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Information on EC 1.14.13.8 - flavin-containing monooxygenase and Organism(s) Mus musculus and UniProt Accession P50285

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IUBMB Comments
A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
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Mus musculus
UNIPROT: P50285
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fmo, flavin-containing monooxygenase, flavin monooxygenase, flavin-dependent monooxygenase, flavin-containing monooxygenase 3, fad-containing monooxygenase, flavoprotein monooxygenase, hfmo3, flavin-containing mono-oxygenase, flavin-containing monooxygenase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavin-containing monooxygenase
-
flavin-containing monooxygenase 1
-
dimethylaniline monooxygenase (N-oxide-forming)
-
-
-
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dimethylaniline N-oxidase
-
-
-
-
dimethylaniline oxidase
-
-
-
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DMA oxidase
-
-
-
-
FAD-containing monooxygenase
-
-
-
-
FAD-containing monooxygenase 3
-
-
flavin mono-oxygenase
-
-
flavin monooxygenase
flavin-containing monooxygenase
flavin-containing monooxygenase 5
flavin-containing monooxygenase-3
FMO 1A1
-
-
-
-
FMO 1B1
-
-
-
-
FMO 1C1
-
-
-
-
FMO 1D1
-
-
-
-
FMO 1E1
-
-
-
-
FMO-I
-
-
-
-
FMO-II
-
-
-
-
mixed-function amine oxidase
-
-
-
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N,N-dimethylaniline monooxygenase
-
-
-
-
oxygenase, dimethylaniline mono- (N-oxide-forming)
-
-
-
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oxygenase, methylphenyltetrahydropyridine N-mono-
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
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Baeyer-Villiger reaction
oxidation
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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]
CAS REGISTRY NUMBER
COMMENTARY hide
117910-56-2
-
148848-55-9
-
37256-46-5
-
37256-73-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
hypotaurine + NADH + H+ + O2
taurine + NAD+ + H2O
show the reaction diagram
S-oxygenation
-
-
?
hypotaurine + NADPH + H+ + O2
taurine + NADP+ + H2O
show the reaction diagram
S-oxygenation
-
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
show the reaction diagram
S-oxygenation
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
1-butanethiol + 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
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
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
-
-
-
r
2-acetylsulfanylmethyl-4-(4-methoxyphenyl)-4-oxobutyric acid + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
2-mercaptobenzimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
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
-
-
?
alpha-naphthylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
aminopyrine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
substrate of isoforms FMO1 and FMO3
-
-
?
cysteamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
dibenzylamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
ephedrine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
ethylene sulfide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
imipramine + NADPH + H+ + O2
imipramine N-oxide + NADP+ + H2O
show the reaction diagram
-
substrate of isoform FMO1
-
-
?
imipramine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
mercaptoimidazole + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1 and FMO3, no activity with FMO5
-
-
?
methamphetamine + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
methimazole + NADPH + H+ + O2
?
show the reaction diagram
-
FMO1, FMO2, and FMO3
-
-
?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + 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
-
FMO1, FMO2, but poor substrate of FMO3
-
-
?
methylphenylsulfide + NADPH + O2
?
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-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
-
-
-
-
?
n-decylamine + NADPH + O2
1-nitrosodecane + NADP+ + H2O
show the reaction diagram
-
lung enzyme active, liver enzyme not
-
-
?
n-octylamine + NADPH + O2
1-nitrosooctane + NADP+ + H2O
show the reaction diagram
-
lung enzyme active, liver enzyme not
-
-
?
p-chloro-N-methylaniline + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
pentoxifylline + NADPH + H+ + O2
pentoxifylline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
phenylthiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
S-methyl esonarimod + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
show the reaction diagram
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
thioacetamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiobenzamide + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
thiourea + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
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
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
voriconazole + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hypotaurine + NADH + H+ + O2
taurine + NAD+ + H2O
show the reaction diagram
S-oxygenation
-
-
?
hypotaurine + NADPH + H+ + O2
taurine + NADP+ + H2O
show the reaction diagram
S-oxygenation
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline 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
-
-
?
cysteamine + NADPH + O2
cysteamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ethionamide + NADPH + H+ + O2
ethionamide S-oxide + NADP+ + H2O
show the reaction diagram
ethionamide is a pro-drug requiring bioactivation to exert toxicity
-
-
?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway, high activity by isozyme FMO1
-
-
?
