Triazolam substrate inhibition: evidence of competition for heme-bound reactive oxygen within the CYP3A4 active site.

@article{Schrag2001TriazolamSI,
  title={Triazolam substrate inhibition: evidence of competition for heme-bound reactive oxygen within the CYP3A4 active site.},
  author={Michael L Schrag and Larry C. Wienkers},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2001},
  volume={29 1},
  pages={70-5}
}
In human liver microsomes, triazolam is principally metabolized by CYP3A4 to form two metabolites, 1'-hydroxytriazolam (1'OHTz) and 4-hydroxytriazolam (4OHTz). The velocity of 1'OHTz formation was found to decrease at higher triazolam concentrations (>200 microM), indicative of "substrate inhibition". Coincubation of [(14)C]triazolam with authentic metabolite standards of either 1'OHTz or 4OHTz up to 30 microM did not significantly inhibit the rate of [(14)C]1'OHTz formation. The effects of… CONTINUE READING
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