Back Monoossigenasi contenente flavina Italian フラビン含有モノオキシゲナーゼ Japanese Dimetilanilin monooksigenaza (formiranje N-oksida) Serbo-Croatian Dimetilanilin monooksigenaza (formiranje N-oksida) Serbian
| Flavin-containing monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Ribbon diagram of yeast FMO (PDB: 1VQW). | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.13.8 | ||||||||
| CAS no. | 37256-73-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Flavin-containing monooxygenase FMO | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Flavin_mOase | ||||||||
| Pfam | PF00743 | ||||||||
| InterPro | IPR000960 | ||||||||
| Membranome | 262 | ||||||||
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The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms.[1] These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group.[2][3][4] FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals.[5] These monooxygenases are often misclassified because they share activity profiles similar to those of cytochrome P450 (CYP450), which is the major contributor to oxidative xenobiotic metabolism. However, a key difference between the two enzymes lies in how they proceed to oxidize their respective substrates; CYP enzymes make use of an oxygenated heme prosthetic group, while the FMO family utilizes FAD to oxidize its substrates.
- ^ Eswaramoorthy S, Bonanno JB, Burley SK, Swaminathan S (June 2006). "Mechanism of action of a flavin-containing monooxygenase". Proceedings of the National Academy of Sciences of the United States of America. 103 (26): 9832–9837. Bibcode:2006PNAS..103.9832E. doi:10.1073/pnas.0602398103. PMC 1502539. PMID 16777962.
- ^ Cashman JR (March 1995). "Structural and catalytic properties of the mammalian flavin-containing monooxygenase". Chemical Research in Toxicology. 8 (2): 166–81. doi:10.1021/tx00044a001. PMID 7766799.
- ^ Poulsen LL, Ziegler DM (April 1995). "Multisubstrate flavin-containing monooxygenases: applications of mechanism to specificity". Chemico-Biological Interactions. 96 (1): 57–73. doi:10.1016/0009-2797(94)03583-T. PMID 7720105.
- ^ Krueger SK, Williams DE (June 2005). "Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism". Pharmacology & Therapeutics. 106 (3): 357–387. doi:10.1016/j.pharmthera.2005.01.001. PMC 1828602. PMID 15922018.
- ^ Hernandez D, Addou S, Lee D, Orengo C, Shephard EA, Phillips IR (September 2003). "Trimethylaminuria and a human FMO3 mutation database". Human Mutation. 22 (3): 209–13. doi:10.1002/humu.10252. PMID 12938085. S2CID 5965257.