메뉴 건너뛰기




Volumn 8, Issue 6, 2012, Pages 635-646

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

Author keywords

Crystal structure; Phase II metabolism; Substrate inhibition; Sulfonation; SULTs

Indexed keywords

3 CYANO 7 HYDROXYCOUMARIN; 3 HYDROXYCOUMARIN; 4 NITROPHENOL; ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; DAIDZEIN; ESTRADIOL; FLAVONE DERIVATIVE; FLAVONOL DERIVATIVE; GENISTEIN; HYDROGEN; ISOFLAVONE; KAEMPFEROL; PRASTERONE; RESVERATROL; SULFOTRANSFERASE; SULFOTRANSFERASE 1A1; SULFOTRANSFERASE 1A2; SULFOTRANSFERASE 1A3; SULFOTRANSFERASE 1B1; SULFOTRANSFERASE 1C1; SULFOTRANSFERASE 1C2; SULFOTRANSFERASE 1C3; SULFOTRANSFERASE 1E1; SULFOTRANSFERASE 2A1; SULFOTRANSFERASE 2B1; SULFOTRANSFERASE 2B1A; SULFOTRANSFERASE 2B1B; SULFOTRANSFERASE 4A1; SULFOTRANSFERASE M137; SULFOTRANSFERASE Y238; UNCLASSIFIED DRUG;

EID: 84862073598     PISSN: 17425255     EISSN: 17447607     Source Type: Journal    
DOI: 10.1517/17425255.2012.677027     Document Type: Review
Times cited : (41)

