Inhibition of UDP-glucuronosyltransferase 2b7-catalyzed morphine glucuronidation by ketoconazole: dual mechanisms involving a novel noncompetitive mode.

@article{Takeda2006InhibitionOU,
  title={Inhibition of UDP-glucuronosyltransferase 2b7-catalyzed morphine glucuronidation by ketoconazole: dual mechanisms involving a novel noncompetitive mode.},
  author={Shuso Takeda and Yurie Kitajima and Yuji Ishii and Yoshio Nishimura and Peter I. Mackenzie and Kazuta Oguri and Hideyuki Yamada},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2006},
  volume={34 8},
  pages={1277-82}
}
Glucuronidation of morphine in humans is predominantly catalyzed by UDP-glucuronosyltransferase 2B7 (UGT2B7). Since our recent research suggested that cytochrome P450s (P450s) interact with UGT2B7 to affect its function [Takeda S et al. (2005) Mol Pharmacol 67:665-672], P450 inhibitors are expected to modulate UGT2B7-catalyzed activity. To address this issue, we investigated the effects of P450 inhibitors (cimetidine, sulfaphenazole, erythromycin, nifedipine, and ketoconazole) on the UGT2B7… CONTINUE READING

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