The functions of key residues in the inhibitor, substrate and cofactor sites of human 3β-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis

@article{Thomas2010TheFO,
  title={The functions of key residues in the inhibitor, substrate and cofactor sites of human 3β-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis},
  author={James L. Thomas and Vance L. Mack and Jingping Sun and James Ross Terrell and Kevin M. Bucholtz},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  year={2010},
  volume={120},
  pages={192-199}
}
In postmenopausal women, human 3beta-hydroxysteroid dehydrogenase type 1 (3beta-HSD1) is a critical enzyme in the conversion of DHEA to estradiol in breast tumors, while 3beta-HSD2 participates in the production of cortisol and aldosterone in the human adrenal gland. The goals of this project are to determine if Arg195 in 3beta-HSD1 vs. Pro195 in 3beta-HSD2 in the substrate/inhibitor binding site is a critical structural difference responsible for the higher affinity of 3beta-HSD1 for inhibitor… CONTINUE READING
BETA

References

Publications referenced by this paper.
SHOWING 1-10 OF 23 REFERENCES

Structural basis for the selective inhibition of human 3  - hydroxysteroid dehydrogenase 1 in human breast tumor MCF - 7 cells

  • R. J. Santen, S. J. Santner, +6 authors J. P. Wang
  • Mol . Cell Endocrinol .
  • 2009

Struc - ture / function of the inhibition of human 3  - hydroxysteroid dehydrogenase type 1 and type 2 by trilostane

  • V. L. Mack, J. A. Glow, D. Moshkelani, K. M. Bucholtz
  • J . Steroid Biochem . Mol . Biol .
  • 2008

Similar Papers

Loading similar papers…