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  • Metabolism of (+)-fenchone by CYP2A6 and CYP2B6 in human liver microsomes.

Metabolism of (+)-fenchone by CYP2A6 and CYP2B6 in human liver microsomes.

Biological & pharmaceutical bulletin (2006-12-05)
Mitsuo Miyazawa, Kunihiko Gyoubu
ABSTRACT

The in vitro metabolism of (+)-fenchone was examined in human liver microsomes and recombinant enzymes. Biotransformation of (+)-fenchone was investigated by gas chromatography-mass spectrometry. (+)-Fenchone was found to be oxidized to 6-exo-hydroxyfenchone, 6-endo-hydroxyfenchone and 10-hydroxyfenchone by human liver microsomal P450 enzymes. The formation of metabolite of (+)-fenchone was determined by relative abundance of mass fragments and retention time with GC. CYP2A6 and CYP2B6 in human liver microsomes were major enzymes involved in the hydroxylation of (+)-fenchone, based on the following lines of evidence. First, of eleven recombinant human P450 enzymes tested, CYP2A6 and CYP2B6 catalyzed oxidation of (+)-fenchone. Second, oxidation of (+)-fenchone was inhibited by thioTEPA, (+)-menthofuran anti-CYP2A6 and anti-CYP2B6 antibodies. Finally, there was a good correlation between CYP2A6, CYP2B6 contents and (+)-fenchone hydroxylation activities in liver microsomes of 8 human samples.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
(+)-Fenchone, purum, ≥98.0% (sum of enantiomers, GC)
Supelco
(+)-Fenchone, analytical standard
Sigma-Aldrich
(1R)-(−)-Fenchone, ≥98%
Sigma-Aldrich
L-Fenchone, ≥98%