Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase
Open accessAbstract
Estrogen sulfotransferase (EST) catalyzes the transfer of the sulfuryl group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to 17beta-estradiol (E2). The sulfation of E2 prevents it from binding to, and thereby activating, the estrogen receptor. The regulation of EST appears to be causally linked to tumorigenesis in the breast and endometrium. In this study, recombinant human EST is characterized, and the catalytic mechanism of the transfer reaction is investigated in ligand binding and initial rate experiments. The native enzyme is a dimer of 35-kDa subunits. The apparent equilibrium constant for transfer to E2 is (4.5 +/- 0.2) x 10(3) at pH 6.3 and T = 25 +/- 2 degrees C. Initial rate studies provide the kinetic constants for the reaction and suggest a sequential mechanism. E2 is a partial substrate inhibitor (Ki = 80 +/- 5 nM). The binding of two E2 per EST subunit suggests that the partial inhibition occurs through binding at an allosteric site. In addition to providing the dissociation constants for the ligand-enzyme complexes, binding studies demonstrate that each substrate binds independently to the enzyme and that both the E.PAP.E2S and E.PAP.E2 dead-end complexes form. These results strongly suggest a Random Bi Bi mechanism with two dead-end complexes.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SULT1E1 is the major SULT for estrogen sulfation.
“SULT1E1 is the major SULT for estrogen sulfation [328,329], while SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity [327].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [328]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157 · see citing works
MOLECULAR MECHANISMS OF ACTION OF STEROID/THYROID RECEPTOR SUPERFAMILY MEMBERS
Tsai, M., & O’Malley, B. W. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.002315 · Cited by 2,887 · see citing works
[6] Statistical analysis of enzyme kinetic data
Cleland, W. W. (1979) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(79)63008-2 · Cited by 1,990 · see citing works
Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look
Wyman, J. (1964) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60190-4 · Cited by 1,613 · see citing works
Ultraviolet spectra Of Proteins and Amino Acids
Wetlaufer, D. B. (1963) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60056-x · Cited by 960 · see citing works
Maina, C. V., Riggs, P. D., Grandea, A. G., Slatko, B. E., Moran, L. S., Tagliamonte, J. A., McReynolds, L. A., & Chu, D. G. (1988) · Gene · doi:10.1016/0378-1119(88)90170-9 · Cited by 535 · see citing works
Cleland, W. W. (1970) · The Enzymes · doi:10.1016/s1874-6047(08)60180-8 · Cited by 512 · see citing works
Estrogen Receptors in the Rat Uterus
Shyamala, G., & Górski, J. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91813-2 · Cited by 282 · see citing works
Crystal structure of estrogen sulphotransferase
Kakuta, Y., Pedersen, L. G., Carter, C. W., Negishi, M., & Pedersen, L. C. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb1197-904 · Cited by 265 · see citing works
Fromm, H. J. (1975) · Molecular biology, biochemistry, and biophysics · doi:10.1007/978-3-642-80966-8 · Cited by 249 · see citing works
Jensen, R. T., Lemp, G. F., & Gardner, J. D. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83812-7 · Cited by 241 · see citing works
Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
Falany, C. N., Krasnykh, V., & Falany, J. L. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00015-r · Cited by 220 · see citing works
Self-citation[22] Measurement of ligand binding to proteins by fluorescence spectroscopy
Ward, L. D. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)17024-2 · Cited by 188 · see citing works
Steroid sulfation by expressed human cytosolic sulfotransferases
Falany, C. N., Wheeler, J. B., Oh, T. S., & Falany, J. L. (1994) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(94)90077-9 · Cited by 177 · see citing works
Self-citationHemmerich, S., Bertozzi, C. R., Leffler, H., & Rosen, S. D. (1994) · Biochemistry · doi:10.1021/bi00182a010 · Cited by 166 · see citing works
Falany, J. L., & Falany, C. N. (1996) · PubMed · Cited by 165 · see citing works
Self-citationOn the mechanism of aryl sulfotransferase.
