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Literature summary extracted from

  • Miyazawa, M.; Shindo, M.; Shimada, T.
    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.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.56 (3beta,16alpha)-3-hydroxy-20-oxopregn-5-ene-16-carbonitrile induces activity Rattus norvegicus
1.14.14.56 Phenobarbital induces activity Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.56 expression in insect cells Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.56 ketoconazole significant inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.56 0.02
-
1,8-cineole pH 7.4, 37°C, after treatment of animals with pregenolone-16alpha-carbonitrile Rattus norvegicus
1.14.14.56 0.05
-
1,8-cineole pH 7.4, 37°C Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.56 microsome
-
Rattus norvegicus
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.56 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.56 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.56 1,8-cineole + [reduced NADPH-hemoprotein reductase] + H+ + O2
-
Rattus norvegicus 2-exo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
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Synonyms

EC Number Synonyms Comment Organism
1.14.14.56 CYP3A4
-
Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.14.14.56 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