References (43)
  • 1
    • 4544226091 scopus 로고    scopus 로고
    • Sulfotransferases: Structure, mechanism, biological activity, inhibition, and synthetic utility
    • 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
    • (2004) Angew Chem Int Ed Engl , vol.43 , Issue.27 , pp. 3526-3548
    • Chapman, E.1    Best, M.D.2    Hanson, S.R.3    Wong, C.H.4
  • 2
    • 0036165473 scopus 로고    scopus 로고
    • Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: A case-control analysis
    • DOI 10.1016/S0169-5002(01)00406-8, PII S0169500201004068
    • Wang Y, Spitz MR, Tsou AM, et al. Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer 2002;35(2):137-42 (Pubitemid 34136090)
    • (2002) Lung Cancer , vol.35 , Issue.2 , pp. 137-142
    • Wang, Y.1    Spitz, M.R.2    Tsou, A.M.-H.3    Zhang, K.4    Makan, N.5    Wu, X.6
  • 3
    • 0034534841 scopus 로고    scopus 로고
    • Sulfotransferases in the bioactivation of xenobiotics
    • DOI 10.1016/S0009-2797(00)00202-7, PII S0009279700002027
    • Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem Biol Interact 2000;129(1-2):141-70 (Pubitemid 32061058)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 141-170
    • Glatt, H.1
  • 4
    • 0020022341 scopus 로고
    • Pharmacokinetics of 3H-phenylephrine in man
    • Hengstmann JH, Goronzy J. Pharmacokinetics of 3H-phenylephrine in man. Eur J Clin Pharmacol 1982;21(4):335-41
    • (1982) Eur J Clin Pharmacol , vol.21 , Issue.4 , pp. 335-341
    • Hengstmann, J.H.1    Goronzy, J.2
  • 5
    • 1642268315 scopus 로고    scopus 로고
    • A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily
    • DOI 10.1097/00008571-200403000-00009
    • Blanchard RL, Freimuth RR, Buck J, et al. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 2004;14(3):199-211 (Pubitemid 38373115)
    • (2004) Pharmacogenetics , vol.14 , Issue.3 , pp. 199-211
    • Blanchard, R.L.1    Freimuth, R.R.2    Buck, J.3    Weinshilboum, R.M.4    Coughtrie, M.W.H.5
  • 6
    • 34249799590 scopus 로고    scopus 로고
    • Identification and localization of soluble sulfotransferases in the human gastrointestinal tract
    • DOI 10.1042/BJ20061431
    • Teubner W, Meinl W, Florian S, et al. Identification and localization of soluble sulfotransferases in the human gastrointestinal tract. Biochem J 2007;404(2):207-15 (Pubitemid 46849592)
    • (2007) Biochemical Journal , vol.404 , Issue.2 , pp. 207-215
    • Teubner, W.1    Meinl, W.2    Florian, S.3    Kretzschmar, M.4    Glatt, H.5
  • 7
    • 70350319524 scopus 로고    scopus 로고
    • Quantitative evaluation of the expression and activity of five major sulfotransferases (SULTs) in human tissues: The SULT "pie"
    • 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
    • (2009) Drug Metab Dispos , vol.37 , Issue.11 , pp. 2255-2261
    • Riches, Z.1    Stanley, E.L.2    Bloomer, J.C.3    Coughtrie, M.W.4
  • 8
    • 34249073088 scopus 로고    scopus 로고
    • Structural and chemical profiling of the human cytosolic sulfotransferases
    • Allali-Hassani A, Pan PW, Dombrovski L, et al. Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol 2007;5(5):e97
    • (2007) PLoS Biol , vol.5 , Issue.5
    • Allali-Hassani, A.1    Pan, P.W.2    Dombrovski, L.3
  • 10
    • 77952745911 scopus 로고    scopus 로고
    • Crystal structures of SULT1A2 and SULT1A1 *3: Insights into the substrate inhibition and the role of Tyr149 in SULT1A2
    • Lu J, Li H, Zhang J, et al. 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
    • (2010) Biochem Biophys Res Commun , vol.396 , Issue.2 , pp. 429-434
    • Lu, J.1    Li, H.2    Zhang, J.3
  • 11
    • 80055109953 scopus 로고    scopus 로고
    • The molecular basis for the broad substrate specificity of human sulfotransferase 1A1
    • Berger I, Guttman C, Amar D, et al. The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. PLoS One 2011;6(11):e26794
    • (2011) PLoS One , vol.6 , Issue.11
    • Berger, I.1    Guttman, C.2    Amar, D.3
  • 12
    • 40849137940 scopus 로고    scopus 로고
    • Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1)
    • Lu LY, Hsieh YC, Liu MY, et al. Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Mol Pharmacol 2008;73(3):660-8
    • (2008) Mol Pharmacol , vol.73 , Issue.3 , pp. 660-668
    • Lu, L.Y.1    Hsieh, Y.C.2    Liu, M.Y.3
  • 15
    • 23744515308 scopus 로고    scopus 로고
    • Crystal structure of human sulfotransferase SULT1A3 in complex with dopamineand 3′-phosphoadenosine 5′-phosphate
    • Lu JH, Li HT, Liu MC, et al. Crystal structure of human sulfotransferase SULT1A3 in complex with dopamineand 3′-phosphoadenosine 5′-phosphate. Biochem Biophys Res Commun 2005;335(2):417-23
    • (2005) Biochem Biophys Res Commun , vol.335 , Issue.2 , pp. 417-423
    • Lu, J.H.1    Li, H.T.2    Liu, M.C.3
  • 16
    • 0037124087 scopus 로고    scopus 로고
    • 137 in the sulfuryl transfer reaction
    • DOI 10.1074/jbc.M111651200
    • 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 (Pubitemid 34967603)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 17928-17932
    • Pedersen, L.C.1    Petrotchenko, E.2    Shevtsov, S.3    Negishi, M.4
  • 17
    • 0037093546 scopus 로고    scopus 로고
    • Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate
    • Rehse PH, Zhou M, Lin SX. Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate. Biochem J 2002;364(Pt 1):165-71 (Pubitemid 34538959)
    • (2002) Biochemical Journal , vol.364 , Issue.1 , pp. 165-171
    • Rehse, P.H.1    Zhou, M.2    Lin, S.-X.3
  • 18
    • 1642453680 scopus 로고    scopus 로고
    • Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: Structure of the enzyme-ADT complex
    • DOI 10.1074/jbc.M310446200
    • 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 theenzyme-ADT complex. J Biol Chem 2004;279(4):2689-96 (Pubitemid 38114257)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2689-2696
    • Chang, H.-J.1    Shi, R.2    Rehse, P.3    Lin, S.-X.4
  • 22
    • 84886588118 scopus 로고    scopus 로고
    • Structural rearrangement of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation
