7.4, 37C
0.0426
Benzydamine
-
pH 7.4, 37C
7
benzylhydrazine
-
-
3.3
beta-ethylphenylhydrazine
-
-
0.408
bupivacaine
-
pH 8.0, 25C
6.9
butylhydrazine
-
-
0.022
chlorpromazine
-
pH 8.4, 37C, recombinant mutant H360P His6-tagged MBT-fusion-FMO1
0.026
chlorpromazine
-
pH 8.4, 37C, recombinant mutant L360P His6-tagged MBT-fusion-FMO3
0.028
chlorpromazine
-
pH 8.4, 37C, recombinant mutant L360H His6-tagged MBT-fusion-FMO3
0.058
chlorpromazine
-
pH 8.4, 37C, recombinant wild-type His6-tagged MBT-fusion-FMO1
0.061
chlorpromazine
-
pH 8.4, 37C, recombinant wild-type His6-tagged MBT-fusion-FMO3
0.076
chlorpromazine
-
pH 8.4, 37C, recombinant mutant L360Q His6-tagged MBT-fusion-FMO3
0.08
chlorpromazine
-
pH 8.4, 37C, 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
1.2
cysteamine
-
-
0.013
demeton-O
-
pH 9.0, isozyme FMO1
0.25
demeton-O
-
pH 9.0, isozyme FMO3
0.014
Deprenyl
-
-
0.018
dimethylaniline
-
-
0.02
dimethylaniline
-
-
0.044
dimethylaniline
-
-
0.101
ethiofencarb
-
pH 9.0, isozyme FMO1
1.45
ethiofencarb
-
pH 9.0, isozyme FMO3
0.104
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37C
0.105
Ethionamide
-
37C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37C
0.114
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO3
0.261
Ethionamide
-
37C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37C
0.336
Ethionamide
-
37C, isozyme FMO3
2.131
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37C
0.0502
ethylenethiourea
-
recombinant mutant K416N, pH 8.5
0.0557
ethylenethiourea
-
recombinant wild-type enzyme, pH 8.5
0.0761
ethylenethiourea
-
recombinant mutant E24D, pH 8.5
40
ethylhydrazine
-
-
0.145
fenthion
-
wild-type enzyme, FMO3
0.15
fenthion
-
mutant enzyme D132H, FMO3
0.2
fenthion
-
mutant enzyme K158L, FMO3
0.22
fenthion
-
mutant enzyme K158L/D132H, FMO3
0.24
fenthion
-
mutant enzyme I303T, FMO1
0.3
fenthion
-
mutant enzyme R502X, FMO1
0.32
fenthion
-
mutant enzyme H97Q, FMO1
0.34
fenthion
-
wild-type enzyme, FMO1
0.351
fenthion
-
mutant enzyme I303V, FMO1
0.0047
imipramine
-
37C
0.0078
imipramine
-
37C
0.014
imipramine
-
mutant enzyme I303T, FMO1; wild-type enzyme, FMO1
0.015
imipramine
-
mutant enzyme H97Q, FMO1
0.016
imipramine
-
mutant enzyme R502X, FMO1
0.02
imipramine
-
mutant enzyme I303V, FMO1
0.005
indole
Q83XK4
wild-type, pH 8.0, temperature not specified in the publication
0.008
indole
Q83XK4
mutant Y207S, pH 8.0, temperature not specified in the publication
0.09
indole
-
pH 8.5, 25C
8.3
isopropylhydrazine
-
-
2.8
L-methionine
-
pH 7.6, 37C, purified FMO3 from kidney
3.4
L-methionine
-
pH 7.6, 37C, purified FMO3 from liver
6.5
L-methionine
-
recombinant FMO3, pH 7.4, 37C
10
L-methionine
-
above, recombinant FMO4, pH 7.4, 37C
30
L-methionine
-
recombinant FMO2, pH 7.4, 37C
48
L-methionine
-
recombinant FMO1, pH 7.4, 37C
0.143
lidocaine
-
pH 8.0, 25C
0.018
mercaptoimidazole
-
pH 8.4, 37C, recombinant wild-type His6-tagged MBT-fusion-FMO3
0.02
mercaptoimidazole
-
pH 8.4, 37C, recombinant mutant H360P His6-tagged MBT-fusion-FMO1
0.022
mercaptoimidazole
-
pH 8.4, 37C, recombinant mutant L360Q His6-tagged MBT-fusion-FMO3
0.03
mercaptoimidazole
-
pH 8.4, 37C, recombinant wild-type His6-tagged MBT-fusion-FMO1
0.034
mercaptoimidazole
-
pH 8.4, 37C, recombinant mutant L360P His6-tagged MBT-fusion-FMO3
0.038
mercaptoimidazole
-
pH 8.4, 37C, recombinant mutant L360H His6-tagged MBT-fusion-FMO3
0.0437
mercaptoimidazole
-
pH 8.4, 37C, recombinant FMO3
0.046
mercaptoimidazole
-
pH 8.4, 37C, recombinant mutant L360A His6-tagged MBT-fusion-FMO3
0.0527
mercaptoimidazole
-
pH 8.4, 37C, recombinant FMO1
0.007
Methimazole
-
mutant enzyme I303V, FMO1; wild-type enzyme, FMO1
0.0081
Methimazole
-
9.5, 37C, FMO1
0.01
Methimazole
-
pH 7.6, 37C, purified FMO3 from liver
0.014
Methimazole
-
mutant enzyme H97Q, FMO1
0.016
Methimazole
-
mutant enzyme I303T, FMO1
0.0293
Methimazole
-
9.5, 37C, FMO3
0.037
Methimazole
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
0.04
Methimazole
-
pH 7.6, 37C, purified FMO3 from kidney
0.066
Methimazole
-
pH 8.5, 25C
0.0718
Methimazole
-
recombinant wild-type enzyme, pH 8.5
0.0773
Methimazole
-
recombinant mutant K416N, pH 8.5
0.0854
Methimazole
-
recombinant mutant E24D, pH 8.5
0.11
Methimazole
-
pH 8.0, 37C
0.118
Methimazole
-
pH 8.0, 37C, liver microsomes
0.1233
Methimazole
-
recombinant mutant N61K, pH 8.5
0.163
Methimazole
Methylophaga sp.