Duffel, M. W., & Jakoby, W. B. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68565-0 · Cited by 134 · see citing works
Complete tyrosine-O-sulphation of gastrin in neonatal rat pancreas
Brand, S. J., Andersen, B. N., & Rehfeld, J. F. (1984) · Nature · doi:10.1038/309456a0 · Cited by 131 · see citing works
Merriam, G. R., MacLusky, N. J., Picard, M. K., & Naftolin, F. N. (1980) · Steroids · doi:10.1016/0039-128x(80)90062-8 · Cited by 111 · see citing works
The Physical Biochemistry and Molecular Genetics of Sulfate Activation
Leyh, T. S. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309085137 · Cited by 94 · see citing works
Self-citationHerschlag, D., & Jencks, W. P. (1990) · Biochemistry · doi:10.1021/bi00473a025 · Cited by 93 · see citing works
O-sulphated Leu-enkephalin in brain
Unsworth, C. D., Hughes, J. M., & Morley, J. S. (1982) · Nature · doi:10.1038/295519a0 · Cited by 86 · see citing works
Kobayashi, M., Habuchi, H., Habuchi, O., Saito, M., & Kimata, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7645 · Cited by 77 · see citing works
Unconjugated steroids in the human endometrium
Guerrero, R., Landgren, B.-M., Montiel, R., Čekan, Z., & Diczfalusy, E. R. (1975) · Contraception · doi:10.1016/0010-7824(75)90028-1 · Cited by 59 · see citing works
Garay, R. P., Labaune, J. P., Mesangeau, D., Nazaret, C., Imbert, T., & Moinet, G. (1990) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)23066-x · Cited by 19 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Falany, J. L., and Falany, C. N. (1998) Oncol. Res., in press
Cited by
Sorted by citations
Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility
Chapman, E., Best, M. D., Hanson, S. R., & Wong, C. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200300631 · Cited by 544 · see citing works
Schiffer, L., Barnard, L., Baranowski, E. S., Gilligan, L. C., Taylor, A. E., Arlt, W., Shackleton, C. H. L., & Storbeck, K.-H. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.105439 · Cited by 450 · see citing works
“[328,329], while SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity [327].”
Liu, X., Ji, K., & Choi, K. (2012) · Aquatic Toxicology · doi:10.1016/j.aquatox.2012.02.019 · Cited by 439 · see citing works
The Regulation of Steroid Action by Sulfation and Desulfation
Mueller, J. W., Gilligan, L. C., Idkowiak, J., Arlt, W., & Foster, P. A. (2015) · Endocrine Reviews · doi:10.1210/er.2015-1036 · Cited by 419 · see citing works
Enzymatic Mechanisms of Phosphate and Sulfate Transfer
Cleland, W. W., & Hengge, A. C. (2006) · Chemical Reviews · doi:10.1021/cr050287o · Cited by 404 · see citing works
Riches, Z., Stanley, E. L., Bloomer, J. C., & Coughtrie, M. W. H. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.028399 · Cited by 365 · see citing works
Wincent, E., Amini, N., Luecke-Johansson, S., Glatt, H. R., Bergman, J., Crescenzi, C., Rannug, A., & Rannug, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808321200 · Cited by 280 · see citing works
Wang, L., Falany, C. N., & James, M. O. (2004) · Drug Metabolism and Disposition · doi:10.1124/dmd.104.000273 · Cited by 187 · see citing works
Self-citationKester, M. H. A., Bulduk, S., van Toor, H., Tibboel, D., Meinl, W., Glatt, H., Falany, C. N., Coughtrie, M. W. H., Schuur, A. G., Brouwer, A., et al. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.3.1142 · Cited by 182 · see citing works
Self-citationStructure of a Human Carcinogen-converting Enzyme, SULT1A1
Gamage, N. U., Duggleby, R. G., Barnett, A. C., Tresillian, M. J., Latham, C. F., Liyou, N. E., McManus, M. E., & Martin, J. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207246200 · Cited by 168 · see citing works
X-ray Crystal Structure of Human Dopamine Sulfotransferase, SULT1A3
Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. M., Modi, S. P., Hersey, A., Taskinen, J., Cooke, R. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37862 · Cited by 158 · see citing works
Gong, H., Jarzynka, M. J., Cole, T. J., Lee, J. H., Wada, T., Zhang, B., Gao, J., Song, W., DeFranco, D. B., Cheng, S., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1545 · Cited by 155 · see citing works
Pharmacogenetics of soluble sulfotransferases (SULTs)
Glatt, H. R., & Meinl, W. (2004) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-003-0826-0 · Cited by 150 · see citing works
Nagar, S., WALTHER, S. E., & Blanchard, R. L. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.019240 · Cited by 144 · see citing works
Function and organization of the human cytosolic sulfotransferase (SULT) family
Coughtrie, M. W. H. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.05.005 · Cited by 142 · see citing works
Triclosan is a potent inhibitor of estradiol and estrone sulfonation in sheep placenta
James, M. O., Li, W., Summerlot, D. P., Rowland‐Faux, L., & Wood, C. E. (2009) · Environment International · doi:10.1016/j.envint.2009.02.004 · Cited by 134 · see citing works
Hirschmann, F., Krause, F., & Papenbrock, J. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00556 · Cited by 116 · see citing works
Interactions of cytosolic sulfotransferases with xenobiotics
James, M. O., & Ambadapadi, S. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2013.835613 · Cited by 113 · see citing works
Stanley, E. L., Hume, R., & Coughtrie, M. W. H. (2005) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.06.003 · Cited by 111 · see citing works
Biochemical characterization and tissue distribution of human SULT2B1
Geese, W. J., & Blanchard Raftogianis, R. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5746 · Cited by 98 · see citing works
Adjei, A. A., Thomae, B. A., Prondzinski, J. L., Eckloff, B. W., Wieben, E. D., & Weinshilboum, R. M. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705369 · Cited by 98 · see citing works
Gosavi, R. A., Knudsen, G. A., Birnbaum, L. S., & Pedersen, L. C. (2013) · Environmental Health Perspectives · doi:10.1289/ehp.1306902 · Cited by 96 · see citing works
Estrogen Sulfotransferases in Breast and Endometrial Cancers
Pasqualini, J. R. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04113.x · Cited by 95 · see citing works
Sulfation of Environmental Estrogens by Cytosolic Human Sulfotransferases
Nishiyama, T., Ogura, K., Nakano, H., Kaku, T., Takahashi, E., Ohkubo, Y., Sekine, K., Hiratsuka, A., Kadota, S., & Watabe, T. (2002) · Drug Metabolism and Pharmacokinetics · doi:10.2133/dmpk.17.221 · Cited by 94 · see citing works
Marine Polysaccharide Sulfatases
Helbert, W. (2017) · Frontiers in Marine Science · doi:10.3389/fmars.2017.00006 · Cited by 92 · see citing works
Regulation of MCF-7 Breast Cancer Cell Growth by β-estradiol Sulfation
Falany, J. L., Macrina, N., & Falany, C. N. (2002) · Breast Cancer Research and Treatment · doi:10.1023/a:1016147004188 · Cited by 92 · see citing works
Self-citationPinto, R., Tang, Q. X., Britton, W. J., Leyh, T. S., & Triccas, J. A. (2004) · Microbiology · doi:10.1099/mic.0.26894-0 · Cited by 90 · see citing works
Self-citationRegulation of the cytosolic sulfotransferases by nuclear receptors
Runge‐Morris, M., Kocarek, T. A., & Falany, C. N. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2012.748794 · Cited by 90 · see citing works
Self-citationRubin, G. L. (1999) · Molecular Human Reproduction · doi:10.1093/molehr/5.11.995 · Cited by 88 · see citing works
Enzymatic aspects of the phenol (aryl) sulfotransferases*
Duffel, M. W., Marshall, A., McPhie, P., Sharma, V., & Jakoby, W. B. (2001) · Drug Metabolism Reviews · doi:10.1081/dmr-120001394 · Cited by 87 · see citing works
