Crystal structures of human sulfotransferases: insights into the mechanisms of action and substrate selectivity

Bibliography

• Chapman E, Best MD, Hanson SR, Wong CH. Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed Engl 2004;43(27):3526-48
   PubMed Web of Science ®Google Scholar
• Wang Y, Spitz MR, Tsou AM, Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer 2002;35(2):137-42
   PubMed Web of Science ®Google Scholar
• Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem Biol Interact 2000;129(1-2):141-70
   PubMed Web of Science ®Google Scholar
• Hengstmann JH, Goronzy J. Pharmacokinetics of 3H-phenylephrine in man. Eur J Clin Pharmacol 1982;21(4):335-41
   PubMed Web of Science ®Google Scholar
• Blanchard RL, Freimuth RR, Buck J, A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 2004;14(3):199-211
   PubMedGoogle Scholar
• Teubner W, Meinl W, Florian S, Identification and localization of soluble sulfotransferases in the human gastrointestinal tract. Biochem J 2007;404(2):207-15
   PubMed Web of Science ®Google Scholar
• Riches Z, Stanley EL, Bloomer JC, Coughtrie MW. Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: the SULT "pie". Drug Metab Dispos 2009;37(11):2255-61
   PubMed Web of Science ®Google Scholar
• Allali-Hassani A, Pan PW, Dombrovski L, Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol 2007;5(5):e97
   PubMed Web of Science ®Google Scholar
• Kakuta Y, Pedersen LG, Carter CW, Crystal structure of estrogen sulphotransferase. Nat Struct Biol 1997;4(11):904-8
   PubMedGoogle Scholar
• Lu J, Li H, Zhang J, Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun 2010;396(2):429-34
   PubMed Web of Science ®Google Scholar
• Berger I, Guttman C, Amar D, The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. PLoS One 2011;6(11):e26794
   PubMed Web of Science ®Google Scholar
• Lu LY, Hsieh YC, Liu MY, Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Mol Pharmacol 2008;73(3):660-8
   PubMed Web of Science ®Google Scholar
• Barnett AC, Tsvetanov S, Gamage N, Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3. J Biol Chem 2004;279(18):18799-805
   PubMed Web of Science ®Google Scholar
• Gamage NU, Duggleby RG, Barnett AC, Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem 2003;278(9):7655-62
   PubMed Web of Science ®Google Scholar
• Lu JH, Li HT, Liu MC, Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate. Biochem Biophys Res Commun 2005;335(2):417-23
   PubMed Web of Science ®Google Scholar
• Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem 2002;277(20):17928-32
   PubMed Web of Science ®Google Scholar
• Rehse PH, Zhou M, Lin SX. Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate. Biochem J 2002;364(Pt 1):165-71
   PubMedGoogle Scholar
• Chang HJ, Shi R, Rehse P, Lin SX. 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 2004;279(4):2689-96
   PubMed Web of Science ®Google Scholar
• Yoshinari K, Petrotchenko EV, Pedersen LC, Negishi M. Crystal structure-based studies of cytosolic sulfotransferase. J Biochem Mol Toxicol 2001;15(2):67-75
   PubMed Web of Science ®Google Scholar
• Gamage N, Barnett A, Hempel N, Human sulfotransferases and their role in chemical metabolism. Toxicol Sci 2006;90(1):5-22
   PubMed Web of Science ®Google Scholar
• Negishi M, Pedersen LG, Petrotchenko E, Structure and function of sulfotransferases. Arch Biochem Biophys 2001;390(2):149-57
   PubMed Web of Science ®Google Scholar
• Cook IT, Leyh TS, Kadlubar SA, Falany CN. Structural rearrangement of SULT2A1: effects on dehydroepiandrosterone and raloxifene sulfation. Horm Mol Biol Clin Investig 2010;1(2):81-7
   Google Scholar
• Wu B. Substrate inhibition kinetics in drug metabolism reactions. Drug Metab Rev 2011;43(4):440-56
   PubMed Web of Science ®Google Scholar
• Gulcan HO, Duffel MW. Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexes. Arch Biochem Biophys 2011;507(2):232-40
   PubMed Web of Science ®Google Scholar
• Brix LA, Barnett AC, Duggleby RG, Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: site-directed mutagenesis and kinetic studies. Biochemistry 1999;38(32):10474-9
   PubMed Web of Science ®Google Scholar
• Meinl W, Meerman JH, Glatt H. Differential activation of promutagens by alloenzymes of human sulfotransferase 1A2 expressed in Salmonella typhimurium. Pharmacogenetics 2002;12(9):677-89
   PubMedGoogle Scholar
• Rossi AM, Maggini V, Fredianelli E, Phenotype-genotype relationships of SULT1A1 in human liver and variations in the IC50 of the SULT1A1 inhibitor quercetin. Int J Clin Pharmacol Ther 2004;42(10):561-7
   PubMed Web of Science ®Google Scholar
• Dajani R, Cleasby A, Neu M, X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity. J Biol Chem 1999;274(53):37862-8
   PubMed Web of Science ®Google Scholar
• Nakano H, Ogura K, Takahashi E, Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases. Drug Metab Pharmacokinet 2004;19(3):216-26
   PubMedGoogle Scholar
• Wu B, Basu S, Meng S, Regioselective Sulfation and glucuronidation of phenolics: insights into the structural basis. Curr Drug Metab 2011;12(9):900-16
   PubMed Web of Science ®Google Scholar
• Glatt H, Boeing H, Engelke CE, Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. Mutat Res 2001;482(1-2):27-40
   PubMed Web of Science ®Google Scholar
• Li X, Clemens DL, Cole JR, Anderson RJ. Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate. J Endocrinol 2001;171(3):525-32
   PubMed Web of Science ®Google Scholar
• Stanley EL, Hume R, Visser TJ, Coughtrie MW. Differential expression of sulfotransferase enzymes involved in thyroid hormone metabolism during human placental development. J Clin Endocrinol Metab 2001;86(12):5944-55
   PubMed Web of Science ®Google Scholar
• Adjei AA, Weinshilboum RM. Catecholestrogen sulfation: possible role in carcinogenesis. Biochem Biophys Res Commun 2002;292(2):402-8
   PubMed Web of Science ®Google Scholar
• Honma W, Kamiyama Y, Yoshinari K, Enzymatic characterization and interspecies difference of phenol sulfotransferases, ST1A forms. Drug Metab Dispos 2001;29(3):274-81
   PubMed Web of Science ®Google Scholar
• Gamage NU, Tsvetanov S, Duggleby RG, The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem 2005;280(50):41482-6
   PubMed Web of Science ®Google Scholar
• Fuda H, Lee YC, Shimizu C, Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem 2002;277(39):36161-6
   PubMed Web of Science ®Google Scholar
• Lee KA, Fuda H, Lee YC, Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem 2003;278(45):44593-9
   PubMed Web of Science ®Google Scholar
• Bidwell LM, McManus ME, Gaedigk A, Crystal structure of human catecholamine sulfotransferase. J Mol Biol 1999;293(3):521-30
   PubMed Web of Science ®Google Scholar
• Dombrovski L, Dong A, Bochkarev A, Plotnikov AN. Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP). Proteins 2006;64(4):1091-4
   PubMed Web of Science ®Google Scholar
• Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M. Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect 2003;11(7):884-8
   Google Scholar
• Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 2000;475(1):61-4
   PubMed Web of Science ®Google Scholar
• Gouet P, Courcelle E. ENDscript: a workflow to display sequence and structure information. Bioinformatics 2002;18(5):767-8
   PubMed Web of Science ®Google Scholar