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Review Article

Structure, dynamics and selectivity in the sulfotransferase family

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Pages 423-430 | Published online: 11 Sep 2013

References

  • Allali-Hassani A, Pan PW, Dombrovski L, et al. (2007). Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol 5:e97
  • Alnouti Y, Klaassen CD. (2006). Tissue distribution and ontogeny of sulfotransferase enzymes in mice. Toxicol Sci 93:242–255
  • Bai Q, Xu L, Kakiyama G, et al. (2011). Sulfation of 25-hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells. Atherosclerosis 214:350–356
  • Berger I, Guttman C, Amar D, et al. (2011). The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. PLoS One 6:e26794
  • Chang HJ, Shi R, Rehse P, Lin SX. (2004). Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: Structure of the enzyme-ADT complex. J Biol Chem 279:2689–2696
  • Cook I, Wang T, Almo SC, et al. (2013a). The gate that governs sulfotransferase selectivity. Biochemistry 52:415–424
  • Cook I, Wang T, Almo SC, et al. (2013b). Testing the sulfotransferase molecular pore hypothesis. J Biol Chem 288:8619–8626
  • Cook I, Wang T, Falany CN, Leyh TS. (2012). A nucleotide-gated molecular pore selects sulfotransferase substrates. Biochemistry 51:5674–5683
  • Cook IT, Duniec-Dmuchowski Z, Kocarek TA, et al. (2009). 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: Formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver × receptor activation. Drug Metab Dispos 37:2069–2078
  • Cook IT, Leyh TS, Kadlubar SA, Falany CN. (2010). Structural rearrangment of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation. Horm Mol Biol Clin Invest 1:81–87
  • Dong D, Ako R, Wu B. (2012). Crystal structures of human sulfotransferases: Insights into the mechanisms of action and substrate selectivity. Expert Opin Drug Metab Toxicol 8:635--646
  • Duffel MW, Jakoby WB. (1981). On the mechanism of aryl sulfotransferase. J Biol Chem 256:11123–11127
  • Falany CN. (1997). Enzymology of human cytosolic sulfotransferases. FASEB J 11:206–216
  • Falany CN, Vazquez ME, Heroux JA, Roth JA. (1990). Purification and characterization of human liver phenol-sulfating phenol sulfotransferase. Arch Biochem Biophys 278:312–318
  • Falany CN, Vazquez ME, Kalb JM. (1989). Purification and characterization of human liver dehydroepiandrosterone sulphotransferase. Biochem J 260:641–646
  • Falany JL, Azziz R, Falany CN. (1998). Identification and characterization of cytosolic sulfotransferases in normal human endometrium. Chem Biol Interact 109:329–339
  • Falany JL, Falany CN. (1996). Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone. Endocrinology 137:1395–1401
  • Falany JL, Macrina N, Falany CN. (2002). Regulation of MCF-7 breast cancer cell growth by beta-estradiol sulfation. Breast Cancer Res Treat 74:167–176
  • Falany JL, Pilloff DE, Leyh TS, Falany CN. (2006). Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases. Drug Metab Dispos 34:361–368
  • Gamage NU, Duggleby RG, Barnett AC, et al. (2003). Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem 278:7655–7662
  • Gamage NU, Tsvetanov S, Duggleby RG, et al. (2005). The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem 280:41482–41486
  • Gillespie J. (1981). The Causes of Molecular Evolution. Oxford, UK: Oxford University Press
  • Goresky CA. (1963). A linear method for determining liver sinusoidal and extravascular volumes. Am J Physiol 204:626–640
  • Gulcan HO, Duffel MW. (2011). Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes. Arch Biochem Biophys 507:232–240
  • Hallbrucker C, Vom Dahl S, Lang F, et al. (1991). Modification of liver cell volume by insulin and glucagon. Pflugers Arch 418:519–521
  • Jordan VC. (2007). SERMs: Meeting the promise of multifunctional medicines. J Natl Cancer Inst 99:350–356
  • Kakuta Y, Pedersen LG, Carter CW, et al. (1997). Crystal structure of estrogen sulphotransferase. Nat Struct Biol 4:904–908
  • Kase ET, Andersen B, Nebb HI, et al. (2006). 22-Hydroxycholesterols regulate lipid metabolism differently than T0901317 in human myotubes. Biochim Biophys Acta 1761:1515–1522
  • Klaassen CD, Boles JW. (1997). Sulfation and sulfotransferases 5: The importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J 11:404–418
