1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR012143 | Family | Dimethylaniline monooxygenase, N-oxide-forming |
| Type: | Family | Name: | Flavin monooxygenase (FMO) 3 |
| Description: | Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic- metabolising enzymes []. Using an NADPH cofactor and FAD prosthetic group,these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorous and selenium atoms in a range of structurally diversecompounds. Five mammalian forms of FMO are now known and have been designated FMO1-FMO5 [, , , , ].The mRNA encoding FMO3 is abundant in adult liver and is also present, in low abundance, in some foetal tissues. Thus, like FMO1, FMO3 is subjectto developmental and tissue-specific regulation, with a developmental switch in the expression of the genes taking place in the liver []. The deduced amino acid sequence of human FM03 includes the putative FAD- (GxGxxG) and NADP+pyrophosphate-binding (GxGxxA) sites characteristic of mammalian FMOs [], a 'FATGY' motif that has also been observed in a rangeof siderphore biosynthetic enzymes [], and a C-terminal hydrophobic segment that is believed to anchor the monooxygenase to the microsomal membrane [].Mutations in human FMO3 impair N-oxygenation of xenobiotics and are responsible for the trimethylaminuria phenotype []. Three disease-causingmutations have been identified. Nonsense and missense mutations are associated with a severe phenotype and are also implicated in impairedmetabolism of other nitrogen- and sulphur-containing substrates, including biogenic amines, both clinically and when mutated proteins expressed fromcDNA are studied in vitro []. Human FMO3 thus plays a critical role in themetabolism of xenobiotic substrates and endogenous amines. | Short Name: | Flavin_mOase_3 |
| DB identifier | Type | Name |
|---|---|---|
| IPR012143 | Family | Dimethylaniline monooxygenase, N-oxide-forming |
