메뉴 건너뛰기




Volumn 52, Issue 2, 2013, Pages 415-424

The gate that governs sulfotransferase selectivity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING STUDIES; CLOSED PORE; CYTOSOLIC; CYTOSOLS; HUMAN LIVER; IN-SILICO; MOLECULAR BASIS; NONEQUILIBRIUM MOLECULAR DYNAMICS SIMULATION; PRIMARY AMINES; SELECTION MECHANISM; SUBSTRATE SELECTION;

EID: 84872506191     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301492j     Document Type: Article
Times cited : (66)

References (56)
  • 1
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany, C. N. (1997) Enzymology of human cytosolic sulfotransferases FASEB J. 11, 206-216
    • (1997) FASEB J. , vol.11 , pp. 206-216
    • Falany, C.N.1
  • 2
    • 79151476474 scopus 로고    scopus 로고
    • Sulfation of 25-hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells
    • Bai, Q., Xu, L., Kakiyama, G., Runge-Morris, M. A., Hylemon, P. B., Yin, L., Pandak, W. M., and Ren, S. (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
    • (2011) Atherosclerosis , vol.214 , pp. 350-356
    • Bai, Q.1    Xu, L.2    Kakiyama, G.3    Runge-Morris, M.A.4    Hylemon, P.B.5    Yin, L.6    Pandak, W.M.7    Ren, S.8
  • 3
    • 0032080151 scopus 로고    scopus 로고
    • Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase
    • Zhang, H., Varlamova, O., Vargas, F. M., Falany, C. N., and Leyh, T. S. (1998) Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase J. Biol. Chem. 273, 10888-10892
    • (1998) J. Biol. Chem. , vol.273 , pp. 10888-10892
    • Zhang, H.1    Varlamova, O.2    Vargas, F.M.3    Falany, C.N.4    Leyh, T.S.5
  • 4
    • 0344172843 scopus 로고    scopus 로고
    • Dehydroepiandrosterone and dehydroepiandrosterone sulfate production in the human adrenal during development and aging
    • Parker, C. R. (1999) Dehydroepiandrosterone and dehydroepiandrosterone sulfate production in the human adrenal during development and aging Steroids 64, 640-647
    • (1999) Steroids , vol.64 , pp. 640-647
    • Parker, C.R.1
  • 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, E. L., Bloomer, J. C., and Coughtrie, M. W. (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
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 2255-2261
    • Riches, Z.1    Stanley, E.L.2    Bloomer, J.C.3    Coughtrie, M.W.4
  • 8
    • 33645122881 scopus 로고    scopus 로고
    • Pharmacogenetics of human cytosolic sulfotransferases
    • Nowell, S. and Falany, C. N. (2006) Pharmacogenetics of human cytosolic sulfotransferases Oncogene 25, 1673-1678
    • (2006) Oncogene , vol.25 , pp. 1673-1678
    • Nowell, S.1    Falany, C.N.2
  • 9
    • 34249799590 scopus 로고    scopus 로고
    • Identification and localization of soluble sulfotransferases in the human gastrointestinal tract
    • Teubner, W., Meinl, W., Florian, S., Kretzschmar, M., and Glatt, H. (2007) Identification and localization of soluble sulfotransferases in the human gastrointestinal tract Biochem. J. 404, 207-215
    • (2007) Biochem. J. , vol.404 , pp. 207-215
    • Teubner, W.1    Meinl, W.2    Florian, S.3    Kretzschmar, M.4    Glatt, H.5
  • 10
    • 80055109953 scopus 로고    scopus 로고
    • The molecular basis for the broad substrate specificity of human sulfotransferase 1A1
    • Berger, I., Guttman, C., Amar, D., Zarivach, R., and Aharoni, A. (2011) The molecular basis for the broad substrate specificity of human sulfotransferase 1A1 PLoS One 6, e26794
    • (2011) PLoS One , vol.6 , pp. 26794
    • Berger, I.1    Guttman, C.2    Amar, D.3    Zarivach, R.4    Aharoni, A.5
  • 12
    • 0022540097 scopus 로고