trimethylamine + NADPH + O2
trimethylamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
flavin
NADPH
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Thiourea
thiourea reduces ethionamide oxygenation to ethionamide S-oxide by an average of 73.5% in liver and 76.9% in lung
Phenylthiourea
-
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thiobenzamide
-
-
Thiourea
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
n-octylamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.104
Ethionamide
isozyme FMO1, at pH 9.5 and 37°C
0.117
10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazine
pH 8.4, 37°C
0.0711
4-(4-methoxyphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
-
pH 8.4, 37°C, recombinant FMO1
0.0032 - 0.0038
4-(4-methylphenyl)-2-methylsulfanylmethyl-4-oxobutyric acid
0.104 - 2.131
Ethionamide
0.0437 - 0.0527
mercaptoimidazole
3.6 - 10.2
methyl p-tolyl sulfide
0.0068 - 0.0808
N,N-dimethyl-8-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]octan-1-amine
0.00875
trimethylamine
-
pH 8.4, 37°C, recombinant FMO3
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.52
Ethionamide
isozyme FMO1, at pH 9.5 and 37°C
1.01 - 9.45
Ethionamide
1.25 - 2.9
methyl p-tolyl sulfide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035 - 0.044
Ethionamide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0015
-
purified recombinant FMO5, substrate 5-DPT
0.012
-
purified recombinant FMO5, substrate 8-DPT
0.018
-
purified recombinant FMO3, substrate 3-DPT
0.041
-
purified recombinant FMO3, substrate 5-DPT
0.069
-
purified recombinant FMO3, substrate 8-DPT
0.195
-
purified recombinant FMO1, substrate 3-DPT
0.294
-
purified recombinant FMO1, substrate 8-DPT
0.407
-
purified recombinant FMO1, substrate 5-DPT
2.4
-
thiourea
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
assay at
7.4
assay at
7.4 - 9.5
-
assay at
8.4
-
assay at
8.5
assay at
8.5 - 9.5
-
assay at
8.8 - 9
-
liver, thiobenzamide S-oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
pH profile for the recombinant FMO1, FMO3, and FMO5, overview
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
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of the FMO1 gene is not silenced postnatally in liver and kidney
Manually annotated by BRENDA team
-
prepared from forebrain of 1-day old Swiss Webster mice
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
FMO1 malfunction causes taurine deficiency, which is implicated in a number of pathologic conditions, including cardiomyopathy, muscular abnormalities, and renal dysfunction
physiological function
the formation of taurine from hypotaurine is catalyzed by an FMO in vivo, it is the terminal step of the biosynthetic pathway of taurine production from cysteine
malfunction
-
enzyme-deficient mice are resistant to age-related changes in glucose homeostasis and maintain the higher glucose tolerance and insulin sensitivity characteristic of young animals
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FMO1_MOUSE
532
1
59915
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000 - 59000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure motifs, overview, structural modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H228Y
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
K227D
pKa value 6.6 for N-oxygenation of 10-(N,N-dimethylaminooctyl)2-(trifluoromethyl)phenothiazene, compared with 7.7 for wild-type
additional information
construction of Fmo1-/-, 2-/-, and 4-/- knockout mutants, 1D 1H NMR spectroscopy to compare the urinary metabolite profiles of the knockout-mouse line and wild-type animals, metabolic profiles of hypotaurine and taurine in wild-type and mutant mice' urine samples, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
almost complete loss of activity
724245
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
purified recombinant FMO1, FMO3, and FMO5, the isozymes display similar thermal sensitivity, with activity decreased to 76% to 83% after 1 min preincubation at 40°C, 61% to 71% after 2 min preincubation, and 41% to 55% after 5 min preincubation
50
-
10 min, elimination of most Fmo1 and Fmo3 activity, while 94% of Fmo2 activity remains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preparation of liver microsomes
recombinant maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 from Escherichia coli by amylose affinity chromatography
-
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 insect cells
gene FMO1, DNA and amino acid sequence determination and analysis, the gene contains polyA region, an 80 bp direct repeat, an long terminal, LTR, repeat, a short-interspersed nuclear element, i.e. SINE element, and a poly T tract, expression analysis, expression in Hep-G2 cells
expressed in Sf9 insect cells
expression analysis of FMO3 in liver and after treatment with conjugated linoleic acid isomers
-
expression as maltose-binding fusion proteins in Escherichia coli
expression of maltose-binding protein fusion enzymes FMO1, FMO3, and FMO5 in Escherichia coli
-
FMO isozyme expression patterns, expression analysis
-
gene Fmo5, FMO5 is located at 1q21.1 on chromosome 5, quantitative enzyme expression analysis
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
ORGANISM
UNIPROT
LITERATURE
isozyme Fmo1 is not affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration in contrast to other Fmo isozymes, overview
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
analysis of the diurnal rhythms of Fmo5 expression and activity in mouse liver and of the potential roles of clock genes (Bmal1, Rev-erba, and E4bp4) in the generation of diurnal rhythms. Fmo5 mRNA and protein show robust diurnal rhythms, with peak values at zeitgeber time (ZT) 10/14 and trough values at ZT2/22 in mouse liver. Bmal1 (a known Rev-erba activator) activates Fmo5 transcription via direct binding to an E-box (21822/21816 bp) in the promoter, whereas E4bp4 (a known Rev-erba target gene) inhibits Fmo5 transcription by binding to two D-boxes (21726/21718 and 2804/2796 bp). In conclusion, circadian clock genes control diurnal expression of Fmo5 through transcriptional actions on E-box and D-box cis-elements
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
isozyme Fmo2 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 5fold and 20fold, respectively
isozyme Fmo3 is induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin exposure or castration, 130fold and 180fold, respectively
isozyme Fmo4 is induced by castration, but not by exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin
liver FMO1 is upregulated in diabetic mice
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tynes, R.E.; Sabourin, P.J.; Hodgson, E.
