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Adams, J.B.: Enzymic synthesis of steroid sulphates. V. On the binding of estrogens to estrogen sulphotransferase. Biochim. Biophys. Acta, 146, 522–528 (1967)
Adams, J.B.; Chulavatnatol, M.: Enzymic synthesis of steroid sulphates. IV. The nature of the two forms of estrogen sulphotransferase of bovine adrenals. Biochim. Biophys. Acta, 146, 509–521 (1967)
Adams, J.B.; Poulos, A.: Enzymic synthesis of steroid sulphates. III. Isolation and properties of estrogen sulphotransferase of bovine adrenal glands. Biochim. Biophys. Acta, 146, 493–508 (1967)
Adams, J.B.; Ellyard, R.K.: Enzymic synthesis of steroid sulphates. VIII. Inhibition of estrogen sulphotransferase by retinoic acid and free fatty acids. Biochim. Biophys. Acta, 260, 724–730 (1972)
Adams, J.B.; Ellyard, R.K.; Low, J.: Enzymic synthesis of steroid sulphates. IX. Physical and chemical properties of purified oestrogen sulphotransferase from bovine adrenal glands, the nature of its isoenzymic forms and a proposed model to explain its wave-like kinetics. Biochim. Biophys. Acta, 370, 160–188 (1974)
Adams, J.B.; Low, J.: Enzymic synthesis of steroid sulphates. X. Isolation of oestrogen sulphotransferase from bovine placenta and comparison of its properties with adrenal oestrogen sulphotransferase. Biochim. Biophys. Acta, 370, 189–196 (1974)
Rozhin, J.; Soderstrom, R.L.; Brooks, S.C.: Specificity studies on bovine adrenal estrogen sulfotransferase. J. Biol. Chem., 249, 2079–2087 (1974)
Rozhin, J.; Huo, A.; Zemlicka, J.; Brooks, S.C.: Studies on bovine adrenal estrogen sulfotransferase. Inhibition and possible involvement of adenineestrogen stacking. J. Biol. Chem., 252, 7214–7220 (1977)
Horwitz, J.P.; Misra, R.S.; Rozhin, J.; Neenan, J.P.; Huo, A.; Godefroi, V.E.; Philips, K.D.; Chung, H.L.; Butke, G.; Brooks, S.C.: IV. Synthesis and assay of analogs of adenosine 3,5-diphosphate as inhibitors of bovine adrenal estrogen sulfotranferase. Biochim. Biophys. Acta, 525, 364–372 (1978)
Horwitz, J.P.; Misra, R.S.; Rozhin, J.; Helmer, S.; Bhuta, A.; Brooks, S.C.: Studies on bovine adrenal estrogen sulfotransferase. V. Synthesis and assay of analogs of 3-phosphoadenosine 5-phosphosulfate as cosubstrates for estrogen sulfurylation. Biochim. Biophys. Acta, 613, 85–94 (1980)
Freeman, D.J.; Saidi, F.; Hobkirk, R.: Estrogen sulfotransferase activity in guinea pig uterus and chorion. J. Steroid Biochem., 18, 23–27 (1983)
Tseng, L.; Lee, L.Y.; Mazella, J.: Estrogen sulfotransferase in human placenta. J. Steroid Biochem., 22, 611–615 (1985)
Dick, C.M.; Hobkirk, R.: Characteristics and behavior during partial purification of estrogen sulfotransferase of guinea pig liver and chorion. Biochim. Biophys. Acta, 925, 362–370 (1987)
Hobkirk, R.: Heterogeneity of guinea pig chorion and liver estrogen sulfotransferases. J. Steroid Biochem., 29, 87–91 (1988)
Hobkirk, R.; Glasier, M.A.; Brown, L.Y.: Purification and some characteristics of an oestrogen sulphotransferase from guinea pig adrenal gland and its non-identity with adrenal pregnenolone sulphotransferase. Biochem. J., 268, 759–764 (1990)
Adams, J.B.: Enzymic synthesis of steroid sulphates. XVII. On the structure of bovine estrogen sulphotransferase. Biochim. Biophys. Acta, 1076, 282–288 (1991)