    • Purification and kinetic characterization of a phenol-sulfating form of phenol sulfotransferase from human brain
    • Whittemore, R. M., Pearce, L. B., and Roth, J. A. (1986) Purification and kinetic characterization of a phenol-sulfating form of phenol sulfotransferase from human brain Arch. Biochem. Biophys. 249, 464-471
    • (1986) Arch. Biochem. Biophys. , vol.249 , pp. 464-471
    • Whittemore, R.M.1    Pearce, L.B.2    Roth, J.A.3
  • 14
    • 0034534841 scopus 로고    scopus 로고
    • Sulfotransferases in the bioactivation of xenobiotics
    • Glatt, H. (2000) Sulfotransferases in the bioactivation of xenobiotics Chem.-Biol. Interact. 129, 141-170
    • (2000) Chem.-Biol. Interact. , vol.129 , pp. 141-170
    • Glatt, H.1
  • 16
    • 31844448260 scopus 로고    scopus 로고
    • Human sulphotransferases are involved in the activation of aristolochic acids and are expressed in renal target tissue
    • Meinl, W., Pabel, U., Osterloh-Quiroz, M., Hengstler, J. G., and Glatt, H. (2006) Human sulphotransferases are involved in the activation of aristolochic acids and are expressed in renal target tissue Int. J. Cancer 118, 1090-1097
    • (2006) Int. J. Cancer , vol.118 , pp. 1090-1097
    • Meinl, W.1    Pabel, U.2    Osterloh-Quiroz, M.3    Hengstler, J.G.4    Glatt, H.5
  • 17
    • 0020077328 scopus 로고
    • Acetaminophen and phenol: Substrates for both a thermostable and a thermolabile form of human platelet phenol sulfotransferase
    • Reiter, C. and Weinshilboum, R. M. (1982) Acetaminophen and phenol: Substrates for both a thermostable and a thermolabile form of human platelet phenol sulfotransferase J. Pharmacol. Exp. Ther. 221, 43-51
    • (1982) J. Pharmacol. Exp. Ther. , vol.221 , pp. 43-51
    • Reiter, C.1    Weinshilboum, R.M.2
  • 18
    • 2542445645 scopus 로고    scopus 로고
    • Zebrafish tyrosylprotein sulfotransferase: Molecular cloning, expression, and functional characterization
    • Mishiro, E., Liu, M. Y., Sakakibara, Y., Suiko, M., and Liu, M. C. (2004) Zebrafish tyrosylprotein sulfotransferase: Molecular cloning, expression, and functional characterization Biochem. Cell Biol. 82, 295-303
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 295-303
    • Mishiro, E.1    Liu, M.Y.2    Sakakibara, Y.3    Suiko, M.4    Liu, M.C.5
  • 20
    • 80054762464 scopus 로고    scopus 로고
    • Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1
    • Ekuase, E. J., Liu, Y., Lehmler, H. J., Robertson, L. W., and Duffel, M. W. (2011) Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1 Chem. Res. Toxicol. 24, 1720-1728
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1720-1728
    • Ekuase, E.J.1    Liu, Y.2    Lehmler, H.J.3    Robertson, L.W.4    Duffel, M.W.5
  • 21
    • 33344467530 scopus 로고    scopus 로고
    • Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases
    • Falany, J. L., Pilloff, D. E., Leyh, T. S., and Falany, C. N. (2006) Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases Drug Metab. Dispos. 34, 361-368
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 361-368
    • Falany, J.L.1    Pilloff, D.E.2    Leyh, T.S.3    Falany, C.N.4
  • 22
    • 67650844254 scopus 로고    scopus 로고
    • Selective role of sulfotransferase 2A1 (SULT2A1) in the N-sulfoconjugation of quinolone drugs in humans
    • Senggunprai, L., Yoshinari, K., and Yamazoe, Y. (2009) Selective role of sulfotransferase 2A1 (SULT2A1) in the N-sulfoconjugation of quinolone drugs in humans Drug Metab. Dispos. 37, 1711-1717
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1711-1717
    • Senggunprai, L.1    Yoshinari, K.2    Yamazoe, Y.3
  • 24