Identification of distinct hepatic and pulmonary forms of microsomal flavin-containing monooxygenase in the mouse and rabbit
Biochem. Biophys. Res. Commun.
126
1069-1075
1985
Oryctolagus cuniculus, Mus musculus
Manually annotated by BRENDA team
Tynes, R.E.; Hodgson, E.
Catalytic activity and substrate specificity of the flavin-containing monooxygenase in microsomal systems: characterization of the hepatic, pulmonary and renal enzymes of the mouse, rabbit, and rat
Arch. Biochem. Biophys.
240
77-93
1985
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Chiba, K.; Kubota, E.; Miyakawa, T.; Kato, Y.; Ishizaki, T.
Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice
J. Pharmacol. Exp. Ther.
246
1108-1115
1988
Mus musculus, Mus musculus C-57 BL
Manually annotated by BRENDA team
Di Monte, D.A.; Wu, E.Y.; Irwin, I.; Delanney, L.E.; Langston, J.W.
Biotransformation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in primary cultures of mouse astrocytes
J. Pharmacol. Exp. Ther.
258
594-600
1991
Mus musculus
Manually annotated by BRENDA team
Rasooly, R.; Kelley, D.S.; Greg, J.; Mackey, B.E.
Dietary trans 10, cis 12-conjugated linoleic acid reduces the expression of fatty acid oxidation and drug detoxification enzymes in mouse liver
Br. J. Nutr.
97
58-66
2007
Mus musculus
Manually annotated by BRENDA team
Krueger, S.K.; Vandyke, J.E.; Williams, D.E.; Hines, R.N.
The role of flavin-containing monooxygenase (FMO) in the metabolism of tamoxifen and other tertiary amines
Drug Metab. Rev.
38
139-147
2006
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Krueger, S.K.; Williams, D.E.
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism
Pharmacol. Ther.
106
357-387
2005
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Shephard, E.A.; Chandan, P.; Stevanovic-Walker, M.; Edwards, M.; Phillips, I.R.
Alternative promoters and repetitive DNA elements define the species-dependent tissue-specific expression of the FMO1 genes of human and mouse
Biochem. J.
406
491-499
2007
Mus musculus (P50285), Mus musculus, Homo sapiens (Q01740), Homo sapiens
Manually annotated by BRENDA team
Siddens, L.K.; Henderson, M.C.; Vandyke, J.E.; Williams, D.E.; Krueger, S.K.
Characterization of mouse flavin-containing monooxygenase transcript levels in lung and liver, and activity of expressed isoforms
Biochem. Pharmacol.
75
570-579
2008
Mus musculus
Manually annotated by BRENDA team
Zhang, J.; Cerny, M.A.; Lawson, M.; Mosadeghi, R.; Cashman, J.R.
Functional activity of the mouse flavin-containing monooxygenase forms 1, 3, and 5
J. Biochem. Mol. Toxicol.
21
206-215
2007
Mus musculus
Manually annotated by BRENDA team
Mitchell, S.
Flavin mono-oxygenase (FMO) - The other oxidase
Curr. Drug Metab.
9
280-284
2008
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Zhang, J.; Chaluvadi, M.R.; Reddy, R.; Motika, M.S.; Richardson, T.A.; Cashman, J.R.; Morgan, E.T.
Hepatic flavin-containing monooxygenase gene regulation in different mouse inflammation models
Drug Metab. Dispos.
37
462-468
2009
Mus musculus
Manually annotated by BRENDA team
Novick, R.M.; Mitzey, A.M.; Brownfield, M.S.; Elfarra, A.A.