Cook, I. T., Duniec-Dmuchowski, Z., Kocarek, T. A., Runge-Morris, M., & Falany, C. N. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.108.025759 · Cited by 86 · see citing works
Self-citationKirk, C. J., Bottomley, L., Minican, N., Carpenter, H., Shaw, S., Kohli, N., Winter, M. J., Taylor, E. W., Waring, R. H., Michelangeli, F., et al. (2003) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/s1095-6433(02)00366-5 · Cited by 83 · see citing works
Substrate inhibition kinetics in drug metabolism reactions
Wu, B. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.615320 · Cited by 78 · see citing works
Falany, C. N., He, D., Dumas, N., Frost, A. R., & Falany, J. L. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.09.011 · Cited by 77 · see citing works
Self-citationSULFATION OF RALOXIFENE AND 4-HYDROXYTAMOXIFEN BY HUMAN CYTOSOLIC SULFOTRANSFERASES
Falany, J. L., Pilloff, D. E., Leyh, T. S., & Falany, C. N. (2005) · Drug Metabolism and Disposition · doi:10.1124/dmd.105.006551 · Cited by 75 · see citing works
Self-citationSteroid metabolome in fetal and maternal body fluids in human late pregnancy
Hill, M., Pařı́zek, A., Cibula, D., Kancheva, R. L., Jirasek, J. E., Jirkovská, M., Velíková, M., Kubátová, J., Klímková, M., Pašková, A., et al. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.05.007 · Cited by 75 · see citing works
The Gate That Governs Sulfotransferase Selectivity
Cook, I. T., Wang, T., Almo, S. C., Kim, J., Falany, C. N., & Leyh, T. S. (2012) · Biochemistry · doi:10.1021/bi301492j · Cited by 74 · see citing works
Self-citationDiscovery of Estrogen Sulfotransferase Inhibitors from a Purine Library Screen
Verdugo, D. E., Cancilla, M. T., Ge, X., Gray, N. S., Chang, Y., Schultz, P. G., Negishi, M., Leary, J. A., & Bertozzi, C. R. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010171u · Cited by 74 · see citing works
Specific estrogen sulfotransferase (SULT1E1) substrates and molecular imaging probe candidates
Cole, G. B., Keum, G., Liu, J., Small, G. W., Satyamurthy, N., Kepe, V., & Barrio, J. R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914904107 · Cited by 73 · see citing works
Sulfation of “Estrogenic” Alkylphenols and 17β-Estradiol by Human Platelet Phenol Sulfotransferases
Harris, R. M., Waring, R. H., Kirk, C. J., & Hughes, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.159 · Cited by 71 · see citing works
Hudelist, G., Czerwenka, K., Keckstein, J., Haas, C., Fink-Retter, A., Gschwantler-Kaulich, D., Kubista, E., & Singer, C. F. (2007) · Reproductive Sciences · doi:10.1177/1933719107309120 · Cited by 70 · see citing works
Shevtsov, S. P., Petrotchenko, E. V., Pedersen, L. C., & Negishi, M. (2003) · Environmental Health Perspectives · doi:10.1289/ehp.6056 · Cited by 67 · see citing works
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases
Barbosa, A. C. S., Feng, Y., Yu, C., Huang, M., & Xie, W. (2019) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2019.1588884 · Cited by 66 · see citing works
Tibbs, Z. E., Rohn‐Glowacki, K. J., Crittenden, F., Guidry, A. L., & Falany, C. N. (2014) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2014.10.004 · Cited by 66 · see citing works
Self-citationRegulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells
Kotov, A., Falany, J. L., Wang, J., & Falany, C. N. (1999) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(99)00022-9 · Cited by 66 · see citing works
Self-citationSubstrate Gating Confers Steroid Specificity to Estrogen Sulfotransferase
Petrotchenko, E. V., Doerflein, M. E., Kakuta, Y., Pedersen, L. C., & Negishi, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30019 · Cited by 64 · see citing works
Crystal structure‐based studies of cytosolic sulfotransferase