-
wild-type, pH 8.5, 25C
0.5758
Methimazole
-
9.5, 37C, FMO2.1
0.079
methiocarb
-
pH 9.0, isozyme FMO1
0.0048
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant N413K
0.005
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant S195L
0.0135
methyl p-tolyl sulfide
-
pH 9.0, 37C, wild-type FMO2.1
0.2
methyl p-tolyl sulfide
-
mutant enzyme R502X, FMO1
0.245
methyl p-tolyl sulfide
-
mutant enzyme I303T, FMO1
0.251
methyl p-tolyl sulfide
-
mutant enzyme H97Q, FMO1
0.284
methyl p-tolyl sulfide
-
wild-type enzyme, FMO1
0.3
methyl p-tolyl sulfide
-
mutant enzyme I303V, FMO1
3.6
methyl p-tolyl sulfide
-
pH 8.5, FMO1
10.2
methyl p-tolyl sulfide
-
pH 8.5, FMO2
0.0068
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37C, recombinant FMO1
0.0245
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37C, recombinant FMO3
0.0808
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
-
pH 8.4, 37C, recombinant FMO5
0.0445
N,N-dimethylamphetamine
-
pH 7.4, 37C, FMO1
0.261
N,N-dimethylamphetamine
-
pH 7.4, 37C, FMO3
0.232
N,N-Dimethylaniline
-
pH 8.5, 25C
0.17
N-Aminohomopiperidine
-
-
0.61
N-aminomorpholine
-
-
0.03
N-Aminopiperidine
-
-
0.1
N-aminopyrrolidine
-
-
0.008
N-methyl-1,2,3,4-tetrahydroisoquinoline
-
-
15
n-propylhydrazine
-
-
0.0041
NADPH
Methylophaga sp.
-
wild-type, pH 8.5, 25C
0.0043
NADPH
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
0.0068
NADPH
-
pH 9.0, 37C, mutant N413K
0.0115
NADPH
-
pH 9.0, 37C, wild-type FMO2.1
0.013
NADPH
-
pH 8.5, 25C
0.028
NADPH
-
with dimethylaniline
0.05
NADPH
-
with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
0.132
NADPH
-
pH 9.0, 37C, mutant S195L
0.13
Nicotine
-
pH 8.5, 25C
0.019
O2
Methylophaga sp.
-
wild-type, pH 8.5, 25C
0.042
O2
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
0.043
O2
-
with dimethylaniline
0.049
O2
-
with dimethylaniline
0.0871
p-tolyl sulfide
-
37C
0.0986
p-tolyl sulfide
-
37C
0.012
Pargyline
-
-
3
phenylhydrazine
-
-
5.7
procarbazine
-
-
0.21
propranolol
-
pH 8.0, 25C
0.147
pyrazoloacridine
-
-
4.3
S-allyl-L-cysteine
-
pH 7.6, 37C, purified FMO3 from kidney
5.9
S-allyl-L-cysteine
-
pH 7.6, 37C, purified FMO3 from liver
0.0713
selegiline
-
pH 8.0
0.1775
selegiline
-
pH 7.4
0.31
seleno-L-methionine
-
pH 7.6, 37C, purified FMO3 from liver
0.35
seleno-L-methionine
-
pH 7.6, 37C, purified FMO3 from kidney
0.0665
sulindac
-
recombinant mutant K416N, pH 8.5
0.0693
sulindac
-
pH 9.0, 37C
0.1208
sulindac
-
recombinant mutant E24D, pH 8.5
0.1501
sulindac
-
recombinant wild-type enzyme, pH 8.5
0.2071
sulindac
-
recombinant mutant N61K, pH 8.5
0.043
tamoxifen
-
pH 8.5, 37C, recombinant isozyme FMO1 and recombinant mutant isozyme FMO3 E158K
0.121
tamoxifen
-
pH 8.5, 37C, recombinant wild-type isozyme FMO3
0.0058
thiacetazone
-
9.5, 37C, FMO2.1
0.0063
thiacetazone
-
9.5, 37C, FMO1
0.007
thiacetazone
-
9.5, 37C, FMO3
0.131
thiacetazone
-
recombinant EtaA, pH 9.0, 37C, thiacetazone sulfinic acid formation
0.147
thiacetazone
-
recombinant EtaA, pH 9.0, 37C, thiacetazone carbodiimide formation
0.027
Thiourea
-
-
0.0015
trimethylamine
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
0.0026
trimethylamine
Methylophaga sp.
