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Literature summary for 1.14.14.56 extracted from
- Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from Eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes (2001), Drug Metab. Dispos., 29, 200-205.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| (3beta,16alpha)-3-hydroxy-20-oxopregn-5-ene-16-carbonitrile | induces activity | Rattus norvegicus |  |
| Phenobarbital | induces activity | Rattus norvegicus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in insect cells | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ketoconazole | significant inhibition | Rattus norvegicus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.02 | - |
1,8-cineole | pH 7.4, 37°C, after treatment of animals with pregenolone-16alpha-carbonitrile | Rattus norvegicus | |
| 0.05 | - |
1,8-cineole | pH 7.4, 37°C | Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Rattus norvegicus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,8-cineole + [reduced NADPH-hemoprotein reductase] + H+ + O2 | - |
Rattus norvegicus | 2-exo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYP3A4 | - |
Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | CYP3A4 is a major enzyme involved in the oxidation of 1,8-cineole by human liver microsomes, as there is a good correlation between CYP3A4 contents and 1,8-cineole 2-hydroxylation activities in liver microsomes of eighteen human samples and of various recombinant human P450 enzymes examined, CYP3A4 has the highest activities for 1,8-cineole 2-hydroxylation | Rattus norvegicus |
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Release 2023.1 (January 2023)
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