Kinetic characterization of the 1A subfamily of recombinant human UDP-glucuronosyltransferases.

@article{Luukkanen2005KineticCO,
  title={Kinetic characterization of the 1A subfamily of recombinant human UDP-glucuronosyltransferases.},
  author={Leena Luukkanen and Jyrki Taskinen and Mika Kurkela and Risto Kostiainen and Jouni Hirvonen and Moshe Finel},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2005},
  volume={33 7},
  pages={1017-26}
}
The initial glucuronidation rates were determined for eight recombinant human UDP-glucuronosyltransferases (UGTs) of the 1A subfamily, and the bisubstrate kinetics and inhibition patterns were analyzed. At low substrate concentrations, the reactions followed general ternary complex kinetics, whereas at higher concentrations of both substrates, the reactions were mostly characterized by ternary complex kinetics with substrate inhibition. The glucuronidation of entacapone by UGT1A9 was inhibited… CONTINUE READING

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