-
wild-type, pH 8.5, 25C
0.00875
trimethylamine
-
pH 8.4, 37C, recombinant FMO3
0.0209
trimethylamine
-
recombinant wild-type enzyme, pH 8.5
0.0228
trimethylamine
-
recombinant mutant E24D, pH 8.5
0.0373
trimethylamine
-
recombinant mutant K416N, pH 8.5
0.073
trimethylamine
-
pH 8.5, 25C
3
voriconazole
-
pH 7.4, 37C, recombinant FMO1
3.4
voriconazole
-
pH 7.4, 37C, recombinant FMO3
35
methylhydrazine
-
-
additional information
additional information
-
-
-
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
-
-
-
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
-
Michaelis-Menten kinetics
-
additional information
additional information
-
MichaelisMenten 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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, recombinant MBP-FMO3
0.19
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is CHAPS, recombinant MBP-FMO3
0.22
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, recombinant MBP-FMO3
0.55
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, commercial recombinant FMO3
0.67
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is CHAPS, commercial recombinant FMO3
0.72
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, commercial recombinant FMO3
0.805
Ethionamide
-
37C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37C
0.973
Ethionamide
-
37C, isozyme FMO3
1.01
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO3
1.5
Ethionamide
-
37C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37C
4.52
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO1; isozyme FMO1, at pH 9.5 and 37C
9.45
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO2; isozyme FMO2, at pH 9.5 and 37C
0.036
ethylenethiourea
-
recombinant wild-type enzyme, pH 8.5
0.042
ethylenethiourea
-
recombinant mutant K416N, pH 8.5
0.05
ethylenethiourea
-
recombinant mutant E24D, pH 8.5
0.7
indole
-
pH 8.5, 25C
0.004
Methimazole
-
recombinant mutant N61K, pH 8.5
0.038
Methimazole
-
9.5, 37C, FMO1
0.043
Methimazole
-
9.5, 37C, FMO3
0.047
Methimazole
-
recombinant mutant K416N, pH 8.5
0.124
Methimazole
-
recombinant wild-type enzyme, pH 8.5
0.22
Methimazole
-
recombinant mutant E24D, pH 8.5
0.525
Methimazole
-
9.5, 37C, FMO2.1
0.67
Methimazole
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
1
Methimazole
-
pH 8.5, 25C
2.7
Methimazole
Methylophaga sp.
-
wild-type, pH 8.5, 25C
1.25
methyl p-tolyl sulfide
-
pH 8.5, FMO2
2.9
methyl p-tolyl sulfide
-
pH 8.5, FMO1
10
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant S195L
42.3
methyl p-tolyl sulfide
-
pH 9.0, 37C, wild-type FMO2.1
71.1
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant N413K
1.8
N,N-Dimethylaniline
-
pH 8.5, 25C
0.1
N-methyl-tamoxifen
-
about, recombinant isozyme FMO3
0.33
N-methyl-tamoxifen
-
about, recombinant isozyme FMO1
0.06
NADPH
-
pH 8.5, 25C
0.92
NADPH
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
7.3
NADPH
Methylophaga sp.
-
wild-type, pH 8.5, 25C
15.2
NADPH
-
pH 9.0, 37C, mutant S195L
23.6
NADPH
-
pH 9.0, 37C, wild-type FMO2.1
94.4
NADPH
-
pH 9.0, 37C, mutant N413K
3
Nicotine
-
pH 8.5, 25C
2.7
O2
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
7.7
O2
Methylophaga sp.
-
wild-type, pH 8.5, 25C
0.003
sulindac
-
recombinant mutant N61K, pH 8.5
0.044
sulindac
-
recombinant mutant E24D, pH 8.5
0.047
sulindac
-
recombinant wild-type enzyme, pH 8.5
0.068
sulindac
-
recombinant mutant K416N, pH 8.5
1.02
tamoxifen
-
pH 8.5, 37C, recombinant wild-type isozyme FMO3
1.7
tamoxifen
-
pH 8.5, 37C, recombinant mutant isozyme FMO3 E158K
3.18
tamoxifen
-
pH 8.5, 37C, recombinant isozyme FMO1
0.023
thiacetazone
-
9.5, 37C, FMO3
0.048
thiacetazone
-
recombinant EtaA, pH 9.0, 37C, thiacetazone carbodiimide formation
0.085
thiacetazone
-
recombinant EtaA, pH 9.0, 37C, thiacetazone sulfinic acid formation
0.085
thiacetazone
-
9.5, 37C, FMO1
1.335
thiacetazone
-
9.5, 37C, FMO2.1
0.034
trimethylamine
-
recombinant wild-type enzyme, pH 8.5
0.051
trimethylamine
-
recombinant mutant K416N, pH 8.5
0.065
trimethylamine
-
recombinant mutant E24D, pH 8.5
1.25
trimethylamine
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
6.1
trimethylamine
-
pH 8.5, 25C
6.1
trimethylamine
Methylophaga sp.
-
wild-type, pH 8.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is CHAPS, recombinant MBP-FMO3
6382
0.0057
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, recombinant MBP-FMO3
6382
0.0143
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, recombinant MBP-FMO3
6382
0.0152
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is a minimal detergent, commercial recombinant FMO3
6382
0.027
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine
-
pH 8.5, 37C, detergent is Triton X-100, commercial recombinant FMO3
6382
0.0028
Ethionamide
-
37C, isozyme FMO3
2142
0.0032
Ethionamide
-
37C, isozyme FMO2
2142
0.0035
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO2
2142
0.0088
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO3
2142
0.014
Ethionamide
-
37C, isozyme FMO1
2142
0.044
Ethionamide
P50285, Q8K2I3
37C, isozyme FMO1
2142
0.0091
Methimazole
-
9.5, 37C, FMO2.1
1144
0.015
Methimazole
-
9.5, 37C, FMO3
1144
0.0469
Methimazole
-
9.5, 37C, FMO1
1144
16
Methimazole
Methylophaga sp.
