Mouse steroid sulfotransferases: substrate specificity and preliminary X-ray crystallographic analysis

Biochem Pharmacol. 1998 Feb 1;55(3):313-7. doi: 10.1016/s0006-2952(97)00465-6.


Three mouse cytosolic sulfotransferases were expressed in Escherichia coli cells in order to study their substrate specificities toward natural as well as synthetic steroid hormones. The Km and Vmax values confirmed the high substrate specificity of estrogen and hydroxysteroid sulfotransferases toward estradiol and dehydroepiandrosterone, respectively. In sharp contrast, the synthetic estrogen diethylstilbestrol was metabolized efficiently by both enzymes to its disulfate ester. These sulfotransferases display highly stereospecific sulfotransferase activity for sulfating only the trans-isomer of diethylstilbestrol. Crystals suitable for high-resolution structure determination of estrogen sulfotransferase were grown with polyethylene glycol. The crystals belong to the orthorhombic space group P2(1)2(1)2, and diffracted to 2.5 A.

MeSH terms

  • Animals
  • Chromatography, High Pressure Liquid
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Kinetics
  • Mice
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Steroids / metabolism
  • Substrate Specificity
  • Sulfotransferases / chemistry
  • Sulfotransferases / metabolism*


  • Recombinant Proteins
  • Steroids
  • Sulfotransferases
  • steroid sulfotransferase