Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Homo sapiens | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxy-nabumetone + NADPH + H+ + O2 | Homo sapiens | activation reaction | ? + NADP+ + H2O | - |
? | |
N,N-dimethylaniline + NADPH + H+ + O2 | Homo sapiens | - |
N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P49326 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hepatocyte | - |
Homo sapiens | - |
liver | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxy-nabumetone + NADPH + H+ + O2 | activation reaction | Homo sapiens | ? + NADP+ + H2O | - |
? | |
N,N-dimethylaniline + NADPH + H+ + O2 | - |
Homo sapiens | N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
flavin-containing monooxygenase | - |
Homo sapiens |
flavin-containing monooxygenase 5 | - |
Homo sapiens |
hFMO5 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Homo sapiens | |
NADPH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | role of human flavin-containing monooxygenase (FMO) 5 in the metabolism of (4-(6-methoxynaphthalen-2-yl)butan-2-one, NAB): Baeyer-Villiger oxidation in the activation of the intermediate metabolite, 3-hydroxy-nabumetone, to the active metabolite, 6-methoxy-2-naphthylacetic acid (6-MNA) in vitro. The reaction involves carbon-carbon cleavage catalyzed by the Baeyer-Villiger oxidation (BVO) of a carbonyl compound, the BVO substrate, such as a ketol, by FMO5. Further in vitro inhibition experiments show that multiple non-CYP enzymes are involved in the formation of 6-MNA from 3-OH-NAB in human hepatocytes. NAB is a substrate for CYP1A2, CYP3A4, and CYP2J2. In the extract obtained from 3-hydroxy-nabumetone (3-OH-NAB) by a combined incubation of recombinant human FMO5 and human liver S9 | Homo sapiens |