Yoshinari, K., Petrotchenko, E. V., Pedersen, L. C., & Negishi, M. (2001) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.1 · Cited by 62 · see citing works
van den Hurk, P., Kubiczak, G. A., Lehmler, H., & James, M. O. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110343 · Cited by 62 · see citing works
Steroid catabolism in marine and freshwater fish
James, M. O. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.10.003 · Cited by 61 · see citing works
Wang, L., Li, J., Hao, F., Yuan, Y., Li, J., Lu, W., & Zhou, T. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.39 · Cited by 61 · see citing works
Active Site Mutations and Substrate Inhibition in Human Sulfotransferase 1A1 and 1A3
Barnett, A. C., Tsvetanov, S., Gamage, N. U., Martin, J. L., Duggleby, R. G., & McManus, M. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312253200 · Cited by 60 · see citing works
Estrogen Sulfotransferase/SULT1E1 Promotes Human Adipogenesis
Ihunnah, C. A., Wada, T., Philips, B. J., Ravuri, S. K., Gibbs, R. B., Kirisci, L., Rubin, J. P., Marra, K. G., & Xie, W. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01147-13 · Cited by 56 · see citing works
Schätzle, M. A., Flemming, S., Husain, S. M., Richter, M., Günther, S., & Müller, M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201107695 · Cited by 53 · see citing works
Yi, M., Negishi, M., & Lee, S. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11030194 · Cited by 52 · see citing works
Guo, Y., Hu, B., Huang, H., Tsung, A., Gaikwad, N. W., Xu, M., Jiang, M., Ren, S., Fan, J., Billiar, T. R., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.642124 · Cited by 52 · see citing works
Lu, L.-Y., Hsieh, Y., Liu, M., Lin, Y.-H., Chen, C., & Yang, Y. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.041038 · Cited by 52 · see citing works
Vargas-Martínez, F., Uvnás-Moberg, K., Petersson, M., Olausson, H., & Jiménez-Estrada, I. (2014) · Progress in neurobiology · doi:10.1016/j.pneurobio.2014.10.001 · Cited by 49 · see citing works
Tabrett, C. A., & Coughtrie, M. W. H. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00582-3 · Cited by 51 · see citing works
SULT genetic polymorphisms: physiological, pharmacological and clinical implications
Kurogi, K., Rasool, M. I., Alherz, F. A., Daibani, A. A. E., Bairam, A. F., Abunnaja, M. S., Yasuda, S., Wilson, L. J., Hui, Y., & Liu, M. (2021) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2021.1940952 · Cited by 50 · see citing works
James, M. O., Marth, C. J., & Rowland‐Faux, L. (2012) · Aquatic Toxicology · doi:10.1016/j.aquatox.2012.07.009 · Cited by 48 · see citing works
Ginsberg, G., Guyton, K. Z., Johns, D. O., Schimek, J., Angle, K., & Sonawane, B. R. (2010) · Critical Reviews in Toxicology · doi:10.3109/10408441003742895 · Cited by 47 · see citing works
Klein, M., & Papenbrock, J. (2008) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2008.01182.x · Cited by 46 · see citing works
A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates
Cook, I. T., Wang, T., Falany, C. N., & Leyh, T. S. (2012) · Biochemistry · doi:10.1021/bi300631g · Cited by 45 · see citing works
Self-citationIwuchukwu, O. F., & Nagar, S. (2007) · Drug Metabolism and Disposition · doi:10.1124/dmd.107.018788 · Cited by 45 · see citing works
Wang, L.-Q., & James, M. O. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2005.05.002 · Cited by 43 · see citing works
High Accuracy in Silico Sulfotransferase Models
Cook, I. T., Wang, T., Falany, C. N., & Leyh, T. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510974 · Cited by 43 · see citing works
Self-citationParadigms of Sulfotransferase Catalysis
Wang, T., Cook, I. T., Falany, C. N., & Leyh, T. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573501 · Cited by 43 · see citing works
