| Type: | Family | Name: | Flavin monooxygenase (FMO) 1 |
| 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 diverse compounds. FMOs have been implicated in the metabolism of a number of pharmaceuticals, pesticides and toxicants. In man, lack of hepatic FMO-catalysed trimethylamine metabolism results in trimethylaminuria (fish odour syndrome). Five mammalian forms of FMO are now known and have been designated FMO1-FMO5 [, , , , ].Human FMO1 mRNA is more abundant in foetal than in adult liver, indicating that the enzyme is subject to developmental regulation in man []. The deduced amino sequence contains putative FAD- (GxGxxG) and NADP+-binding (GxGxxA) sites, a 'FATGY' motif that has also been observed in a range of siderphore biosynthetic enzymes [], and a C-terminal hydrophobic segment that is believed to anchor the monooxygenase to the microsomal membrane []. The human sequence shares 88 and 86% identity, respectively, with pig and rabbit 'hepatic' forms of FMO, but is only 58% similar to the abbit 'pulmonary' FMO []. | Short Name: | Flavin_mOase_1 |
| DB identifier | Type | Name |
|---|---|---|
| IPR012143 | Family | Dimethylaniline monooxygenase, N-oxide-forming |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Luann.0082s0193.1.p | PAC:39372984 | Lunaria annua |
390
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