Glucuronidation of amines and hydroxylated xenobiotics and endobiotics catalyzed by expressed human UGT1.4 protein.

@article{Green1996GlucuronidationOA,
  title={Glucuronidation of amines and hydroxylated xenobiotics and endobiotics catalyzed by expressed human UGT1.4 protein.},
  author={Melinda Green and Thomas R. Tephly},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={1996},
  volume={24 3},
  pages={356-63}
}
Glucuronide conjugation of tertiary amine xenobiotics represents a unique and important metabolic pathway for these compounds in humans. In this study, we show that human UDP-glucuronosyltransferase 1.4 protein, stably expressed in human embryonic kidney 293 cells, catalyzes the N-glucuronidation of primary, secondary, and tertiary amine substrates. In addition, the substrate specificity of the expressed enzyme toward many hydroxylated and carboxylic acid-containing compounds was examined. Of… CONTINUE READING
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