The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

FMO1  -  flavin containing monooxygenase 1

Canis lupus familiaris

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on FMO1

  • The amino acid sequence of dFMO1 was 89% homologous to human FMO1 [1].
  • By Western blotting, dog FMO1 and dog FMO3 were detected in microsomes from liver and lung but not in kidney microsomes [2].
  • The cDNAs of dog FMO1 and dog FMO3 encode proteins of 532 amino acids, which contain the NADPH- and FAD-binding sites [2].
  • Methionine has previously been shown to be S-oxidized by flavin-containing monooxygenase (FMO) forms 1, 2, and 3 [3].
  • 4. Human flavin-containing monooxygenase form 3 (FMO3) catalysed exclusively the N-oxidation to M3, with apparent Km and optimum pH comparable with those observed in human liver microsomes [4].
 

Biological context of FMO1

  • The use of enzyme inhibitors, activators and inducers indicated that EMA N-oxide formation was predominantly mediated by FMO in the presence of rabbit hepatic microsomes and that these agents did not generally affect the stereochemical outcome of the biotransformation [5].
 

Anatomical context of FMO1

 

Analytical, diagnostic and therapeutic context of FMO1

  • By Northern blotting, the probe for FMO1 specifically hybridized a 2.6-kilobase (kb) transcript in liver and lung samples only [2].

References

  1. Expression and characterization of functional dog flavin-containing monooxygenase 1. Stevens, J.C., Melton, R.J., Zaya, M.J., Engel, L.C. Mol. Pharmacol. (2003) [Pubmed]
  2. Cloning, sequencing, and tissue-dependent expression of flavin-containing monooxygenase (FMO) 1 and FMO3 in the dog. Lattard, V., Longin-Sauvageon, C., Lachuer, J., Delatour, P., Benoit, E. Drug Metab. Dispos. (2002) [Pubmed]
  3. Methionine S-oxidation in human and rabbit liver microsomes: evidence for a high-affinity methionine S-oxidase activity that is distinct from flavin-containing monooxygenase 3. Ripp, S.L., Itagaki, K., Philpot, R.M., Elfarra, A.A. Arch. Biochem. Biophys. (1999) [Pubmed]
  4. Interspecies comparison and role of human cytochrome P450 and flavin-containing monooxygenase in hepatic metabolism of L-775,606, a potent 5-HT(1D) receptor agonist. Prueksaritanont, T., Lu, P., Gorham, L., Sternfeld, F., Vyas, K.P. Xenobiotica (2000) [Pubmed]
  5. Species differences in the stereoselectivity of N-oxygenation of N-ethyl-N-methylaniline in vitro. Hadley, M.R., Oldham, H.G., Camilleri, P., Damani, L.A., Hutt, A.J. Chirality. (1996) [Pubmed]
  6. Estimation of flavin-containing monooxygenase activity in intact hepatocyte monolayers of rat, hamster, rabbit, dog and human by using N-oxidation of benzydamine. Ubeaud, G., Schiller, C.D., Hurbin, F., Jaeck, D., Coassolo, P. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. (1999) [Pubmed]
 
WikiGenes - Universities