In vitro metabolism of (-)-camphor using human liver microsomes and CYP2A6.
Article Details
- CitationCopy to clipboard
Gyoubu K, Miyazawa M
In vitro metabolism of (-)-camphor using human liver microsomes and CYP2A6.
Biol Pharm Bull. 2007 Feb;30(2):230-3.
- PubMed ID
- 17268056 [ View in PubMed]
- Abstract
The in vitro metabolism of (-)-camphor was examined in human liver microsomes and recombinant enzymes. Biotransformation of (-)-camphor was investigated by gas chromatography-mass spectrometry (GC-MS). (-)-Camphor was oxidized to 5-exo-hydroxyfenchone by human liver microsomal cytochrome (P450) enzymes. The formation of metabolites of (-)-camphor was determined by the relative abundance of mass fragments and retention time on gas chromatography (GC). CYP2A6 was the major enzyme involved in the hydroxylation of (-)-camphor by human liver microsomes, based on the following lines of evidence. First, of eleven recombinant human P450 enzymes tested, CYP2A6 catalyzed the oxidation of (-)-camphor. Second, oxidation of (-)-camphor was inhibited by (+)-menthofuran and anti-CYP2A6 antibody. Finally, there was a good correlation between CYP2A6 contents and (-)-camphor hydroxylation activities in liver microsomes of 9 human samples.
DrugBank Data that Cites this Article
- Drugs
- Drug Reactions
Reaction Details