Glasier, M.A.; Glutek, S.M.; Hobkirk, R.: Comparison of estrogen sulfotransferase and pregnenolone sulfotransferase of guinea pig. Steroids, 57, 295–300 (1992)
Oeda, T.; Lee, Y.C.; Driscoll, W.J.; Chen, H.C.; Strott, C.A.: Molecular cloning and expression of a full-length complementary DNA encoding the guinea pig adrenocortical estrogen sulfotransferase. Mol. Endocrinol., 6, 1216–1226 (1992)
Hondoh, T.; Suzuki, T.; Hirato, K.; Saitoh, H.; Kadofuku, T.; Sato, T.; Yanahara, T.: Purification and properties of estrogen sulfotransferase of human fetal liver. Biomed. Res., 14, 129–136 (1993)
Aksoy, I.A.; Wood, T.C.; Weinshilboum, R.: Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem. Biophys. Res. Commun., 200, 1621–1629 (1994)
Bernier, F.; Lopez, S.I.; Labrie, F.; van Luu, T.: Cloning and expression of cDNA encoding human placental estrogen sulfotransferase. Mol. Cell. Endocrinol., 99, R11–R15 (1994)
Forbes-Bamforth, K.J; Coughtrie, M.W.H.: Identification of a new adult human liver sulfotransferase with specificity for endogenous and xenobiotic estrogens. Biochem. Biophys. Res. Commun., 198, 707–711 (1994)
Lee, Y.C.; Komatsu, K.; Driscoll, W.J.; Strott, C.: Structural and functional characterization of estrogen sulfotransferase isoforms: distinct catalytic and high affinity binding activities. Mol. Endocrinol., 8, 1627–1635 (1994)
Lee, Y.C.; Komatsu, K.; Driscoll, W.J.; Strott, C.A.: Structural and functional characterization of estrogen sulfotransferase isoforms: distinct catalytic and high affinity binding activities. Mol. Endocrinol., 8, 1627–1635 (1994)
Tomizuka, T.; Oeda, T.; Tamura, Y.; Yoshida, S.; Strott, C.A.: Characterization of guinea pig estrogen sulfotransferase expressed by Chinese hamster ovary cell-Kl stable transfectants. Endocrinology, 135, 938–943 (1994)
Falany, J.L.; Krasnykh, V.; Mikheeva, G.; Falany, C.N.: Isolation and expression of an isoform of rat estrogen sulfotransferase. J. Steroid Biochem. Mol. Biol., 52, 35–44 (1995)
Falany, J.L.; Falany, C.N.: Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone. Endocrinology, 137, 1395–1401 (1996)
Her, C.; Szumlanski, C.; Aksoy, I.A.; Weinshilboum, R.M.: Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: immunochemical characterization of individual variation. Drug Metab. Dispos., 24, 1328–1335 (1996)
Chetrite, G.; Pasqualini, J.R.: Steroid sulphotransferase and 17β-hydroxysteroid dehydrogenase activities in Ishikawa human endometrial adenocarcinoma cells. J. Steroid Biochem. Mol. Biol., 61, 27–34 (1997)
Kakuta, Y.; Pedersen, L.C.; Chae, K.; Song, W.-C.; Leblanc, D.; London, R.; Carter, C.W.; Negishi, M.: Mouse steroid sulfotransferases. Substrate specificity and preliminary X-ray crystallographic analysis. Biochem. Pharmacol., 55, 313–317 (1998)
Kakuta, Y.; Petrotchenko, E.V.; Pedersen, L.C.; Negishi, M.: The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis. J. Biol. Chem., 273, 27325–27330 (1998)
Zhang, H.; Varlamova, O.; Vargas, F.M.; Falany, C.N.; Leyh, T.S.; Varmalova, O.: Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. J. Biol. Chem., 273, 10888–10892 (1998)
