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Information on EC 1.14.13.148 - trimethylamine monooxygenase
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1.14.13.148 trimethylamine monooxygenaseIUBMB Comments
A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
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Word Map
- 1.14.13.148
- trimethylamine-n-oxide
- choline
-
flavin-containing
-
trimethylaminuria
- l-carnitine
- roseobacter
- sulindac
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
EC 1.14.13.8, FAD-containing monooxygenase, flavin containing monooxygenase 3, flavin monooxygenase 3, flavin-containing monooxygenase, flavin-containing monooxygenase 3, FMO, FMO3, FMO4, TMA monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.13.8
flavin-containing monooxygenase
flavin-containing monooxygenase 3
FMO
FMO3
TMA monooxygenase
TMM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming)
A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
10-[(N,N-dimethylaminopentyl)]-2-(trifluoromethylphenothiazine) + NADPH + H+ + O2
?
-
functional substrate
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
methyl 4-tolyl sulfide + NADPH + H+ + O2
methyl 4-tolyl sulfoxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADH + H+ + O2
N,N,N-trimethylamine N-oxide + NAD+ + H2O
-
-
-
-
?
N,N-dimethylaniline + NADPH + H+ + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylbutylamine + NADPH + H+ + O2
N,N-dimethylbutylamine N-oxide + NADP+ + H2O
-
-
-
-
?
additional information
?
-
-
no activity with N-monomethylamine, glutathione, and cysteine
-
-
-
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
i.e. 5-dimethylaminopropylamino-8-hydroxytriazoloacridinone
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
i.e. 5-dimethylaminopropylamino-8-hydroxytriazoloacridinone
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
-
-
?
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADPH + H+ + O2
5-{[3-(dimethylnitroryl)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
-
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
highest affinity substrate
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylamine + NADPH + H+ + O2
N,N-dimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
N,N-dimethylamine + NADPH + H+ + O2
N,N-dimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
the enzyme does not display saturability at concentrations through 1 mM of sulindac sulfide
-
-
?
sulindac sulfide + NADPH + H+ + O2
sulindac + NADP+ + H2O
-
the enzyme does not display saturability at concentrations through 1 mM of sulindac sulfide
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N,N-trimethylamine + NADPH + H+ + O2
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
-
NADPH
-
dependent on, in the absence of NADPH the enzyme is rapidly and irreversibly inactivated at 0-5°C. NADP+ also stabilizes the enzyme, but to a lesser extent than NADPH. No oxidation of N,N,N-trimethylamine is observed when NADH is used in the enzyme assay instead of NADPH
NADPH
-
required for activity, in the absence of NADP or NADPH, the FAD-containing monooxygenase is irreversibly inactivated at 37°C during 30 min
NADPH
-
required for activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-dimethylaminopropan-1-ol
-
inhibitory at concentrations above about 1 mM
3-dimethylaminopropan-2-ol
-
inhibitory at concentrations above about 1 mM
Cu2+
-
0.2 mM Cu2+ inhibits the enzyme strongly without any preincubation
N,N-dimethyl-2-chloroethylamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylethanolamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylethylenediamine
-
inhibitory at concentrations above about 1 mM
N,N-dimethylpropylenediamine
-
inhibitory at concentrations above about 1 mM
N-ethylmaleimide
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 1.0 mM N-ethylmaleimide inhibits the enzymatic activity approximately by 25%
p-chloromercuribenzoate
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 0.2 mM p-chloromercuribenzoate inhibits the enzymic activity approximately by 90%
Thiourea
thiourea reduces ethionamide oxygenation to ethionamide S-oxide by an average of 73.5% in liver and 76.9% in lung
additional information
-
the enzyme is not inhibited by CO, cyanide or SKF 525-A (2-diethylaminoethyl 2,2-diphenylvalerate hydrochloride), nor by chelating agents
-
additional information
-
10 mM EDTA, 1 mM potassium cyanide and 1 mM sodium azide do not inhibit the enzyme. Bubbling the enzyme solution with CO for 2 min at 0°C or including CO (CO:O2 ratio 1:1) during the tests has no effect on enzyme activity
-
additional information
-
enzyme reactions are not inhibited by gas phase containing up to 80% carbon monoxide/20% oxygen mixture
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chlorpromazine
-
the activity of the native enzyme is increased at 0.001-0.2 mM of chlorpromazine. Greatest activation is 85% when methimazole and chlorpromazine concentrations are 2 mM and 0.1 mM, respectively
imipramine
-
the activity of the native enzyme is increased at 0.05-0.75 mM of imipramine
O2
-
when the oxygen in the enzyme assay mixture is replaced with 100% nitrogen, there is no formation of N,N,N-trimethylamine N-oxide, showing that the enzyme is oxygen-dependent
additional information
n-octylamine has no effect on isoform FMO3
-
additional information
n-octylamine has no effect on isoform FMO3
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenoma
Genetic polymorphisms of flavin monooxygenase 3 in sulindac-induced regression of colorectal adenomas in familial adenomatous polyposis.