-
wild-type, pH 8.5, 25C
1144
18
Methimazole
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
1144
0.0022
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant S195L
3526
0.0033
methyl p-tolyl sulfide
-
pH 9.0, 37C, wild-type FMO2.1
3526
0.0149
methyl p-tolyl sulfide
-
pH 9.0, 37C, mutant N413K
3526
0.00014
NADPH
-
pH 9.0, 37C, mutant S195L
5
0.0068
NADPH
-
pH 9.0, 37C, wild-type FMO2.1
5
0.0144
NADPH
-
pH 9.0, 37C, mutant N413K
5
210
NADPH
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
5
1800
NADPH
Methylophaga sp.
-
wild-type, pH 8.5, 25C
5
60
O2
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
9
410
O2
Methylophaga sp.
-
wild-type, pH 8.5, 25C
9
0.0033
thiacetazone
-
9.5, 37C, FMO3
5018
0.0132
thiacetazone
-
9.5, 37C, FMO1
5018
0.238
thiacetazone
-
9.5, 37C, FMO2.1
5018
800
trimethylamine
Methylophaga sp.
-
mutant W47F, pH 8.5, 25C
734
2300
trimethylamine
Methylophaga sp.
-
wild-type, pH 8.5, 25C
734
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
0.2
propranolol
-
pH 8.0, 25C, inhibition of reaction with lidocaine
0.008 - 0.013
indole-3-carbinol
-
-
additional information
additional information
-
inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
HgCl2
-
IC50: 4.7 mM, liver microsomes
77.5
MgCl2
-
IC50: 77.5 mM, liver microsomes
4
n-octylamine
-
IC50: 4 mM, liver microsomes
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000163
-
male dog liver microsomes, substrate benzydamine
0.0000367
-
female dog liver microsomes, substrate benzydamine
0.0015
-
purified recombinant FMO5, substrate 5-DPT
0.00238
-
liver microsomes, substrate methimazole
0.00373
-
liver microsomes, substrate imipramine
0.00375
-
liver microsomes, substrate chlorpromazine
0.0038
-
liver microsomes, substrate methimazole
0.0046 - 0.0073
-
recombinant wild-type and mutant His6-tagged MBT-fusion-FMO3s
0.0061
-
liver microsomes, substrate methimazole in presence of 0.1% Triton X-100
0.0107
-
liver microsomes, substrate imipramine
0.012
-
purified recombinant FMO5, substrate 8-DPT
0.0123
-
liver microsomes, substrate chlorpromazine
0.018
-
purified recombinant FMO3, substrate 3-DPT
0.041
-
purified recombinant FMO3, substrate 5-DPT
0.069
-
purified recombinant FMO3, substrate 8-DPT
0.122
-
activity with bupivacaine
0.141
-
activity with propranolol
0.15
-
purified enzyme, substrate L-methionine
0.176
-
activity with lidocaine
0.195
-
purified recombinant FMO1, substrate 3-DPT
0.294
-
purified recombinant FMO1, substrate 8-DPT
0.407
-
purified recombinant FMO1, substrate 5-DPT
0.41
-
thiobenzamide S-oxidase activity, FMO-II
0.436
-
thiobenzamide S-oxidase activity, FMO-I
0.52
-
thiourea
1.43
-
-
2.4
-
thiourea
6.2
-
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
substrate specificities of isozymes, overview
additional information
-
substrate specificity of recombinant wild-type and mutant His6-tagged MBT-fusion-FMO3s, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Q9HFE4
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 9
-
assay at
7.4 - 9
-
assay pH depends on the substrate
7.4 - 9.5
-
assay at
7.4
-
assay at
7.6
-
N,N-dimethylaniline, immobilized enzyme
7.6
-
assay at
8.3
-
assay at
8.4
-
-
8.4
-
demethylation of 1,1-dimethylhydrazine
8.4
-
p-tolyl sulfide S-oxidase activity
8.4
-
assay at
8.4
-
assay at
8.5 - 9.5
-
assay at
8.5
-
hydrazine oxidation
8.5
-
assay at
8.5
-
FMO1 and FMO3
8.5
P97501
assay at
8.8 - 9
-
liver, thiobenzamide S-oxidation
8.8
-
imipramine N-oxidase activity
9 - 10
-
-
9
Methylophaga sp.
-
recombinant PTDH-mFMO
9.5
-
FMO2.1
9.5
-
higher activity compared to pH 8.5
9.8
-
thiobenzamide S-oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
-
pH profile
6 - 11
P49326
-
6.5 - 10
-
isozyme FMO1, pH profile
6.5 - 10
-
pH profile
7 - 11
-
pH profile for the recombinant FMO1, FMO3, and FMO5, overview
7.4 - 8.4
Q01740, Q9HA79
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
7.5 - 10
-
isozyme FMO3, pH profile
7.5 - 9
-
pH 7.5: about 40% of activity maximum, pH 9.0: about 95% of activity maximum
7.5 - 9.5
-
-
7.6 - 9
-
S-oxidase activity incrases from pH 7.6-9.0
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
8.4 - 10.4
-
about 50% of activity maximum at pH 8.4 and 10.4, lung, thiobenzamide S-oxidation
8.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
-
assay at
25 - 28
-
N,N-dimethylaniline, immobilized enzyme
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
P50285, Q8K2I3
assay at
37
-
assay at
37
P97501
assay at
70
Methylophaga sp.
