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Information on EC 1.14.13.8 - flavin-containing monooxygenase and Organism(s) Rattus norvegicus and UniProt Accession Q9EQ76

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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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Select one or more organisms in this record:
This record set is specific for:
Rattus norvegicus
UNIPROT: Q9EQ76
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Rattus norvegicus
Synonyms
class 3 flavin-containing mono-oxygenase, class 3 FMO, dechlorinating flavin-dependent monooxygenase, dimethylaniline monooxygenase (N-oxide-forming), dimethylaniline N-oxidase, dimethylaniline oxidase, dimethylsulfone monooxygenase, DMA oxidase, EtaA, FAD-containing monooxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethylaniline monooxygenase (N-oxide-forming)
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dimethylaniline N-oxidase
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dimethylaniline oxidase
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DMA oxidase
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FAD-containing monooxygenase
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flavin mono-oxygenase
248
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flavin monooxygenase
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flavin-containing monooxygenase
FMO 1A1
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FMO 1B1
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FMO 1C1
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FMO 1D1
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FMO 1E1
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FMO-I
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FMO-II
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Met S-oxidase
289783
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mixed-function amine oxidase
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N,N-dimethylaniline monooxygenase
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oxygenase, dimethylaniline mono- (N-oxide-forming)
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oxygenase, methylphenyltetrahydropyridine N-mono-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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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
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148848-55-9
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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
L-methionine + NADPH + H+ + O2
methionine S-oxide + NADP+ + H2O
show the reaction diagram
stereochemistry, overview
formation of 80% D-isomer
-
?
methimazole + NADPH + H+ + O2
methimazole S-oxide + NADP+ + H2O
show the reaction diagram
i.e. N-methyl-2-mercaptoimidazole
-
-
?
S-allyl-L-cysteine + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
stereochemmistry, overview
-
-
?
seleno-L-methionine + NADPH + H+ + O2
seleno-L-methionine Se-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
show the reaction diagram
1,2,3,4-tetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
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-
-
-
?
1,2-dimethylhydrazine + NADPH + O2
?
show the reaction diagram
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-
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-
?
1,2-dimethylphenylhydrazine + NADPH + O2
?
show the reaction diagram
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-
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-
?
1-butanethiol + NADPH + O2
?
show the reaction diagram
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-
-
-
?
1-methyl-1-phenylhydrazine + NADPH + O2
?
show the reaction diagram
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-
-
-
?
1-methyl-2-benzylhydrazine + NADPH + O2
?
show the reaction diagram
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-
-
-
?
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 + O2
?
show the reaction diagram
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-
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-
?
2-mercaptobenzimidazole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
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
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i.e. C-1305
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-
?
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
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i.e. C-1299
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-
?
alpha-naphthylthiourea + NADPH + O2
?
show the reaction diagram
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-
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?
aminopyrine + NADPH + O2
?
show the reaction diagram
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-
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-
?
benzydamine + NADPH + H+ + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
-
-
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-
?
benzydamine + NADPH + O2
benzydamine N-oxide + NADP+ + H2O
show the reaction diagram
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?
benzylhydrazine + NADPH + O2
?
show the reaction diagram
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?
beta-ethylphenylhydrazine + NADPH + O2
?
show the reaction diagram
-
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-
?
butylhydrazine + NADPH + O2
?
show the reaction diagram
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?
cysteamine + NADPH + O2
?
show the reaction diagram
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?
dibenzylamine + NADPH + O2
?
show the reaction diagram
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?
ephedrine + NADPH + O2
?
show the reaction diagram
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?
ethylene sulfide + NADPH + O2
?
show the reaction diagram
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?
imipramine + NADPH + O2
?
show the reaction diagram
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?
isopropylhydrazine + NADPH + O2
?
show the reaction diagram
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?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
L-seleno-methionine + NADPH + O2
L-methionine seleno-oxide + NADP+ + H2O
show the reaction diagram
-
purified liver isozymes FMO1 and FMO3
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?
methamphetamine + NADPH + O2
?
show the reaction diagram
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?
methimazole + NADPH + O2
N-methylmethimidazole-2-sulfinic acid + NADP+ + H2O
show the reaction diagram
methylphenylsulfide + NADPH + O2
?
show the reaction diagram
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?
