Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine.

@article{Niwa1999ContributionOH,
  title={Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine.},
  author={Toshiro Niwa and Ryo Sato and Yoshiyasu Yabusaki and Fumihide Ishibashi and Masanao Katagiri},
  journal={Xenobiotica; the fate of foreign compounds in biological systems},
  year={1999},
  volume={29 2},
  pages={187-93}
}
1. Aminopyrine N-demethylase activity was determined for 11 forms of human hepatic cytochrome P450s (P450s) expressed in yeast Saccharomyces cerevisiae and for human steroidogenic CYP17 expressed in Escherichia coli. 2. Among the hepatic P450s, the N-demethylation of aminopyrine was catalysed most efficiently by CYP2C19, followed by CYP2C8, 2D6, 2C18 and 1A2, whereas the activity with CYP2E1 was negligible. The kinetics of the N-demethylation process by CYP1A2, 2C8, 2C19 and 2D6 were studied by… CONTINUE READING