Self-citationGülcan, H. O., & Duffel, M. W. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.027 · Cited by 43 · see citing works
The Role of Sulfotransferases in Liver Diseases
Xie, Y., & Xie, W. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.120.000074 · Cited by 42 · see citing works
Redox Control of Aryl Sulfotransferase Specificity
Marshall, A., McPhie, P., & Jakoby, W. B. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2020 · Cited by 42 · see citing works
SOLVENT EFFECT ON cDNA-EXPRESSED HUMAN SULFOTRANSFERASE (SULT) ACTIVITIES IN VITRO
Ma, B., Shou, M., & Schrag, M. L. (2003) · Drug Metabolism and Disposition · doi:10.1124/dmd.31.11.1300 · Cited by 41 · see citing works
Steroid sulfatase and estrogen sulfotransferase in human carcinomas
Suzuki, T., Miki, Y., Nakamura, Y., Ito, K., & Sasano, H. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.11.001 · Cited by 39 · see citing works
Structural characterization of human aryl sulphotransferases
Brix, L. A., Duggleby, R. G., Gaedigk, A., & McManus, M. E. (1999) · Biochemical Journal · doi:10.1042/bj3370337 · Cited by 39 · see citing works
Burkart, M. D., & Wong, C. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4264 · Cited by 39 · see citing works
Hemmerich, S. (2001) · Drug Discovery Today · doi:10.1016/s1359-6446(00)01581-6 · Cited by 38 · see citing works
Structural rearrangement of SULT2A1: effects on dehydroepiandrosterone and raloxifene sulfation
Cook, I. T., Leyh, T. S., Kadlubar, S. A., & Falany, C. N. (2009) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci.2010.012 · Cited by 38 · see citing works
Self-citationPi, N., Yu, Y., Mougous, J. D., & Leary, J. A. (2004) · Protein Science · doi:10.1110/ps.03581904 · Cited by 38 · see citing works
Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry
Pi, N., Hoang, M. B., Gao, H. X., Mougous, J. D., Bertozzi, C. R., & Leary, J. A. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.02.004 · Cited by 37 · see citing works
Ikenaka, Y., Oguri, M., Saengtienchai, A., Nakayama, S. M. M., Ijiri, S., & Ishizuka, M. (2013) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2013.05.018 · Cited by 35 · see citing works
The Human Estrogen Sulfotransferase: A Half-Site Reactive Enzyme
Sun, M., & Leyh, T. S. (2010) · Biochemistry · doi:10.1021/bi902190r · Cited by 35 · see citing works
Self-citationStructure, dynamics and selectivity in the sulfotransferase family
Leyh, T. S., Cook, I. T., & Wang, T. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2013.835625 · Cited by 35 · see citing works
Self-citationRakers, C., Schumacher, F., Meinl, W., Glatt, H. R., Kleuser, B., & Wolber, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685610 · Cited by 35 · see citing works
King, R. J., Ghosh, A., & Wu, J. (2006) · Current Drug Metabolism · doi:10.2174/138920006778520615 · Cited by 35 · see citing works
Rohn‐Glowacki, K. J., Cook, I. T., Leyh, T. S., Kadlubar, S. A., & Falany, C. N. (2012) · Drug Metabolism and Disposition · doi:10.1124/dmd.112.045583 · Cited by 33 · see citing works
Self-citationSULFONATION OF ENVIRONMENTAL CHEMICALS AND THEIR METABOLITES IN THE POLAR BEAR (Ursus maritimus)
Sacco, J., & James, M. O. (2005) · Drug Metabolism and Disposition · doi:10.1124/dmd.105.004648 · Cited by 32 · see citing works
3′-Phosphoadenosine 5′-Phosphosulfate Allosterically Regulates Sulfotransferase Turnover
Wang, T., Cook, I. T., & Leyh, T. S. (2014) · Biochemistry · doi:10.1021/bi501120p · Cited by 32 · see citing works
Self-citationWang, L.-Q., Lehmler, H., Robertson, L. W., Falany, C. N., & James, M. O. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.7837 · Cited by 32 · see citing works