N,N-dimethylaniline + NADPH + O2
N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
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?
N-aminohomopiperidine + NADPH + O2
?
show the reaction diagram
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?
N-aminomorpholine + NADPH + O2
?
show the reaction diagram
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?
N-aminopiperidine + NADPH + O2
?
show the reaction diagram
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?
N-aminopiperidine + NADPH + O2
tetrazene + NADP+ + H2O + ?
show the reaction diagram
N-aminopyrrolidone + NADPH + O2
?
show the reaction diagram
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?
N-methyl-1,2,3,4-tetrahydroisoquinoline + NADPH + O2
?
show the reaction diagram
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?
p-chloro-N-methylaniline + NADPH + O2
?
show the reaction diagram
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?
phenylhydrazine + NADPH + O2
?
show the reaction diagram
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?
phenylthiourea + NADPH + O2
?
show the reaction diagram
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?
procarbazine + NADPH + O2
?
show the reaction diagram
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?
S-benzyl-L-cysteine + NADPH + O2
S-benzyl-L-cysteine S-oxide + NADP+ + H2O
show the reaction diagram
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isozyme FMO1
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?
selegiline + NADPH + O2
selegiline N-oxide + NADP+
show the reaction diagram
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?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
thioacetamide + NADPH + O2
?
show the reaction diagram
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?
thiobenzamide + NADPH + O2
?
show the reaction diagram
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?
thiourea + NADPH + O2
?
show the reaction diagram
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?
trimethylamine + NADPH + O2
?
show the reaction diagram
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?
additional information
?
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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
1,1-dimethylhydrazine + NADPH + O2
formaldehyde + CH3N2H3 + NADP+
show the reaction diagram
-
possibly, and other 1,1-disubstituted hydrazines
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?
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
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?
L-methionine + NADPH + O2
L-methionine S-oxide + NADP+ + H2O
show the reaction diagram
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-
-
-
?
selegiline + NADPH + O2
selegiline N-oxide + NADP+
show the reaction diagram
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-
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?
tamoxifen + NADPH + O2
tamoxifen N-oxide + NADP+ + H2O
show the reaction diagram
-
tamoxifen N-oxygenation represents a detoxication pathway
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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consensus binding sequence is Gly-Xaa-Gly-Xaa-Xaa-Gly
NADPH
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consensus binding sequence is Gly-Leu-Gly-Asn-Ser-Gly
flavin
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flavoprotein
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-aminobenzotriazole
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about 20% inhibition at 2 mM
alpha-naphthylthiourea
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0.5 mM, 59.2% inhibition
dimethyl sulfoxide
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about 50% inhibition at 0.5 % (v/v)
Methimazole
thiobenzamide
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0.5 mM, 68% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
n-octylamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 3.4
L-methionine
0.01 - 0.04
Methimazole
4.3 - 5.9
S-allyl-L-cysteine
0.31 - 0.35
seleno-L-methionine
0.059
1,2,3,4-tetrahydroisoquinoline
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-
0.0018 - 0.006
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
1.2
cysteamine
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0.008
N-methyl-1,2,3,4-tetrahydroisoquinoline
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0.0713 - 0.1775
selegiline
0.027
Thiourea
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-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.15
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purified enzyme, substrate L-methionine
additional information
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
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assay at
7.4
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.4
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the activity is approximately twice as high at pH 8.4 as at pH 7.4
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male sprague-dawley rats
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
differential expression of isozymes in tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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FMO3 plays an important role in kidney metabolism of xenobiotics containing sulfur and selenium atoms
metabolism
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
FMO3_RAT
531
0
59960
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
x * 56000, kidney enzyme, SDS-PAGE
56000
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SDS-PAGE
60000
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Western blot, anti-rat liver FMO antisera
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 56000, kidney enzyme, SDS-PAGE
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
native FMO3 130fold from kidney microsomes
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
FMO isozyme expression patterns, expression analysis
expression in yeast cells
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FMO isozyme expression patterns, expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bacterial lipopolysaccharides lead to enzyme downregulation in the liver, as well as posttranslationally S-nitrosylation by nitric oxide
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liver FMO1 is upregulated in diabetic rats
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prough, R.A.; Freeman, P.C.; Hines, R.N.