Chetrite, G.S.; Kloosterboer, H.J.; Philippe, J.C.; Pasqualini, J.R.: Effect of Org OD14 (LIVIAL) and its metabolites on human estrogen sulphotransferase activity in the hormone-dependent MCF-7 and T-47D, and the hormone-independent MDA-MB-231, breast cancer cell lines. Anticancer Res., 19, 269–275 (1999)
Pasqualini, J.R.; Chetrite, G.S.: Estrone sulfatase versus estrone sulfotransferase in human breast cancer: potential clinical applications. J. Steroid Biochem. Mol. Biol., 69, 287–292 (1999)
Petrotchenko, E.V.; Doerflein, M.E.; Kakuta, Y.; Pedersen, L.C.; Negishi, M.: Substrate gating confers steroid specificity to estrogen sulfotransferase. J. Biol. Chem., 274, 30019–30022 (1999)
Qian, Y.; Song, W.C.: Correlation between PAP-dependent steroid binding activity and substrate specificity of mouse and human estrogen sulfotransferases. J. Steroid Biochem. Mol. Biol., 71, 123–131 (1999)
Qian, Y.M.; Song, W.C.: Regulation of estrogen sulfotransferase expression in Leydig cells by cyclic adenosine 3′,5′-monophosphate and androgen. Endocrinology, 140, 1048–1053 (1999)
Hempel, N.; Barnett, A.C.; Bolton-Grob, R.M.; Liyou, N.E.; McManus, M.E.: Site-directed mutagenesis of the substrate-binding cleft of human estrogen sulfotransferase. Biochem. Biophys. Res. Commun., 276, 224–230 (2000)
Kester, M.H.; Bulduk, S.; Tibboel, D.; Meinl, W.; Glatt, H.; Falany, C.N.; Coughtrie, M.W.; Bergman, A.; Safe, S.H.; Kuiper, G.G.; Schuur, A.G.; Brouwer, A.; Visser, T.J.: Potent inhibition of estrogen sulfotransferase by hydroxylated PCB metabolites: a novel pathway explaining the estrogenic activity of PCBs. Endocrinology, 141, 1897–1900 (2000)
Otake, Y.; Nolan, A.L.; Walle, U.K.; Walle, T.: Quercetin and resveratrol potently reduce estrogen sulfotransferase activity in normal human mammary epithelial cells. J. Steroid Biochem. Mol. Biol., 73, 265–270 (2000)
Pai, T.G.; Suiko, M.; Sakakibara, Y.; Liu, M.-C.: Sulfation of flavonoids and other phenolic dietary compounds by the human cytosolic sulfotransferases. Biochem. Biophys. Res. Commun., 285, 1175–1179 (2001)
Song, W.C.: Biochemistry and reproductive endocrinology of estrogen sulfotransferase. Ann. N.Y. Acad. Sci., 948, 43–50 (2001)
Kester, M.H.; Bulduk, S.; van Toor, H.; Tibboel, D.; Meinl, W.; Glatt, H.; Falany, C.N.; Coughtrie, M.W.; Schuur, A.G.; Brouwer, A.; Visser, T.J.: Potent inhibition of estrogen sulfotransferase by hydroxylated metabolites of polyhalogenated aromatic hydrocarbons reveals alternative mechanism for estrogenic activity of endocrine disrupters. J. Clin. Endocrinol. Metab., 87, 1142–1150 (2002)
Pedersen, L.C.; Petrotchenko, E.; Shevtsov, S.; Negishi, M.: Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Serl37 in the sulfuryl transfer reaction. J. Biol. Chem., 277, 17928–17932 (2002)
Nakamura, Y.; Miki, Y.; Suzuki, T.; Nakata, T.; Darnel, A.D.; Moriya, T.; Tazawa, C.; Saito, H.; Ishibashi, T.; Takahashi, S.; Yamada, S.; Sasano, H.: Steroid sulfatase and estrogen sulfotransferase in the atherosclerotic human aorta. Am. J. Pathol., 163, 1329–1339 (2003)
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(2008). Estrone sulfotransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 39. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-71524-5_41
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