-
recombinant PTDH-mFMO
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 65
-
temperature profile
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
prepared from forebrain of 1-day old Swiss Webster mice
Manually annotated by BRENDA team
P31512, P49326
-
Manually annotated by BRENDA team
A0SZ82
primary hepatic amd gill epithelial cells
Manually annotated by BRENDA team
-
recombinant enzymes expressed in insect cells
Manually annotated by BRENDA team
P31512, P49326
-
Manually annotated by BRENDA team
-
adult and fetal, high expression level of FMO1
Manually annotated by BRENDA team
Q01740
expression of the FMO1 gene is not silenced postnatally in kidney
Manually annotated by BRENDA team
P50285
expression of the FMO1 gene is not silenced postnatally in liver and kidney
Manually annotated by BRENDA team
-
FMO1 is expressed primarily in the kidney and the fetal liver
Manually annotated by BRENDA team
P36365, Q8K4B7
FMO1 shows low expression
Manually annotated by BRENDA team
P36365, Q8K4B7
FMO3 is expressed in the renal collecting tubules, in renal medulla, and in renal glomerulus
Manually annotated by BRENDA team
P36365, Q8K4B7
FMO4 is expressed in the renal collecting tubules, in renal medulla, and in renal glomerulus
Manually annotated by BRENDA team
P31512
no expression of FMO1, but of FMO4
Manually annotated by BRENDA team
-
most abundantly expressed
Manually annotated by BRENDA team
Mus musculus C-57 BL
-
-
-
Manually annotated by BRENDA team
Q93Y23
rosette leaf
Manually annotated by BRENDA team
-
predominantly
Manually annotated by BRENDA team
-
adult and fetal
Manually annotated by BRENDA team
-
male and female
Manually annotated by BRENDA team
-
FMO3 is the major FMO
Manually annotated by BRENDA team
-
adult liver
Manually annotated by BRENDA team
-
expression analysis of FMO3 in liver and after treatment with conjugated linoleic acid isomers
Manually annotated by BRENDA team
-
isozyme FMO1
Manually annotated by BRENDA team
-
isozyme FMO3
Manually annotated by BRENDA team
-
isozyme FMO3
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
P31512, P49326
birth is necessary but not sufficient for FMO3 onset in the liver, it occurs between week 3 and 10 after birth
Manually annotated by BRENDA team
P50285
expression of the FMO1 gene is not silenced postnatally in liver and kidney
Manually annotated by BRENDA team
Q01740
expression of the FMO1 gene is silenced postnatally in liver
Manually annotated by BRENDA team
-
FMO1, FMO3, and FMO5
Manually annotated by BRENDA team
P31512, P49326
high level expression in adult liver
Manually annotated by BRENDA team
-
FMO1 is expressed primarily in the kidney and the fetal liver
Manually annotated by BRENDA team
-
FMO1 is the major isozyme in liver
Manually annotated by BRENDA team
P36365, Q8K4B7
FMO4 occurs in lobular distribution
Manually annotated by BRENDA team
P36365, Q8K4B7
highest expression of FMO1 in the perivenous region
Manually annotated by BRENDA team
P36365, Q8K4B7
highest expression of FMO3 in the perivenous region
Manually annotated by BRENDA team
P31512
no expression of FMO1, but of FMO4
Manually annotated by BRENDA team
-
FMO3 and FMO5 are the predominant FMO forms in adult liver
Manually annotated by BRENDA team
-
in human fetal liver, the major isozyme is FMO1
Manually annotated by BRENDA team
-
most abundantly expressed
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
Mus musculus C-57 BL
-
predominantly
-
Manually annotated by BRENDA team
-
high expression of isozyme FMO2
Manually annotated by BRENDA team
-
isozyme FMO2
Manually annotated by BRENDA team
-
low expression of isozyme FMO2
Manually annotated by BRENDA team
-
lung isozyme FMO2
Manually annotated by BRENDA team
P31512, P49326
FMO2 mainly
Manually annotated by BRENDA team
-
isozyme FMO2 is expressed at high levels in lung
Manually annotated by BRENDA team
P31512, P49326
FMO1, expression profiling in tissue from patients with atrial fibrillation
Manually annotated by BRENDA team
-
reduced expression in amyotrophic lateral sclerosis
Manually annotated by BRENDA team
Mus musculus C-57 BL
-
-
-
Manually annotated by BRENDA team
additional information
-
not activity in brain A
Manually annotated by BRENDA team
additional information
-
differential expression of isozymes in tissues
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
P31512, P49326
broad tissue distribution, overview
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
P31512, P49326
tissue-specific and devlopmental expression of FMO3, overview
Manually annotated by BRENDA team
additional information
-
tissue-specific expression of FMO isozymes, quantitative expression analysis, overview
Manually annotated by BRENDA team
additional information
P31512, P49326
tissue-specific expression of FMO1, overview
Manually annotated by BRENDA team
additional information
P31512, P49326
tissue-specific expression of FMO2, overview
Manually annotated by BRENDA team
additional information
P31512, P49326
tissue-specific expression of FMO5, overview, the enzyme is increased in ERalpha-positive tumors
Manually annotated by BRENDA team
additional information
-
specific isozyme localization patterns, overview
Manually annotated by BRENDA team
additional information
P31512
specific isozyme localization patterns, overview
Manually annotated by BRENDA team
additional information
-
recombinant FMO1
Manually annotated by BRENDA team
additional information
-
no activity in fetal human liver, intestine, and kidney
Manually annotated by BRENDA team
additional information
Mus musculus C-57 BL
-
not activity in brain A
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
membrane-bound
-
Manually annotated by BRENDA team
-
isozyme FMO3
-
Manually annotated by BRENDA team
-
the highly hydrophobic FMO shows multiple internal sites of membrane association
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J, Mus musculus C-57 BL
-
-
-
-
Manually annotated by BRENDA team
Methylophaga sp.