    • 84863931141 scopus 로고    scopus 로고
    • A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates
    • Cook, I., Wang, T., Falany, C. N., and Leyh, T. S. (2012) A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates Biochemistry 51, 5674-83
    • (2012) Biochemistry , vol.51 , pp. 5674-5683
    • Cook, I.1    Wang, T.2    Falany, C.N.3    Leyh, T.S.4
  • 25
    • 0031149235 scopus 로고    scopus 로고
    • Human sulfotransferase SULT1C1: CDNA cloning, tissue-specific expression, and chromosomal localization
    • Her, C., Kaur, G. P., Athwal, R. S., and Weinshilboum, R. M. (1997) Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization Genomics 41, 467-470
    • (1997) Genomics , vol.41 , pp. 467-470
    • Her, C.1    Kaur, G.P.2    Athwal, R.S.3    Weinshilboum, R.M.4
  • 26
    • 77953261062 scopus 로고    scopus 로고
    • The human estrogen sulfotransferase: A half-site reactive enzyme
    • Sun, M. and Leyh, T. S. (2010) The human estrogen sulfotransferase: A half-site reactive enzyme Biochemistry 49, 4779-4785
    • (2010) Biochemistry , vol.49 , pp. 4779-4785
    • Sun, M.1    Leyh, T.S.2
  • 27
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr. D62, 859-866
    • (2006) Acta Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D53, 240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0034625464 scopus 로고    scopus 로고
    • Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase
    • Pedersen, L. C., Petrotchenko, E. V., and Negishi, M. (2000) Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase FEBS Lett. 475, 61-64
    • (2000) FEBS Lett. , vol.475 , pp. 61-64
    • Pedersen, L.C.1    Petrotchenko, E.V.2    Negishi, M.3
  • 34
    • 0037124087 scopus 로고    scopus 로고
    • Crystal structure of the human estrogen sulfotransferase-PAPS complex: Evidence for catalytic role of Ser137 in the sulfuryl transfer reaction
    • Pedersen, L. C., Petrotchenko, E., Shevtsov, S., and 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
    • (2002) J. Biol. Chem. , vol.277 , pp. 17928-17932
    • Pedersen, L.C.1    Petrotchenko, E.2    Shevtsov, S.3    Negishi, M.4
  • 35
    • 0001398008 scopus 로고    scopus 로고
    • How Well Does a Restrained Electrostatic Potential (RESP) Model Perform in Calculating Conformational Energies of Organic and Biological Molecules?
    • Wang, J., Cieplak, P., and Kollman, P. (2000) How Well Does a Restrained Electrostatic Potential (RESP) Model Perform in Calculating Conformational Energies of Organic and Biological Molecules? J. Comput. Chem. 21, 1049-1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.3
  • 36
    • 84943200457 scopus 로고
    • A leap-frog algorithm for stochastic dynamics
    • van Gunsteren, W. and Berendsen, H. (1988) A leap-frog algorithm for stochastic dynamics Mol. Simul. 1, 173-185
    • (1988) Mol. Simul. , vol.1 , pp. 173-185
    • Van Gunsteren, W.1    Berendsen, H.2
  • 37
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H., Postma, J., DiNola, A., and Haak, J. (1984) Molecular dynamics with coupling to an external bath J. Chem. Phys. 81, 3684-3690
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.1    Postma, J.2    Dinola, A.3    Haak, J.4
  • 38
    • 0003242622 scopus 로고
    • Transport properties computed by linear response through weak coupling to a bath
    • Kluwer Academic Publishers, New York
    • Berendsen, H. J. C. (1991) Transport properties computed by linear response through weak coupling to a bath. Computer Simulation in Materials Science (Meyer, M. and Pontikis, V., Eds.) pp 139-155, Kluwer Academic Publishers, New York.
