Alteration of human UDP-glucuronosyltransferase UGT2B17 regio-specificity by a single amino acid substitution.

@article{DuBois1999AlterationOH,
  title={Alteration of human UDP-glucuronosyltransferase UGT2B17 regio-specificity by a single amino acid substitution.},
  author={Steven G DuBois and Martin Beaulieu and Eric Levesque and Dean W. Hum and Alain B{\'e}langer},
  journal={Journal of molecular biology},
  year={1999},
  volume={289 1},
  pages={
          29-39
        }
}
The glucuronidation of steroid hormones is catalyzed by a family of UDP-glucuronosyltransferase (UGT) enzymes. Previously, two cDNA clones, UGT2B15 and UGT2B17, which encode UGT enzymes capable of glucuronidating C19steroids, were isolated and characterized. These proteins are 95% identical in primary structure; however, UGT2B17 is capable of conjugating C19steroid molecules at both the 3alpha and 17beta-OH positions, whereas UGT2B15 is only active at the 17beta-OH position. To identify the… CONTINUE READING
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