| Primary Identifier | IPR002256 | Type | Family |
| Short Name | Flavin_mOase_4 |
| 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 designatedFMO1-FMO5 [, , , , ].FMO4 mRNA is present in low abundance in several foetal and adult tissuesand the corresponding gene thus appears to be expressed constitutively [].Sequence analysis reveals that FMO4 is 56% identical to FMO3; each isencoded by a single gene []. The deduced amino acid sequence of human FM04 includes the putative FAD- (GxGxxG) and NADP+pyrophosphate-binding (GxGxxA)sites characteristic of mammalian FMOs, a 'FATGY' motif that has also beenobserved in a range of siderphore biosynthetic enzymes [], and a C-terminalhydrophobic segment that is believed to anchor the monooxygenase to themicrosomal membrane []. |