-
-
-
Manually annotated by BRENDA team
Methylophaga aminisulfidivorans SK1, Methylophaga sp. SK1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
Western blot, anti-FMO 2 antisera
348501
54000
-
SDS-PAGE, FMO-I
348496
55000 - 60000
-
SDS-PAGE, amino acid composition
348493
55000
-
Western blot, anti-FMO1 and anti-FMO2 (mammalian) antisera
348509
56000 - 59000
-
SDS-PAGE
348489
56000
-
SDS-PAGE, FMO-II
348496
56000
-
SDS-PAGE, gel filtration
348505
56000
-
SDS-PAGE
348513
58000
-
recombinant protein expressed in E. coli
348504
58950
-
calculation from amino acid sequence
348494
59000
-
SDS-PAGE
348506
60000
-
Western blot, anti-rat liver FMO antisera
348503
60000
-
recombinant protein expressed in E. coli
348504
64000
-
SDS-PAGE
348488
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
KC734478, KC734481, KC734482, KC734486
x * 65000, SDS-PAGE
?
-
x * 64000, SDS-PAGE, active enzyme exists as aggregating units of the monomer, amino acid composition
?
-
x * 56000, FMO-II, SDS-PAGE, x * 54000, FMO-I, SDS-PAGE
?
-
x * 58952, calculation from amino acid sequence
?
P31512, P49326
x * 60047, sequence calcualtion
?
P31512, P49326
x * 63338, sequence calculation
?
-
x * 56000, kidney enzyme, SDS-PAGE
?
-
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation
dimer
-
2 * 53000, SDS-PAGE
dimer
Methylophaga aminisulfidivorans SK1
-
2 * 53000, SDS-PAGE
-
homodimer
Methylophaga sp.
-
2 * 54000, SDS-PAGE
homodimer
Methylophaga sp. SK1
-
2 * 54000, SDS-PAGE
-
octamer
-
8 * 65000, SDS-PAGE
monomer
-
1 * 56000, gel filtration
additional information
-
molecular modeling of the FMO3 structure
additional information
-
structure motifs, overview, structural modeling
additional information
Q9HFE4
the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
FMO1 is selectively N-glycosylated at Asn120, N-glycosylation is not essential for functional activity
glycoprotein
-
amino acid analysis
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
Q83XK4
mutant E158A/E159A, ligand-free or in complex with NADP+, microbatch technique at 4C 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
Q9HFE4
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
P97872
almost complete loss of activity
724245
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
-
15C, 76% loss of activity, 45C 99% loss of activity
348501
24
-
liver microsomes, enzyme inactivation after 20 days
672958
35
Methylophaga sp.
-
purified recombinant PTDH-mFMO, half-life is 5 h
713168
37
-
liver microsomes, enzyme inactivation after 48 h
672958
38
-
pH 7.6, half-life of free enzyme: 10 min, half-life of immobilized enzyme 5 h
348486
40
-
in absence of NADPH, residue 360 is important for thermal stability, half-lives of wild-type and mutant isozymes FMO1 and FMO3, overview
673296
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 40C, 61% to 71% after 2 min preincubation, and 41% to 55% after 5 min preincubation
687477
50
-
the enzyme is unstable in absence of NADPH
671729
50
-
liver microsomes, enzyme inactivation after 1.5 h
672958
50
-
10 min, elimination of most Fmo1 and Fmo3 activity, while 94% of Fmo2 activity remains
685036
60
-
90 s, inactivation of FMO in liver microsomes
706921
65
-
liver microsomes, enzyme inactivation after 5 min
672958
additional information
-
the lung isozyme shows high thermal stability as the liver isozyme
676315
additional information
-
loss of about 30% of activity after heat treatment of mutant enzyme N413K, activity is preservable by NADPH
703409
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADPH stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, several months with little or no loss of activity
-
glass-bead immobilized enzyme: 0-4C, 0.025 M phosphate buffer, several months with little or no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms: FMO-I and FMO-II
-
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
P49326
recombinant wild-type and mutant FMO3 from Escherichia coli strain JM109 in a multistep process
-
N-terminal amino acid sequence
-
one-step purification of the recombinant PTDH-mFMO from Escherichia coli by nickel affinity chromatography
Methylophaga sp.
