Steroid sulfation by expressed human cytosolic sulfotransferases.

作者: Charles N. Falany , James Wheeler , Tae Sung Oh , Josie L. Falany

DOI: 10.1016/0960-0760(94)90077-9

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摘要: Abstract The human cytosolic sulfotransferases (STs), dehydroepiandrosterone sulfotransferase (DHEA-ST) and the phenol-sulfating form of phenol sulfotransferase, (P-PST), have been expressed in bacteria used to investigate ability cloned enzymes conjugate steroids related compounds. DHEA-ST was capable sulfating all 3-hydroxysteroids, testosterone estrogens tested as substrates. androsterone, epiandrosterone androstenediol, were conjugated at 50–60% rate DHEA. Of tested, P-PST conjugating only estrogens. catechol estrogens, 2-hydroxyestradiol, 4-hydroxyestradiol 4-hydroxyestrone, compounds with estrogenic activity such 17α-ethynylestradiol trans -4-hydroxytamoxifen, also subtrates. showed little or no sulfation these compounds; however, sulfated by P-PST. These results indicate that STs are valuable analyzing overlapping substrate specificities may an important role metabolism tissues.

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