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Literature summary extracted from

  • Zhou, J.; Shephard, E.A.
    Mutation, polymorphism and perspectives for the future of human flavin-containing monooxygenase 3 (2006), Mutat. Res., 612, 165-171.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.8 E158K/E308G naturally occuring polymorphism, in many cases in vivo, altered clinical responses or altered susceptibility to various chemicals due to these sequence variants are observed compared to the carriers of at least one wild-type allele Homo sapiens
1.14.13.8 E158K/V257M the naturally occuring polymorphisms reduce the oxidation and clearance of FMO3 substrates such as tyramine, and TMA in vitro, and mutations are highly likely to eliminate the enzyme function in vivo Homo sapiens
1.14.13.8 additional information identification and analysis of 18 mutations of FMO3 genes from 134 African–Americans and 129 Caucasians from the United States, missense and nonsense nucleotide substitutions, and polymorphic variants of the gene, both involved in development of trimethylaminuria, TMAU, interindividual variability in the expression of FMO3 may affect drug and exogenous chemical metabolism in the liver and other tissues, clinical relevance of the polymorphisms, overview Homo sapiens
1.14.13.8 V257M/E308G naturally occuring polymorphism, the substitutions do not affect enzyme activity in vitro Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.8 microsome
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.8 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2 Homo sapiens
-
 ?
-
 ?
1.14.13.8 methimazole + NADPH + O2 Homo sapiens
-
 ?
-
 ?
1.14.13.8 additional information Homo sapiens FMOs catalyze NADPH-dependent monooxygenation of soft-nucleophilic nitrogen, sulfur, and phosphorous atoms contained within various drugs, pesticides, and xenobiotics, isozyme FMO3 is responsible for the majority of FMO-mediated xenobiotic metabolism in the adult human liver, FMO3 mutations causing defects in trimethylamine N-oxygenation, result in the disorder known as trimethylaminuria, TMAU, or fish-odour syndrome, overview, interindividual variability in the expression of FMO3 affect drug and exogenous chemical metabolism in the liver and other tissues ?
-
 ?
1.14.13.8 trimethylamine + NADPH + O2 Homo sapiens
-
 trimethylamine N-oxide + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Homo sapiens
-
 isozymes FMO1–FMO6
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.8 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2
-
 Homo sapiens ?
-
 ?
1.14.13.8 10-(N,N-dimethylaminopentyl)-2-(trifluoromethyl)phenothiazine + NADPH + O2 isozyme FMO3 Homo sapiens ?
-
 ?
1.14.13.8 methimazole + NADPH + O2
-
 Homo sapiens ?
-
 ?
1.14.13.8 methimazole + NADPH + O2 isozyme FMO3 Homo sapiens ?
-
 ?
1.14.13.8 additional information FMOs catalyze NADPH-dependent monooxygenation of soft-nucleophilic nitrogen, sulfur, and phosphorous atoms contained within various drugs, pesticides, and xenobiotics, isozyme FMO3 is responsible for the majority of FMO-mediated xenobiotic metabolism in the adult human liver, FMO3 mutations causing defects in trimethylamine N-oxygenation, result in the disorder known as trimethylaminuria, TMAU, or fish-odour syndrome, overview, interindividual variability in the expression of FMO3 affect drug and exogenous chemical metabolism in the liver and other tissues Homo sapiens ?
-
 ?
1.14.13.8 trimethylamine + NADPH + O2
-
 Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?
1.14.13.8 trimethylamine + NADPH + O2 isozyme FMO3 Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.8 FMO
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.8 FAD
-
 Homo sapiens
1.14.13.8 NADPH
-
 Homo sapiens