    • 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
    • (2010) Horm Mol Biol Clin Investig , vol.1 , Issue.2 , pp. 81-87
    • Cook, I.T.1    Leyh, T.S.2    Kadlubar, S.A.3    Falany, C.N.4
  • 23
    • 80054939373 scopus 로고    scopus 로고
    • Substrate inhibition kinetics in drug metabolism reactions
    • Wu B. Substrate inhibition kinetics in drug metabolism reactions. Drug Metab Rev 2011;43(4):440-56
    • (2011) Drug Metab Rev , vol.43 , Issue.4 , pp. 440-456
    • Wu, B.1
  • 24
    • 79951943420 scopus 로고    scopus 로고
    • Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes
    • 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
    • (2011) Arch Biochem Biophys , vol.507 , Issue.2 , pp. 232-240
    • Gulcan, H.O.1    Duffel, M.W.2
  • 25
    • 0033543168 scopus 로고    scopus 로고
    • Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: Site-directed mutagenesis and kinetic studies
    • Brix LA, Barnett AC, Duggleby RG, et al. Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: site-directed mutagenesis and kinetic studies. Biochemistry 1999;38(32):10474-9
    • (1999) Biochemistry , vol.38 , Issue.32 , pp. 10474-10479
    • Brix, L.A.1    Barnett, A.C.2    Duggleby, R.G.3
  • 26
    • 12244310133 scopus 로고    scopus 로고
    • Differential activation of promutagens by alloenzymes of human sulfotransferase 1A2 expressed in Salmonella typhimurium
    • DOI 10.1097/00008571-200212000-00002
    • 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 (Pubitemid 36054935)
    • (2002) Pharmacogenetics , vol.12 , Issue.9 , pp. 677-689
    • Meinl, W.1    Meerman, J.H.N.2    Glatt, H.3
  • 29
    • 16544377221 scopus 로고    scopus 로고
    • Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases
    • Nakano H, Ogura K, Takahashi E, et al. Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases. Drug Metab Pharmacokinet 2004;19(3):216-26
    • (2004) Drug Metab Pharmacokinet , vol.19 , Issue.3 , pp. 216-226
    • Nakano, H.1    Ogura, K.2    Takahashi, E.3
  • 30
    • 80053510564 scopus 로고    scopus 로고
    • Regioselective Sulfation and glucuronidation of phenolics: Insights into the structural basis
    • Wu B, Basu S, Meng S, et al. Regioselective Sulfation and glucuronidation of phenolics: insights into the structural basis. Curr Drug Metab 2011;12(9):900-16
    • (2011) Curr Drug Metab , vol.12 , Issue.9 , pp. 900-916
    • Wu, B.1    Basu, S.2    Meng, S.3
  • 32
    • 0035666996 scopus 로고    scopus 로고
    • Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3′,5-triiodothyronine as the substrate
    • DOI 10.1677/joe.0.1710525
    • 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 (Pubitemid 34026367)
    • (2001) Journal of Endocrinology , vol.171 , Issue.3 , pp. 525-532
    • Li, X.1    Clemens, D.L.2    Cole, J.R.3    Anderson, R.J.4
  • 33
    • 0035216622 scopus 로고    scopus 로고
    • Differential expression of sulfotransferase enzymes involved in thyroid hormone metabolism during human placental development
    • DOI 10.1210/jc.86.12.5944
    • 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 (Pubitemid 33152648)
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , Issue.12 , pp. 5944-5955
    • Stanley, E.L.1    Hume, R.2    Visser, T.J.3    Coughtrie, M.W.H.4
  • 36
    • 29244470499 scopus 로고    scopus 로고
    • The structure of human SULT1A1 crystallized with estradiol: An insight into active site plasticity and substrate inhibition with multi-ring substrates
    • DOI 10.1074/jbc.M508289200
    • Gamage NU, Tsvetanov S, Duggleby RG, et al. 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 (Pubitemid 41832208)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41482-41486
    • Gamage, N.U.1    Tsvetanov, S.2    Duggleby, R.G.3    McManus, M.E.4    Martin, J.L.5
  • 37
    • 0037184096 scopus 로고    scopus 로고
    • 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
    • Fuda H, Lee YC, Shimizu C, et al. 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
    • (2002) J Biol Chem , vol.277 , Issue.39 , pp. 36161-36166
    • Fuda, H.1    Lee, Y.C.2    Shimizu, C.3
  • 38
    • 0242582327 scopus 로고    scopus 로고
    • 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 SULT2B1 isoforms
    • DOI 10.1074/jbc.M308312200
    • Lee KA, Fuda H, Lee YC, et al. 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 (Pubitemid 37377213)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44593-44599
    • Lee, K.A.1    Fuda, H.2    Lee, Y.C.3    Negishi, M.4    Strott, C.A.5    Pedersen, L.C.6
  • 40
    • 33748457919 scopus 로고    scopus 로고
    • Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3′-5′-diphosphate (PAP)
    • DOI 10.1002/prot.21048
    • 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 (Pubitemid 44420947)
    • (2006) Proteins: Structure, Function and Genetics , vol.64 , Issue.4 , pp. 1091-1094
    • Dombrovski, L.1    Dong, A.2    Bochkarev, A.3    Plotnikov, A.N.4
  • 41
    • 0037745545 scopus 로고    scopus 로고
    • Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase
    • 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 (Pubitemid 36790381)
    • (2003) Environmental Health Perspectives , vol.111 , Issue.7 , pp. 884-888
    • Shevtsov, S.1    Petrochenko, E.V.2    Pedersen, L.C.3    Negishi, M.4
  • 42
    • 0034625464 scopus 로고    scopus 로고
    • Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
    • DOI 10.1016/S0014-5793(00)01479-4, PII S0014579300014794
    • Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 2000;475(1):61-4 (Pubitemid 30331079)
    • (2000) FEBS Letters , vol.475 , Issue.1 , pp. 61-64
    • Pedersen, L.C.1    Petrotchenko, E.V.2    Negishi, M.3
  • 43
    • 0036080428 scopus 로고    scopus 로고
    • ENDscript: A workflow to display sequence and structure information
    • Gouet P, Courcelle E. ENDscript: a workflow to display sequence and structure information. Bioinformatics 2002;18(5):767-8 (Pubitemid 34679126)
    • (2002) Bioinformatics , vol.18 , Issue.5 , pp. 767-768
    • Gouet, P.1    Courcelle, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.