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Literature summary extracted from

  • Yeung, C.K.; Adman, E.T.; Rettie, A.E.
    Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria (2007), Arch. Biochem. Biophys., 464, 251-259.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.8 expression of wild-type enzyme and mutants M66I and R492W in Spodoptera frugiperda Sf9 cell membranes Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.8 E158K naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
1.14.13.8 E158K/E308G naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
1.14.13.8 E308G naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
1.14.13.8 M66I naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor Homo sapiens
1.14.13.8 N61S naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme Homo sapiens
1.14.13.8 P153L naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme Homo sapiens
1.14.13.8 R492W naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor Homo sapiens
1.14.13.8 V257M naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.8 membrane
-
 Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.8 trimethylamine + NADPH + H+ + O2 Homo sapiens mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview trimethylamine N-oxide + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 trimethylamine + NADPH + H+ + O2
-
 Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?
1.14.13.8 trimethylamine + NADPH + H+ + O2 mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.8 More structure homology model for FMO3 based on the crystal structure for yeast FMO with N61 in close proximity to the FAD catalytic center, in contrast to residues M66, P153, R492, E158, V257, and E308, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.14.13.8 FMO3
-
 Homo sapiens

Cofactor

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