-
recombinant maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 from Escherichia coli by amylose affinity chromatography
-
recombinant protein
P97872
recombinant His-tagged EtaA from Escherichia coli strain DH5alpha by nickel affinity chromatography
-
isozyme from lung microsomes
-
native enzyme from lung microsomes
-
native FMO3 130fold from kidney microsomes
-
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q9HFE4
amino acid composition
-
from liver microsomes
-
native enzyme from liver microsomes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of the FMO1 cDNA under control of the 35S CaMV promoter in independent transgenic Col-0 lines
-
whole genome microarrays to examine the EDS1 regulatory node in disease resistance and correlation of FMO1 expression, overview
Q9LMA1
gene tetX, expression in Escherichia coli confers antibiotic resistance
-
FMO3 cDNA from liver, DNA and amino acid sequence determination and analysis, expression in Spodoptera frugiperda Sf9 insect cells
-
using a baculovuirus expression system in Sf-9 insect cells, dFMO1 is expressed to protein levels of 0.4 nM/mg
-
FMO, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21 (DE3)
Q93Y23
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
-
DNA sequence determination and analysis, and genotyping
-
expressed in Sf9 insect cells; expressed in Sf9 insect cells
-
expressed in Trichoplusia ni cells using a baculovirus expression vector system
-
expression as maltose-binding fusion proteins in Escherichia coli
P49326
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 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 wild-type and mutant FMO3 in Escherichia coli strain JM109
-
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
P31512
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
P31512, P49326
FMO3 cDNA from liver, expression in Spodoptera frugiperda Sf9 insect cells
-
FMO3, DNA and amino acid sequence determination and analysis, genotyping
-
FMO3, genotyping in relation to gender, age, race/ethnic, and FMO3 expression in response to administration of the anti-schizophrenia drug olanzapine
P31513
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
Q01740
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
-
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
-
missense mutations causing fish-odour syndrome
-
using a baculovuirus expression system in Sf-9 insect cells, dFMO1 is expressed to protein levels of 0.4 nM/mg
-
expression in Escherichia coli
Q83XK4
expression in Escherichia coli
Methylophaga sp.
-
overexpression of PTDH-mFMO fusion protein in Escherichia coli
Methylophaga sp.
-
expressed in Sf9 insect cells; expressed in Sf9 insect cells
P50285, Q8K2I3
expression analysis of FMO3 in liver and after treatment with conjugated linoleic acid isomers
-
expression as maltose-binding fusion proteins in Escherichia coli
P97872
expression of maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 in Escherichia coli
-
FMO isozyme expression patterns, expression analysis
-
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
P50285
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
-
quantitative Fmo isozyme expression analysis in female C3H/HeOuJ and C57BL/6 mice
-
expression of His-tagged EtaA in Escherichia coli strain DH5alpha
-
cDNA from liver, DNA and amino acid sequence determination and analysis, genomic structure and sequence comparison, expression analysis
A0SZ82
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
P17635
functional expression of isozymes FMO1-FMO3, in Escherichia coli
-
expression in yeast cells
-
FMO isozyme expression patterns, expression analysis; FMO isozyme expression patterns, expression analysis; FMO isozyme expression patterns, expression analysis
P36365, Q8K4B7
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q9HFE4
cDNA data
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
FMO3 expression in response to administration of the anti-schizophrenia drug olanzapine, allele frequencies and phenotypes, overview
P31513
in female mice, testosterone plays a role in negative FMO regulation
-
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
-
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
P97501
liver FMO1 is upregulated in diabetic mice
-
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
P97501
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively
P50285, P97501, P97872, Q8K2I3, Q8VHG0
isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively
P50285, P97501, P97872, Q8K2I3, Q8VHG0
isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
P50285, P97501, P97872, Q8K2I3, Q8VHG0
isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview
Mus musculus C57BL/6J
-
-
isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively
Mus musculus C57BL/6J
-
-
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively
Mus musculus C57BL/6J
-
-
isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
Mus musculus C57BL/6J
-
-
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
A0SZ82
downregulation of FMO1 and FMO3 by glucocorticoids and progesterone
-
bacterial lipopolysaccharides lead to enzyme downregulation in the liver, as well as posttranslationally S-nitrosylation by nitric oxide
-
liver FMO1 is upregulated in diabetic rats
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A52T
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
C530L
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
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
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows substrate-dependent reduced activity
D198E
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
D227K
P49326
pKa value 7.3 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
D36G
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
down
-
FMO5 is downregulated in type II diabetes in liver. FMO1 downregulation and inhibition by 3,3'-diindolylmethane
E132H
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E132H/E158K
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K
-
major naturally occuring structural varainat of isozyme FMO3, the mutant shows increased activity with tamoxifen compared to the wild-type enzyme
E158K
-
natural genetic variant of isozymes FMO2 and FMO3, substrate specificity, overview
E158K
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E158K
-
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 mutation not involved in primary trimethylaminuria
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
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly affects enzyme activity, substrate-dependent reduced activity
E158K/E308G
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E158K/E308G
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K/E308G
-
naturally occuring polymorphism, in many cases in vivo, altered clinical responses or altered susceptibility to various chemicals due to these sequence variants are observed compared to the carriers of at least one wild-type allele
E158K/E308G
-
naturally occuring mutation not involved in primary trimethylaminuria
E158K/E308G
-
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
E158K/E308G
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutation affects enzyme activity, substrate-dependent reduced activity
E158K/T201K/E308G
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
E158K/V257M
-
the naturally occuring polymorphisms reduce the oxidation and clearance of FMO3 substrates such as tyramine, and TMA in vitro, and mutations are highly likely to eliminate the enzyme function in vivo
E24D
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview, the mutant shows altered substrate specificity compared to the wild-type mutant
E24D
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
E305X
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E308G
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
E308G
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview
E308G
-
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 mutation not involved in primary trimethylaminuria
E308G
-
naturally occuring single nucleotide polymorphism of FMO3 in Europeans and Asians, the mutation slightly affects enzyme activity, substrate-dependent reduced activity, phenotype, overview
E308G
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutation slightly affects enzyme activity, substrate-dependent reduced activity
E314G
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
E314X
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E32K
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
E339Q
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
E362Q
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3
F182S
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
F510X
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
F69Y
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
F81S
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
G148X
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
G180V
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant is similar to the wild-type enzyme
G182E
P49326
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
G475D
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
G503R
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3
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
-
