Contribution of CYP3A4, CYP2B6, and CYP2C9 isoforms to N-demethylation of ketamine in human liver microsomes.

@article{Hijazi2002ContributionOC,
  title={Contribution of CYP3A4, CYP2B6, and CYP2C9 isoforms to N-demethylation of ketamine in human liver microsomes.},
  author={Youssef Hijazi and Roselyne Boulieu},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2002},
  volume={30 7},
  pages={
          853-8
        }
}
  • Y. Hijazi, R. Boulieu
  • Published 1 July 2002
  • Chemistry, Medicine
  • Drug metabolism and disposition: the biological fate of chemicals
Ketamine is a widely used drug for its anesthetic and analgesic properties; it is also considered as a drug of abuse, as many cases of ketamine illegal consumption were reported. Ketamine is N-demethylated by liver microsomal cytochrome P450 into norketamine. The identification of the enzymes responsible for ketamine metabolism is of great importance in clinical practice. In the present study, we investigated the metabolism of ketamine in human liver microsomes at clinically relevant… 
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TLDR
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TLDR
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Equine cytochrome P450 2B6--genomic identification, expression and functional characterization with ketamine.
TLDR
Equine CYP2B6 was determined to be a CYP enzyme involved in ketamine and norketamine metabolism, thus confirming results from inhibition studies with horse liver microsomes.
Effects of medetomidine and its active enantiomer dexmedetomidine on N‐demethylation of ketamine in canines determined in vitro using enantioselective capillary electrophoresis
TLDR
S‐ketamine combined with dexmedetomidine should be the best option for canines and the enantioselective CE assay with highly sulfated γ‐cyclodextrin as chiral selector is an effective tool for determining kinetic and inhibition parameters of metabolic pathways.
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