Differential localization of flavin-containing monooxygenase (FMO) isoforms 1, 3, and 4 in rat liver and kidney and evidence for expression of FMO4 in mouse, rat, and human liver and kidney microsomes
J. Pharmacol. Exp. Ther.
329
1148-1155
2009
Homo sapiens, Homo sapiens (P31512), Mus musculus, Rattus norvegicus (P36365), Rattus norvegicus (Q8K4B7), Rattus norvegicus (Q9EQ76)
Manually annotated by BRENDA team
Henderson, M.C.; Siddens, L.K.; Morre, J.T.; Krueger, S.K.; Williams, D.E.
Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes
Toxicol. Appl. Pharmacol.
233
420-427
2008
Homo sapiens, Homo sapiens (Q01740), Homo sapiens (Q99518), Mus musculus, Mus musculus (P50285), Mus musculus (Q8K2I3)
Manually annotated by BRENDA team
Novick, R.; Vezina, C.; Elfarra, A.
Isoform distinct time-, dose-, and castration-dependent alterations in flavin-containing monooxygenase expression in mouse liver after 2,3,7,8-tetrachlorodibenzo-p-dioxin treatment
Biochem. Pharmacol.
79
1345-1351
2010
Mus musculus (P50285), Mus musculus (P97501), Mus musculus (P97872), Mus musculus (Q8K2I3), Mus musculus (Q8VHG0), Mus musculus, Mus musculus C57/BL6J (P50285), Mus musculus C57/BL6J (P97501), Mus musculus C57/BL6J (P97872), Mus musculus C57/BL6J (Q8K2I3), Mus musculus C57/BL6J (Q8VHG0)
Manually annotated by BRENDA team
Celius, T.; Pansoy, A.; Matthews, J.; Okey, A.B.; Henderson, M.C.; Krueger, S.K.; Williams, D.E.
Flavin-containing monooxygenase-3: induction by 3-methylcholanthrene and complex regulation by xenobiotic chemicals in hepatoma cells and mouse liver
Toxicol. Appl. Pharmacol.
247
60-69
2010
Mus musculus (P97501), Mus musculus
Manually annotated by BRENDA team
Motika, M.S.; Zhang, J.; Ralph, E.C.; Dwyer, M.A.; Cashman, J.R.
pH dependence on functional activity of human and mouse flavin-containing monooxygenase 5
Biochem. Pharmacol.
83
962-968
2012
Homo sapiens (P49326), Homo sapiens, Mus musculus (P97872), Mus musculus
Manually annotated by BRENDA team
Tanino, T.; Bando, T.; Komada, A.; Nojiri, Y.; Okada, Y.; Ueda, Y.; Sakurai, E.
Hepatic flavin-containing monooxygenase 3 enzyme suppressed by type 1 allergy-produced nitric oxide
Drug Metab. Dispos.
45
1189-1196
2017
Mus musculus
Manually annotated by BRENDA team
Scott, F.; Gonzalez Malagon, S.G.; OBrien, B.A.; Fennema, D.; Veeravalli, S.; Coveney, C.R.; Phillips, I.R.; Shephard, E.A.
Identification of flavin-containing monooxygenase 5 (FMO5) as a regulator of glucose homeostasis and a potential sensor of gut bacteria
Drug Metab. Dispos.
45
982-989
2017
Mus musculus
Manually annotated by BRENDA team
Phillips, I.R.; Shephard, E.A.
Drug metabolism by flavin-containing monooxygenases of human and mouse
Expert. Opin. Drug Metab. Toxicol.
13
167-181
2017
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Liao, B.M.; McManus, S.A.; Hughes, W.E.; Schmitz-Peiffer, C.
Flavin-containing monooxygenase 3 reduces endoplasmic reticulum stress in lipid-treated hepatocytes
Mol. Endocrinol.
30
417-428
2016
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
El-Serafi, I.; Terelius, Y.; Abedi-Valugerdi, M.; Naughton, S.; Saghafian, M.; Moshfegh, A.; Mattsson, J.; Potacova, Z.; Hassan, M.
Flavin-containing monooxygenase 3 (FMO3) role in busulphan metabolic pathway
PLoS ONE
12
e0187294
2017
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chen, M.; Guan, B.; Xu, H.; Yu, F.; Zhang, T.; Wu, B.
The molecular mechanism regulating diurnal rhythm of flavin-containing monooxygenase 5 in mouse liver
Drug Metab. Dispos.
47
1333-1342
2019
Mus musculus (P97872), Mus musculus, Mus musculus C57BL/6 (P97872)
Manually annotated by BRENDA team
Veeravalli, S.; Phillips, I.R.; Freire, R.T.; Varshavi, D.; Everett, J.R.; Shephard, E.A.
Flavin-containing monooxygenase 1 catalyzes the production of taurine from hypotaurine
Drug Metab. Dispos.
48
378-385
2020
Homo sapiens, Homo sapiens (Q01740), Mus musculus (P50285)
Manually annotated by BRENDA team