How many and which amino acids are responsible for the large activity differences between the highly homologous UDP-glucuronosyltransferases (UGT) 1A9 and UGT1A10?

@article{Itaho2010HowMA,
  title={How many and which amino acids are responsible for the large activity differences between the highly homologous UDP-glucuronosyltransferases (UGT) 1A9 and UGT1A10?},
  author={Katriina It{\"a}aho and Liisa Laakkonen and Moshe Finel},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2010},
  volume={38 4},
  pages={687-96}
}
The amino acid sequences of the human UDP-glucuronosyltransferases (UGTs) 1A9 and 1A10 are 93% identical, yet there are large differences in their activity and substrate selectivity. For example, the regioselectivity in propranolol glucuronidation, the regioselectivity in dobutamine glucuronidation, and the glucuronidation rate of alpha- and beta-estradiol differ greatly between UGT1A9 and UGT1A10. To identify the residue responsible for the activity differences, we divided the N-terminal half… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 29 references

Similar Papers

Loading similar papers…