Adenomatous Polyposis Coli
Genetic polymorphisms of flavin monooxygenase 3 in sulindac-induced regression of colorectal adenomas in familial adenomatous polyposis.
Adenomatous Polyposis Coli
Genetic polymorphisms of human flavin monooxygenase 3 in sulindac-mediated primary chemoprevention of familial adenomatous polyposis.
Atherosclerosis
Emerging roles of flavin monooxygenase 3 in cholesterol metabolism and atherosclerosis.
Atherosclerosis
Trimethylamine-N-oxide: a link between the gut microbiome, bile acid metabolism, and atherosclerosis.
Diabetes Mellitus, Type 2
Association between microbiota-dependent metabolite trimethylamine-N-oxide and type 2 diabetes.
Infections
Selective Modulation of Hepatic Cytochrome P450 and Flavin Monooxygenase 3 Expression during Citrobacter rodentium Infection in Severe Combined Immune-Deficient Mice.
Thrombosis
Flavin monooxygenase 3, the host hepatic enzyme in the metaorganismal trimethylamine N-oxide-generating pathway, modulates platelet responsiveness and thrombosis risk.
trimethylamine monooxygenase deficiency
Biochemical and molecular studies in mild flavin monooxygenase 3 deficiency.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1116
5-{[3-(dimethylamino)propyl]amino}-8-hydroxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO3, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
0.1624
5-{[3-(dimethylamino)propyl]amino}-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
isozyme FMO3, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C
3.139
cysteamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0357
dimethylaniline
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0103
Dimethylsulfide
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
3.575
DMSO
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0897
N,N-dimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.045
Benzydamine
-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.056
Benzydamine
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0282
Methimazole
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.03
Methimazole
isoform FMO3, at pH 8.4, temperature not specified in the publication
0.033
Methimazole
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.035
Methimazole
-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0003
N,N,N-trimethylamine
-
in potassium diphosphate buffer (pH 7.7), at 14°C
0.0094
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.013 - 0.0548
N,N,N-trimethylamine
-
the Km for isoform FMO3 determined in human liver microsomes ranges from 0.013.to 0.0548 mM, at pH 7.4 and 22°C
0.0208
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0216
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0275
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.0285
N,N,N-trimethylamine
-
recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C
0.022
sulindac sulfide
-
truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.025
sulindac sulfide
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00047
-
supernatant of homogenate, in potassium diphosphate buffer (pH 7.7), at 14°C
0.025
isoform FMO3, using 1 mM methimazole as substrate, at pH 8.4, temperature not specified in the publication
0.049
-
crude enzyme from membranes, using methyl 4-tolyl sulfide as substrate, in 25 mM potassium diphosphate (pH 8.5), at 37°C
0.085
-
after 180fold purification, in potassium diphosphate buffer (pH 7.7), at 14°C
0.201
-
after purification, using methyl 4-tolyl sulfide as substrate, in 25 mM potassium diphosphate (pH 8.5), at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 8.4
7.4 - 8.4
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform FMO4 is most prominent in the kidney
brenda
additional information
-
FMO3 is the major form of flavin-containing monooxygenase expressed in adult human liver
brenda
additional information
-
no activity in fetal human liver, intestine, and kidney
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
-
isozyme FMO3 regulates the conversion of N,N,N-trimethylamine into its N-oxide and hence controls the release of volatile N,N,N-trimethylamine from the individual
malfunction
-
trimethylaminuria (fish-odor syndrome) is associated with defective hepatic N-oxidation of dietary-derived trimethylamine catalyzed by flavin-containing monooxygenase
malfunction
-
mutations of the flavin-containing monooxygenase gene FMO3 cause trimethylaminuria
malfunction
-
FMO3 deficiency results in trimethylaminuria or the fish-like odour syndrome