The oxidation of hydrazine derivatives catalyzed by the purified liver microsomal FAD-containing monooxygenase
J. Biol. Chem.
256
4178-4184
1981
Mesocricetus auratus, Rattus norvegicus, Sus scrofa
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
Mus musculus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kawaji, A.; Miki, T.; Takabatake, E.
Partial purification and substrate specificity of flavin-containing monooxygenase from rat brain microsomes
Biol. Pharm. Bull.
18
1657-1659
1995
Rattus norvegicus
Manually annotated by BRENDA team
Lattard, V.; Buronfosse, T.; Lachuer, J.; Longin-Sauvageon, C.; Moulin, C.; Benoit, E.
Cloning, sequencing, tissue distribution, and heterologous expression of rat flavin-containing monooxygenase 3
Arch. Biochem. Biophys.
391
30-40
2001
Rattus norvegicus
Manually annotated by BRENDA team
Chiba, K.; Kobayashi, K.; Itoh, K.; Itoh, S.; Chiba, T.; Ishizaki, T.; Kamataki, T.
N-oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells
Eur. J. Pharmacol.
293
97-100
1995
Rattus norvegicus
Manually annotated by BRENDA team
Tsutsumi, H.; Katagi, M.; Nishikawa, M.; Tsuchihashi, H.; Kasuya, F.; Igarashi, K.
In vitro confirmation of selegiline N-oxidation by flavin-containing monooxygenase in rat microsome using LC-ESI MS
Biol. Pharm. Bull.
27
1572-1575
2004
Rattus norvegicus
Manually annotated by BRENDA team
Elfarra, A.A.; Krause, R.J.
Potential roles of flavin-containing monooxygenases in sulfoxidation reactions of L-methionine, N-acetyl-L-methionine and peptides containing L-methionine
Biochim. Biophys. Acta
1703
183-189
2005
Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
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
Borbas, T.; Benko, B.; Dalmadi, B.; Szabo, I.; Tihanyi, K.
Insulin in flavin-containing monooxygenase regulation. Flavin-containing monooxygenase and cytochrome P450 activities in experimental diabetes
Eur. J. Pharm. Sci.
28
51-58
2006
Rattus norvegicus
Manually annotated by BRENDA team
Mitchell, S.
Flavin mono-oxygenase (FMO) - The other oxidase
Curr. Drug Metab.
9
280-284
2008
Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Novick, R.M.; Elfarra, A.A.
Purification and characterization of flavin-containing monooxygenase isoform 3 from rat kidney microsomes
Drug Metab. Dispos.
36
2468-2474
2008
Rattus norvegicus (Q9EQ76)
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
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, Homo sapiens (Q01740), Homo sapiens (Q9HA79), Rattus norvegicus
Manually annotated by BRENDA team
Taniguchi-Takizawa, T.; Shimizu, M.; Kume, T.; Yamazaki, H.
Benzydamine N-oxygenation as an index for flavin-containing monooxygenase activity and benzydamine N-demethylation by cytochrome P450 enzymes in liver microsomes from rats, dogs, monkeys, and humans
Drug Metab. Pharmacokinet.
30
64-69
2015
Canis lupus familiaris, Homo sapiens, Macaca fascicularis, Rattus norvegicus
Manually annotated by BRENDA team
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