Self-citationLu, F., Yuen, Y.-L., Xu, J., Liu, X., Chan, M. Y.-C., Wang, K., Fong, W., Cheung, W., & Lee, S. S. T. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m074302 · Cited by 31 · see citing works
Parker, V. S., Squirewell, E. J., Lehmler, H., Robertson, L. W., & Duffel, M. W. (2018) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2018.01.010 · Cited by 31 · see citing works
Substrate Specificity and Kinetic Mechanism of the Insect Sulfotransferase, Retinol Dehydratase
Vakiani, E., Luz, J. G., & Buck, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35381 · Cited by 31 · see citing works
Itäaho, K., Alakurtti, S., Yli‐Kauhaluoma, J. T., Taskinen, J., Coughtrie, M. W. H., & Kostiainen, R. K. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.05.003 · Cited by 30 · see citing works
Sasaki, Y., Miki, Y., Hirakawa, H., Onodera, Y., Takagi, K., Akahira, J., Honma, S., Ishida, T., Watanabe, M., Sasano, H., et al. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01673.x · Cited by 30 · see citing works
Li, L., & Falany, C. N. (2006) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2006.05.001 · Cited by 30 · see citing works
Self-citationWong, S. Q., Tan, K. H., Carey, K. T., Fukushima, A., Tiganis, T., & Cole, T. J. (2009) · Endocrinology · doi:10.1210/en.2009-0590 · Cited by 30 · see citing works
Sulphation of o‐desmethylnaproxen and related compounds by human cytosolic sulfotransferases
Falany, C. N., Ström, P., & Swedmark, S. (2005) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2005.02506.x · Cited by 29 · see citing works
Self-citationSteuer, A. E., Meyer, M. R., Zapp, J., & Maurer, H. H. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.01.026 · Cited by 29 · see citing works
Furimsky, A. M., Green, C. E., Sharp, L. E. H., Catz, P., Adjei, A. A., Parman, T., Kapetanović, I. M., Weinshilboum, R. M., & Iyer, L. (2007) · Drug Metabolism and Disposition · doi:10.1124/dmd.107.016725 · Cited by 29 · see citing works
Testing the Sulfotransferase Molecular Pore Hypothesis
Cook, I. T., Wang, T., Almo, S. C., Kim, J., Falany, C. N., & Leyh, T. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.445015 · Cited by 28 · see citing works
Self-citationRiches, Z., Bloomer, J. C., & Coughtrie, M. W. H. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.04.006 · Cited by 28 · see citing works
Danan, L. M., Yu, Z., Ludden, P. J., Jia, W., Moore, K. L., & Leary, J. A. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.03.037 · Cited by 27 · see citing works
- Authors
- Zhang, H., Varmalova, O., Vargas, F. M., Falany, C. N., & Leyh, T. S.
- Affiliations
- Albert Einstein College of Medicine (US)
- University of Alabama at Birmingham (US)
- Corresponding author
- Leyh, Thomas S.
- ORCID
- Leyh, Thomas S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-05
- Volume
- 273
- Issue
- 18
- Pages
- 10888-10892
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968379731
- Cited by
- 223
- References
- 26
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 5 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 7 · 2015: 10 · 2014: 13 · 2013: 12 · 2012: 15
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM54469, GM38953)
- National Institute of General Medical Sciences (GM 54469, R01GM054469, GM-38953)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
- Keywords
- estrogen sulfotransferase, PAPS, catalytic mechanism, sequential mechanism, dead-end complex, substrate inhibition, allosteric binding, enzyme kinetics, estrogen receptor, breast cancer, endometrial cancer, enzyme dimer
- MeSH terms
- Catalysis, Cell Line, Chromatography, Gel, Humans, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Protein Binding, Sulfites, Sulfotransferases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review