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

研究成果: Contribution to journalArticle査読

27 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)313-317
ページ数5
ジャーナルBiochemical Pharmacology
55
3
DOI
出版ステータス出版済み - 2 1 1998
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Pharmacology

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