metabolism
-
isoform FMO3 in human liver may contribute to the toxicity and/or affect efficacy of ethionamide administration
metabolism
the flavin monooxygenase FMO3 contributes to metabolism of anti-tumour triazoloacridinone, C-1305 (5-dimethylaminopropylamino-8-hydroxytriazoloacridinone), in liver microsomes and Hep-G2 cells
metabolism
-
the flavin monooxygenase FMO3 contributes to metabolism of anti-tumour triazoloacridinone, C-1305 (5-dimethylaminopropylamino-8-hydroxytriazoloacridinone), in liver microsomes
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
59815
59815, isofom FMO3, calculated from amino acid sequence
62992
x * 62992, isoform FMO4, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
59815, isofom FMO3, calculated from amino acid sequence; x * 62992, isoform FMO4, calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
N-linked glycosylation at Asn61 and O-linked glycosylation at Thr29, Thr249, and Thr381. Posttranslational modification of human FMO3 by insect cells is limited to cleavage at the N-terminal methionine
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E158K
E24D
-
the mutation impacts the structure of the Rossmann fold involved in FAD binding and does not alter FMO3 catalytic activity
E308G
K416N
-
the mutation has minimal impact on either hydrophilicity or protein structure
N61K
-
the mutation disrupts the secondary structure of a conserved membrane interaction domain and does not alter FMO3 catalytic activity
T428R
-
methimazole activity of the mutant enzyme is stimulated (maximally 25% when the methimazole concentration is 2 mM) to the same extend of native enzyme up to an imipramine concentration of 3 mM. The activity of the mutant is inhibited at concentrations above 0.3 mM imipramine, 0.75 mM imipramine causes 93% inhibition of methimazole activity of the mutant enzyme. Chlorpromazine activates the mutant enzyme only at high substrate concentrations (0.1-2 mM)
V257M
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
the enzyme is stable at 0°C for 30min at any pH value in the range 4.0-9.0
717207
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 20
-
the enzyme is stable for 30 min at temperatures between 0 and 20°C, when the enzyme is preincubated for 30 min at temperatures above 20°C, a decrease in enzymic activity ensues
35
-
the enzyme has a half-life in the crude extract of 20 min at 35°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of FAD and dithiothreitol together with NADPH improves the stability of the enzyme
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sephadex G-200 gel filtration, DEAE-cellulose column chromatography, and calcium phosphate chromatography
-
cholate solubilization and sequential column chromatography on octyl-Sepharose, DEAE-Sepharose, and hydroxyapatite
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BLR(DE3) pLysS cells
expressed in Saccharomyces cerevisiae strain 334 and in Escherichia coli JM109 cells; expressed in Saccharomyces cerevisiae strain 334 and in Escherichia coli JM109 cells
expressed in Sf9 insect cells
expressed in Spodoptera frugiperda insect cells using a baculovirus expression system
-
expressed in Trichoplusia ni cells using a baculovirus expression vector system
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5-aza-2'-deoxycytidine at 0.001 mM and 0.0025 mM results in 6.6fold and 9.2fold increases in FMO3 mRNA levels, respectively. HNF4alpha transient expression results in a 3.1fold increase in FMO3 mRNA levels. Co-transfection of HepG2 cells with the CCAAT/enhancer-binding protein beta expression vector and the pRNH694 reporter construct results in a dose-dependent increase in FMO3 promoter activity with a maximal 2fold increase using 0.001 mg of expression
-
no changes in relative FMO3 mRNA levels are observed with 50 nM trichostatin A
-
the enzyme is highly expressed in N,N,N-trimethylamine-grown Methylocella silvestris
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adali, O.; Carver, G.C.; Philpot, R.M.
The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine
Exp. Toxicol. Pathol.
51
271-276
1999
Homo sapiens
brenda
Klick, D.E.; Shadley, J.D.; Hines, R.N.
Differential regulation of human hepatic flavin containing monooxygenase 3 (FMO3) by CCAAT/enhancer-binding protein beta (C/EBPbeta) liver inhibitory and liver activating proteins
Biochem. Pharmacol.
76
268-278
2008
Homo sapiens
brenda
Lickteig, A.J.; Riley, R.; Melton, R.J.; Reitz, B.A.; Fischer, H.D.; Stevens, J.C.
