Mouse steroid sulfotransferases. Substrate specificity and preliminary X-ray crystallographic analysis

Yoshimitsu Kakuta, Lars C. Pedersen, Kun Chae, Wen Chao Song, Darryl Leblanc, Robert London, Charles W. Carter, Masahiko Negishi

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


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 K(m) and V(max) 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 P21212, and diffracted to 2.5 Å.

Original languageEnglish
Pages (from-to)313-317
Number of pages5
JournalBiochemical Pharmacology
Issue number3
Publication statusPublished - Feb 1 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Pharmacology


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