KM-value for methimazole is 3fold higher than wild-type value, Vmax with methimazole is 1.6fold higher than the wild-type value, KM-value for methyl p-tolyl sulfide is 88% of the wild-type value, Vmax with methyl p-tolyl sulfide is 1.4fold higher than the wild-type value, KM-value for imipramine is is nearly identical to the the wild-type value, Vmax with imipramine is 1.3fold higher than the wild-type value, KM-value for fenthion is 94% of the wild-type value, Vmax with fenthion is 1.3fold higher than the wild-type value, mutant of FMO1
H97Q
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
H97Q
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO1, the mutant enzyme is similar to the wild-type enzyme
I199T
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
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
P31512, P49326
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
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO1, the mutant enzyme is similar to the wild-type enzyme
I37T
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
I37T
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
I468M
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3
K158L
-
Km-value for fenthion is 1.4fold higher than the wild-type value, Vmax for fenthion is nearly identical to the wild-type value, mutant of FMO3
K158L/D132H
-
Km-value for fenthion is 1.5fold higher than the wild-type value, Vmax for fenthion is 1.5fold higher than the wild-type value, mutant of FMO3
K416N
-
naturally occuring polymorphism of FMO3, frequency in different human populations, the mutation has an impact on protein structure, overview, the mutant shows altered substrate specificity compared to the wild-type mutant
K416N
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
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
-
natural genetic variant of isozyme FMO2, substrate specificity, overview
L360P
-
site-directed mutagenesis of isozyme FMO3, the mutant shows altered thermal stability and increased activity with mercaptoimidazole, chlorpromazine, and 10-[(N,N-dimethylaminopentyl)-2-(trifluoromethyl)]phenothiazine compared to the wild-type FMO3
L360P
Q99518
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows increased activity
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
M260V
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3
M434I
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
M66I
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
M66I
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
N114S
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
N413K
P31512, P49326
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
Q99518
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
N61S
Q99518
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, nuta this mutant is still active with methimazole, phenotype, overview
N61S
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
P153L
P31512, P49326
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
P153L
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
P153L
-
naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme
P457L
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
Q170K
P49326
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
Q206H
P49326
pKa value 6.5 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 6.9 for wild-type
Q470X
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
Q472X
Q99518
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
-
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
R205C
-
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows highly reduced activity
R205C
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows reduced activity
R223Q
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R223Q
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO1
R238P
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R238Q
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
R249X
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2, probably inactive mutant
R378L
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
R391T
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO2
R492W
-
naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor
R500X
P31512, P49326
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
-
natural genetic variant of isozyme FMO1, substrate specificity, overview
R502X
Q99518
naturally occuring single nucleotide polymorphism of FMO1, the mutant shows substrate-dependent reduced activity compared to the wild-type enzyme
R506S
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
R51G
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
S195L
P31512, P49326
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
T201K
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
T308S
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
V143E
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
V257M
-
variant with 13.21% allele frequency. Mutation causes a transformation of the secondary structure. The presence of this mutant allele correlates significantly with a reduction in caffeine N-1-demethylating activity
V257M
-
natural genetic variant of isozyme FMO3, substrate specificity, overview
V257M
-
naturally occuring genetic variant of isozyme FMO3, and site-directed mutagenesis, the mutant shows reduced activity with sulindac and methyl 4-toyl sulfide compared to the wild-type FMO3
V257M
-
loss of function mutation of FMO3 results in trimethylaminuria or fish-odor-syndrome, the mutant enzyme is incapable of metabolizing trimethylamine to its non-odorous N-oxide, phenotype, overview
V257M
-
naturally occuring mutation not involved in primary trimethylaminuria
V257M
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3, the mutant shows slightly reduced activity
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
V277A
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO3
V323A
P31512, P49326
naturally occuring single nucleotide polymorphism of FMO4
V58I
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
W388X
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
Y228H
P49326
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
Q83XK4
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
Methylophaga aminisulfidivorans SK1
-
the mutant shows similar activity with trimethylamine compared to the wild-type enzyme
-
W47A
Methylophaga sp.
-
insoluble inactive protein
W47A
Methylophaga sp. SK1
-
insoluble inactive protein
-
W47F
Methylophaga sp. SK1
-
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
P97872
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
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
Q9LMA1
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
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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
M82T
P31512, P49326
naturally occuring mutation causing trimethylaminuria or fish-odor-syndrome
additional information
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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
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effects of genetic variants of isozyme FMO3 on N- and S-oxygenation activities, genotype-phenotype studies, overview
additional information
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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
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occuring single nucleotide polymorphisms are associated with dramatic functional differences in selective functional enzyme activity, overview
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three of the five expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms, overview
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FMO3 is highly polymorphic, with as many as 15 nonsynonymous single nucleotide polymorphisms identified, many of which are present at relatively high frequency, several single nucleotide polymorphisms cause loss of function mutation of FMO3 resulting in trimethylaminuria or fish-odor-syndrome, the mutant enzymes are incapable of metabolizing trimethylamine to its non-odorous N-oxide, haplotypes and phenotypes, overview
additional information
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genotyping of FMO3 in a Japanese cohort, missense and nonsense mutations, overview
additional information
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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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naturally occuring mutations, including silent mutations, genotyping, overview
additional information
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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
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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
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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
Y207S
Methylophaga aminisulfidivorans SK1
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mutant exhibits very little indoxyl producing activity but the NADPH oxidase activity of the mutant is higher than that of the wild-type enzyme
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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
W47F
Methylophaga sp.
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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+
additional information
Methylophaga sp. SK1
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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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K227D
P97872
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
additional information
P17635
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
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