Expression and characterization of functional dog flavin-containing monooxygenase 3
Drug Metab. Dispos.
37
1987-1990
2009
Canis lupus familiaris, Homo sapiens
brenda
Henderson, M.C.; Siddens, L.K.; Morre, J.T.; Krueger, S.K.; Williams, D.E.
Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes
Toxicol. Appl. Pharmacol.
233
420-427
2008
Homo sapiens (P31513), Mus musculus (P97501)
brenda
Large, P.; Boulton, C.; Crabbe, M.
The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans
Biochem. J.
128
137P-138P
1972
Aminobacter aminovorans
brenda
Lang, D.H.; Yeung, C.K.; Peter, R.M.; Ibarra, C.; Gasser, R.; Itagaki, K.; Philpot, R.M.; Rettie, A.E.
Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes: selective catalysis by FMO3
Biochem. Pharmacol.
56
1005-1012
1998
Homo sapiens
brenda
Catucci, G.; Gilardi, G.; Jeuken, L.; Sadeghi, S.
In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3
Biochem. Pharmacol.
83
551-558
2012
Homo sapiens
brenda
Strøm, A.
Biosynthesis of trimethylamine oxide in Calanus finmarchicus. Properties of a soluble trimethylamine monooxygenase
Comp. Biochem. Physiol. B
65
243-249
1980
Calanus finmarchicus
-
brenda
Haining, R.; Hunter, A.; Sadeque, A.; Philpot, R.; Rettie, A.
Baculovirus-mediated expression and purification of human FMO3: Catalytic, immunochemical, and structural characterization
Drug Metab. Dispos.
25
790-797
1997
Homo sapiens
brenda
Gut, I.; Conney, A.H.
The FAD-containing monooxygenase-catalyzed N-oxidation and demethylation of trimethylamine in rat liver microsomes
Drug Metabol. Drug Interact.
9
201-208
1991
Rattus norvegicus
brenda
Dolphin, C.; Riley, J.; Smith L, R.; Shephard, E.; Phillips, I.
Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA
Genomics
46
260-267
1997
Homo sapiens (P31513)
brenda
Treacy, E.; Akerman, B.; Chow, L.; Youil, R.; Bibeau, C.; Lin, J.; Bruce, A.; Knight, M.; Danks, D.; Cashman, J.; Forrest, S.
Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication
Hum. Mol. Genet.
7
839-845
1998
Homo sapiens
brenda
Burnettt, V.; Lawton, M.; Philpot, R.
Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3
J. Biol. Chem.
269
14314-14322
1994
Oryctolagus cuniculus (P32417), Oryctolagus cuniculus (P36367)
brenda
Koukouritaki, S.; Poch, M.; Cabacungan, E.; McCarver, D.; Hines, R.
Discovery of novel flavin-containing monooxygenase 3 (FMO3) single nucleotide polymorphisms and functional analysis of upstream haplotype variants
Mol. Pharmacol.
68
383-392
2005
Homo sapiens (P31513)
brenda
Chen, Y.; Patel, N.A.; Crombie, A.; Scrivens, J.H.; Murrell, J.C.
Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase
Proc. Natl. Acad. Sci. USA
108
17791-17796
2011
Candidatus Pelagibacter ubique, Candidatus Pelagibacter ubique HTCC1002, Candidatus Pelagibacter ubique HTCC7211, Methylocella silvestris, no activity in Dinoroseobacter shibae, no activity in Oceanicola batsensis, no activity in Roseobacter sp., no activity in Roseobacter sp. SK209-2-6, no activity in Sagittula stellata, Roseovarius sp. 217, Roseovarius sp., Ruegeria pomeroyi
brenda
Mitchell, S.; Smith, R.
A physiological role for flavin-containing monooxygenase (FMO3) in humans
Xenobiotica
40
301-305
2010
Homo sapiens
brenda
Fedejko-Kap, B.; Niemira, M.; Radominska-Pandya, A.; Mazerska, Z.
Flavin monooxygenases, FMO1 and FMO3, not cytochrome P450 isoenzymes, contribute to metabolism of anti-tumour triazoloacridinone, C-1305, in liver microsomes and HepG2 cells
Xenobiotica
41
1044-1055
2011
Homo sapiens (P31513), Rattus norvegicus
brenda
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