EC Number   |
General Information |
Reference |
|---|
   1.14.13.8 | malfunction |
a sidechain at position Gly74 can have interactions with the substrate. Despite being a pre-Pro residue, the phi-psi angles (-130,175°) will also fit non-Glycine residues. Mutation of Cys78 can fill up a cavity in the active site making binding of indole more productive. Tyr207 and Asp317 form part of the entrance to the substrate binding cavity while residues Trp319, Phe397, and Trp400 limit the size of the substrate binding cavity |
764904 |
| 1.14.13.8 | malfunction |
enzyme-deficient mice are resistant to age-related changes in glucose homeostasis and maintain the higher glucose tolerance and insulin sensitivity characteristic of young animals |
742355 |
| 1.14.13.8 | malfunction |
FMO1 malfunction causes taurine deficiency, which is implicated in a number of pathologic conditions, including cardiomyopathy, muscular abnormalities, and renal dysfunction |
764558 |
| 1.14.13.8 | malfunction |
genetic mutations in FMO3 can cause trimethylaminuria (or fish-odor syndrome) as a result of impaired N-oxygenation of food-derived trimethylamine |
764561, 764562 |
| 1.14.13.8 | malfunction |
mutations in isoform FMO3 are causative of the disorder trimethylaminuria |
742335 |
| 1.14.13.8 | malfunction |
naturally occurring polymorphic enzyme variants demonstrate differences in rates of turnover of its substrates: xenobiotics including drugs as well as dietary compound |
764033 |
| 1.14.13.8 | malfunction |
the hFMO3 gene contains many naturally occuring single SNPs and these mutations can severely affect the activity of the enzyme resulting in lower or abolished activity |
764944 |
| 1.14.13.8 | metabolism |
flavin-containing monooxygenase (FMO) 3 is a member of a family of NADPH-dependent enzymes that oxygenate a range of highly polarizable soft nucleophilic heteroatom-containing substances. Human liver FMO3 potentially forms a complementary enzyme system to the NADPH-dependent cytochrome P450 enzymes (P450s, EC 1.14.14.1) responsible for drug metabolism |
764562 |
| 1.14.13.8 | metabolism |
FMOs are involved in Phase I metabolism catalyzing the NADPH-dependent oxygenation of drugs, xenobiotics and endogenous compounds containing a soft nucleophilic heteroatom, typically nitrogen or sulfur, but in some cases also selenium or phosphorous |
703435 |
| 1.14.13.8 | metabolism |
isoform FMO3 contribute a major part in busulphan metabolic pathway |
743624 |