  • Kotov A, Falany JL, Wang J, Falany CN. (1999). Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells. J Steroid Biochem Mol Biol 68:137–144
  • Labrie F, Bélanger A, Luu-The V, et al. (1998). DHEA and the intracrine formation of androgens and estrogens in peripheral target tissues: Its role during aging. Steroids 63:322–328
  • Latté KP, Appel KE, Lampen A. (2011). Health benefits and possible risks of broccoli -- an overview. Food Chem Toxicol 49:3287–3309
  • Lu J, Li H, Zhang J, et al. (2010). Crystal structures of SULT1A2 and SULT1A1 *3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun 396:429–434
  • Lu LY, Hsieh YC, Liu MY, et al. (2008). Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Mol Pharmacol 73:660–668
  • Mesiano S, Jaffe RB. (1997). Developmental and functional biology of the primate fetal adrenal cortex. Endocr Rev 18:378–403
  • Mishell DR, Thorneycroft IH, Nagata Y, et al. (1973). Serum gonadotropin and steroid patterns in early human gestation. Am J Obstet Gynecol 117:631–642
  • Moore KL. (2003). The biology and enzymology of protein tyrosine O-sulfation. J Biol Chem 278:24243–24246
  • Morris ME, Levy G. (1983). Serum concentration and renal excretion by normal adults of inorganic sulfate after acetaminophen, ascorbic acid, or sodium sulfate. Clin Pharmacol Ther 33:529–536
  • Nowell S, Falany CN. (2006). Pharmacogenetics of human cytosolic sulfotransferases. Oncogene 25:1673–1678
  • Okanoue T, Ohta M, Ou O, et al. (1985). Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study. Lab Invest 53:534–540
  • Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. (2002). Crystal structure of the human estrogen sulfotransferase-PAPS complex: Evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem 277:17928–17932
  • Pedersen LC, Petrotchenko EV, Negishi M. (2000). Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 475:61–64
  • Petrotchenko EV, Pedersen LC, Borchers CH, et al. (2001). The dimerization motif of cytosolic sulfotransferases. FEBS Lett 490:39–43
  • Poeppel P, Habetha M, Marcão A, et al. (2005). Missense mutations as a cause of metachromatic leukodystrophy. Degradation of arylsulfatase A in the endoplasmic reticulum. FEBS J 272:1179–1188
  • Rehse PH, Zhou M, Lin SX. (2002). Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate. Biochem J 364:165–171
  • Renwick AB, Ball SE, Tredger JM, et al. (2002). Inhibition of zaleplon metabolism by cimetidine in the human liver: In vitro studies with subcellular fractions and precision-cut liver slices. Xenobiotica 32:849–862
  • Riches Z, Stanley EL, Bloomer JC, Coughtrie MW. (2009). Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: The SULT “pie”. Drug Metab Dispos 37:2255–2261
  • Shore LS, Gurevitz M, Shemesh M. (1993). Estrogen as an environmental pollutant. Bull Environ Contam Toxicol 51:361–366
  • Sun M, Leyh TS. (2010). The human estrogen sulfotransferase: A half-site reactive enzyme. Biochemistry 49:4779–4785
  • Teubner W, Meinl W, Florian S, et al. (2007). Identification and localization of soluble sulfotransferases in the human gastrointestinal tract. Biochem J 404:207–215
  • Tyapochkin E, Cook PF, Chen G. (2008). Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry 47:11894–11899
  • Tyapochkin E, Cook PF, Chen G. (2009). para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the EċPAP complex and reformation of EċPAPS. J Biol Chem 284:29357–29364
  • Van Koevering MT, Gill DR, Owens FN, et al. (1995). Effect of time on feed on performance of feedlot steers, carcass characteristics, and tenderness and composition of longissimus muscles. J Anim Sci 73:21–28
  • Verdonk ML, Berdini V, Hartshorn MJ, et al. (2004). Virtual screening using protein-ligand docking: Avoiding artificial enrichment. J Chem Inf Comput Sci 44:793–806
  • Waterhouse AL. (2002). Wine phenolics. Ann N Y Acad Sci 957:21–36
  • Wynne HA, Wood P, Herd B, et al. (1992). The association of age with the activity of alcohol dehydrogenase in human liver. Age Ageing 21:417–420
  • Zhang H, Varlamova O, Vargas FM, et al. (1998). Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase. J Biol Chem 273:10888–10892
  • Zollner G, Trauner M. (2006). Molecular mechanisms of cholestasis. Wien Med Wochenschr 156:380–385

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