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Enzyme Nomenclature
Information on EC 1.14.13.148 - trimethylamine monooxygenase
for references in articles please use BRENDA:EC1.14.13.148
Word Map on EC 1.14.13.148
- 1.14.13.148
- trimethylamine-n-oxide
-
flavin-containing
- choline
-
trimethylaminuria
- roseobacter
- sulindac
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.14.13.148
-
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RECOMMENDED NAME
GeneOntology No.
trimethylamine monooxygenase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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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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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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INHIBITORS
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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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
FMO3 is the major form of flavin-containing monooxygenase expressed in adult human liver
additional information
-
no activity in fetal human liver, intestine, and kidney
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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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SUBUNITS
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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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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ENGINEERING
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.148)
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