    • (1991) Computer Simulation in Materials Science , pp. 139-155
    • Berendsen, H.J.C.1    Meyer, M.2    Pontikis, V.3
  • 44
    • 67349237767 scopus 로고    scopus 로고
    • Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate
    • Teramoto, T., Sakakibara, Y., Liu, M. C., Suiko, M., Kimura, M., and Kakuta, Y. (2009) Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate Biochem. Biophys. Res. Commun. 383, 83-87
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , pp. 83-87
    • Teramoto, T.1    Sakakibara, Y.2    Liu, M.C.3    Suiko, M.4    Kimura, M.5    Kakuta, Y.6
  • 45
    • 0037093546 scopus 로고    scopus 로고
    • Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate
    • Rehse, P. H., Zhou, M., and Lin, S. X. (2002) Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate Biochem. J. 364, 165-171
    • (2002) Biochem. J. , vol.364 , pp. 165-171
    • Rehse, P.H.1    Zhou, M.2    Lin, S.X.3
  • 46
    • 0025230526 scopus 로고
    • Purification and characterization of human liver phenol-sulfating phenol sulfotransferase
    • Falany, C. N., Vazquez, M. E., Heroux, J. A., and Roth, J. A. (1990) Purification and characterization of human liver phenol-sulfating phenol sulfotransferase Arch. Biochem. Biophys. 278, 312-318
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 312-318
    • Falany, C.N.1    Vazquez, M.E.2    Heroux, J.A.3    Roth, J.A.4
  • 47
    • 66149131846 scopus 로고    scopus 로고
    • An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases
    • Weitzner, B., Meehan, T., Xu, Q., and Dunbrack, R. L. (2009) An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases Proteins 75, 289-295
    • (2009) Proteins , vol.75 , pp. 289-295
    • Weitzner, B.1    Meehan, T.2    Xu, Q.3    Dunbrack, R.L.4
  • 49
    • 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
    • Gamage, N. U., Tsvetanov, S., Duggleby, R. G., McManus, M. E., and Martin, J. L. (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
    • (2005) J. Biol. Chem. , vol.280 , pp. 41482-41486
    • Gamage, N.U.1    Tsvetanov, S.2    Duggleby, R.G.3    McManus, M.E.4    Martin, J.L.5
  • 50
    • 1842633460 scopus 로고    scopus 로고
    • Fulvestrant: Pharmacokinetics and pharmacology
    • Robertson, J. F. and Harrison, M. (2004) Fulvestrant: Pharmacokinetics and pharmacology Br. J. Cancer 90 (Suppl. 1) S7-S10
    • (2004) Br. J. Cancer , vol.90 , Issue.SUPPL. 1
    • Robertson, J.F.1    Harrison, M.2
  • 51
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • (Sigman, D. S. Ed.), Academic Press, New York
    • Johnson, K. A. (1992) Transient-state kinetic analysis of enzyme reaction pathways. In The enzymes (Sigman, D. S., Ed.) pp 1-61, Academic Press, New York.
    • (1992) The Enzymes , pp. 1-61
    • Johnson, K.A.1
  • 52
    • 0027076199 scopus 로고
    • The association of age with the activity of alcohol dehydrogenase in human liver
    • Wynne, H. A., Wood, P., Herd, B., Wright, P., Rawlins, M. D., and James, O. F. (1992) The association of age with the activity of alcohol dehydrogenase in human liver Age Ageing 21, 417-420
    • (1992) Age Ageing , vol.21 , pp. 417-420
    • Wynne, H.A.1    Wood, P.2    Herd, B.3    Wright, P.4    Rawlins, M.D.5    James, O.F.6
  • 53
    • 0036794380 scopus 로고    scopus 로고
    • Inhibition of zaleplon metabolism by cimetidine in the human liver: In vitro studies with subcellular fractions and precision-cut liver slices
    • Renwick, A. B., Ball, S. E., Tredger, J. M., Price, R. J., Walters, D. G., Kao, J., Scatina, J. A., and Lake, B. G. (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
    • (2002) Xenobiotica , vol.32 , pp. 849-862
    • Renwick, A.B.1    Ball, S.E.2    Tredger, J.M.3    Price, R.J.4    Walters, D.G.5    Kao, J.6    Scatina, J.A.7    Lake, B.G.8
  • 54
    • 0001244133 scopus 로고
    • A linear method for determining liver sinusoidal and extravascular volumes
    • Goresky, C. A. (1963) A linear method for determining liver sinusoidal and extravascular volumes Am. J. Physiol. 204, 626-640
    • (1963) Am. J. Physiol. , vol.204 , pp. 626-640
    • Goresky, C.A.1
  • 56
    • 0022379968 scopus 로고
    • Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study
    • Okanoue, T., Ohta, M., Ou, O., Kachi, K., Kagawa, K., Yuki, T., Okuno, T., Takino, T., and French, S. W. (1985) Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study Lab. Invest. 53, 534-540
    • (1985) Lab. Invest. , vol.53 , pp. 534-540
    • Okanoue, T.1    Ohta, M.2    Ou, O.3    Kachi, K.4    Kagawa, K.5    Yuki, T.6    Okuno, T.7    Takino, T.8    French, S.W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.