BRENDA - Enzyme Database show
show all sequences of 1.14.13.148

A physiological role for flavin-containing monooxygenase (FMO3) in humans

Mitchell, S.; Smith, R.; Xenobiotica 40, 301-305 (2010)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Homo sapiens
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N,N,N-trimethylamine + NADPH + H+ + O2
Homo sapiens
-
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N,N,N-trimethylamine + NADPH + H+ + O2
-
718454
Homo sapiens
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Homo sapiens
NADPH
required for activity
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Homo sapiens
NADPH
required for activity
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Homo sapiens
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N,N,N-trimethylamine + NADPH + H+ + O2
Homo sapiens
-
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N,N,N-trimethylamine + NADPH + H+ + O2
-
718454
Homo sapiens
N,N,N-trimethylamine N-oxide + NADP+ + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
FMO3 deficiency results in trimethylaminuria or the fish-like odour syndrome
Homo sapiens
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
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
FMO3 deficiency results in trimethylaminuria or the fish-like odour syndrome
Homo sapiens
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
Homo sapiens
Other publictions for EC 1.14.13.148
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
717229
Catucci
In vitro drug metabolism by C- ...
Homo sapiens
Biochem. Pharmacol.
83
551-558
2012
-
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1
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6
1
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1
1
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1
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6
1
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718325
Chen
Bacterial flavin-containing mo ...
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
Proc. Natl. Acad. Sci. USA
108
17791-17796
2011
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4
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11
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22
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14
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8
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8
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11
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14
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2
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2
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718455
Fedejko-Kap
Flavin monooxygenases, FMO1 an ...
Homo sapiens, Rattus norvegicus
Xenobiotica
41
1044-1055
2011
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-
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-
-
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2
2
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2
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3
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4
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2
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4
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2
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3
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4
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2
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2
2
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718454
Mitchell
A physiological role for flavi ...
Homo sapiens
Xenobiotica
40
301-305
2010
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1
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1
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1
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1
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2
2
-
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703411
Lickteig
Expression and characterizatio ...
Canis lupus familiaris, Homo sapiens
Drug Metab. Dispos.
37
1987-1990
2009
-
-
1
-
-
-
-
3
1
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2
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2
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2
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4
2
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4
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1
4
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1
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4
2
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685038
Klick
Differential regulation of hum ...
Homo sapiens
Biochem. Pharmacol.
76
268-278
2008
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2
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2
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706824
Henderson
Metabolism of the anti-tubercu ...
Homo sapiens, Mus musculus
Toxicol. Appl. Pharmacol.
233
420-427
2008
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2
-
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2
2
2
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2
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3
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2
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4
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2
4
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2
2
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3
-
-
2
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2
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1
1
-
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-
718139
Koukouritaki
Discovery of novel flavin-cont ...
Homo sapiens
Mol. Pharmacol.
68
383-392
2005
-
-
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6
-
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1
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1
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2
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2
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6
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1
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348510
Adali
The effect of arginine-428 mut ...
Homo sapiens
Exp. Toxicol. Pathol.
51
271-276
1999
2
-
1
-
1
-
-
2
-
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2
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2
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1
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2
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2
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1
2
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1
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2
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1
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717226
Lang
Isoform specificity of trimeth ...
Homo sapiens
Biochem. Pharmacol.
56
1005-1012
1998
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1
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2
1
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3
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2
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1
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2
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1
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717652
Treacy
Mutations of the flavin-contai ...
Homo sapiens
Hum. Mol. Genet.
7
839-845
1998
-
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9
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1
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3
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2
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2
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9
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3
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1
1
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717530
Haining
Baculovirus-mediated expressio ...
Homo sapiens
Drug Metab. Dispos.
25
790-797
1997
-
-
1
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-
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1
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1
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1
1
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1
2
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1
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2
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1
2
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1
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2
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1
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717640
Dolphin
Structural organization of the ...
Homo sapiens
Genomics
46
260-267
1997
-
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1
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1
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1
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1
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2
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1
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1
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1
1
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717752
Burnettt
Cloning and sequencing of flav ...
Oryctolagus cuniculus
J. Biol. Chem.
269
14314-14322
1994
1
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1
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1
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2
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4
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1
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2
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717533
Gut
The FAD-containing monooxygena ...
Rattus norvegicus
Drug Metabol. Drug Interact.
9
201-208
1991
-
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1
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1
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717521
Strøm
-
Biosynthesis of trimethylamine ...
Calanus finmarchicus
Comp. Biochem. Physiol. B
65
243-249
1980
1
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1
4
2
1
1
1
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1
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4
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1
1
1
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1
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4
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1
1
1
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1
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2
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4
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1
1
1
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1
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717207
Large
The reduced nicotinamide-adeni ...
Aminobacter aminovorans
Biochem. J.
128
137P-138P
1972
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13
2
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1
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11
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1
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13
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2
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11
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