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Volumn 53, Issue 44, 2014, Pages 6893-6900

3′-Phosphoadenosine 5′-phosphosulfate allosterically regulates sulfotransferase turnover

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; DIMERS; EFFICIENCY; ENZYMES; HISTOLOGY; TISSUE;

EID: 84909636845     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501120p     Document Type: Article
Times cited : (25)

References (28)
  • 1
    • 0035990745 scopus 로고    scopus 로고
    • Regulation of MCF-7 breast cancer cell growth by β-estradiol sulfation
    • Falany, J. L., Macrina, N., and Falany, C. N. (2002) Regulation of MCF-7 breast cancer cell growth by β-estradiol sulfation Breast Cancer Res. Treat. 74, 167-176
    • (2002) Breast Cancer Res. Treat. , vol.74 , pp. 167-176
    • Falany, J.L.1    Macrina, N.2    Falany, C.N.3
  • 2
    • 0029976195 scopus 로고    scopus 로고
    • Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone
    • Falany, J. L. and Falany, C. N. (1996) Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone Endocrinology 137, 1395-1401
    • (1996) Endocrinology , vol.137 , pp. 1395-1401
    • Falany, J.L.1    Falany, C.N.2
  • 4
    • 33846005168 scopus 로고    scopus 로고
    • Elevated hepatic SULT1E1 activity in mouse models of cystic fibrosis alters the regulation of estrogen responsive proteins
    • Li, L. and Falany, C. N. (2007) Elevated hepatic SULT1E1 activity in mouse models of cystic fibrosis alters the regulation of estrogen responsive proteins J. Cystic Fibrosis 6, 23-30
    • (2007) J. Cystic Fibrosis , vol.6 , pp. 23-30
    • Li, L.1    Falany, C.N.2
  • 5
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine O-sulfation
    • Moore, K. L. (2003) The biology and enzymology of protein tyrosine O-sulfation J. Biol. Chem. 278, 24243-24246
    • (2003) J. Biol. Chem. , vol.278 , pp. 24243-24246
    • Moore, K.L.1
  • 6
    • 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
  • 7
    • 0027757048 scopus 로고
    • The physical biochemistry and molecular genetics of sulfate activation
    • Leyh, T. S. (1993) The physical biochemistry and molecular genetics of sulfate activation Crit. Rev. Biochem. Mol. Biol. 28, 515-542
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 515-542
    • Leyh, T.S.1
  • 8
    • 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
  • 9
    • 0028240253 scopus 로고
    • Role of sulfation in thyroid hormone metabolism
    • Visser, T. J. (1994) Role of sulfation in thyroid hormone metabolism Chem.-Biol. Interact. 92, 293-303
    • (1994) Chem.-Biol. Interact. , vol.92 , pp. 293-303
    • Visser, T.J.1
  • 10
    • 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 , pp. 7-S10
    • Robertson, J.F.1    Harrison, M.2
  • 11
    • 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
  • 12
    • 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, 5674-5683
    • (2012) Biochemistry , vol.51 , pp. 5674-5683
    • Cook, I.1    Wang, T.2    Falany, C.N.3    Leyh, T.S.4
  • 13
    • 84887359121 scopus 로고    scopus 로고
    • Structure, dynamics and selectivity in the sulfotransferase family
    • Leyh, T. S., Cook, I., and Wang, T. (2013) Structure, dynamics and selectivity in the sulfotransferase family Drug Metab. Rev. 45, 423-430
    • (2013) Drug Metab. Rev. , vol.45 , pp. 423-430
    • Leyh, T.S.1    Cook, I.2    Wang, T.3
  • 15
    • 84889037440 scopus 로고    scopus 로고
    • High Accuracy In-Silico Sulfotransferase Models
    • Cook, I., Wang, T., Falany, C. N., and Leyh, T. S. (2013) High Accuracy In-Silico Sulfotransferase Models J. Biol. Chem. 288, 34494-34501
    • (2013) J. Biol. Chem. , vol.288 , pp. 34494-34501
    • Cook, I.1    Wang, T.2    Falany, C.N.3    Leyh, T.S.4
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • In (Sigman, D. S. Ed.) pp, Academic Press, New York.
    • Johnson, K. (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.1
  • 19
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data Methods Enzymol. 63, 103-138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 21
    • 84907200601 scopus 로고    scopus 로고
    • Paradigms of Sulfotransferase Catalysis: The Mechanism of SULT2A1
    • Wang, T., Cook, I., Falany, C. N., and Leyh, T. S. (2014) Paradigms of Sulfotransferase Catalysis: The Mechanism of SULT2A1 J. Biol. Chem. 289, 26474-26480
    • (2014) J. Biol. Chem. , vol.289 , pp. 26474-26480
    • Wang, T.1    Cook, I.2    Falany, C.N.3    Leyh, T.S.4
  • 22
    • 55849116013 scopus 로고    scopus 로고
    • Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase
    • Tyapochkin, E., Cook, P. F., and Chen, G. (2008) Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase Biochemistry 47, 11894-11899
    • (2008) Biochemistry , vol.47 , pp. 11894-11899
    • Tyapochkin, E.1    Cook, P.F.2    Chen, G.3
  • 23
    • 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
  • 24
    • 0023110646 scopus 로고
    • Comparison of adenosine 3′-phosphate 5′-phosphosulfate concentrations in tissues from different laboratory animals
    • Brzeznicka, E. A., Hazelton, G. A., and Klaassen, C. D. (1987) Comparison of adenosine 3′-phosphate 5′-phosphosulfate concentrations in tissues from different laboratory animals Drug Metab. Dispos. 15, 133-135
    • (1987) Drug Metab. Dispos. , vol.15 , pp. 133-135
    • Brzeznicka, E.A.1    Hazelton, G.A.2    Klaassen, C.D.3
  • 25
    • 0024447657 scopus 로고
    • Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3′-phosphate 5′-phosphosulphate in human tissues
    • Cappiello, M., Franchi, M., Giuliani, L., and Pacifici, G. M. (1989) Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3′-phosphate 5′-phosphosulphate in human tissues Eur. J. Clin. Pharmacol. 37, 317-320
    • (1989) Eur. J. Clin. Pharmacol. , vol.37 , pp. 317-320
    • Cappiello, M.1    Franchi, M.2    Giuliani, L.3    Pacifici, G.M.4
  • 26
    • 0023897466 scopus 로고
    • Sulfotransferase in humans: Development and tissue distribution
    • Pacifici, G. M., Franchi, M., Colizzi, C., Giuliani, L., and Rane, A. (1988) Sulfotransferase in humans: Development and tissue distribution Pharmacology 36, 411-419
    • (1988) Pharmacology , vol.36 , pp. 411-419
    • Pacifici, G.M.1    Franchi, M.2    Colizzi, C.3    Giuliani, L.4    Rane, A.5
  • 27
    • 0032545405 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene
    • Sakakibara, Y., Yanagisawa, K., Katafuchi, J., Ringer, D. P., Takami, Y., Nakayama, T., Suiko, M., and Liu, M. C. (1998) Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene J. Biol. Chem. 273, 33929-33935
    • (1998) J. Biol. Chem. , vol.273 , pp. 33929-33935
    • Sakakibara, Y.1    Yanagisawa, K.2    Katafuchi, J.3    Ringer, D.P.4    Takami, Y.5    Nakayama, T.6    Suiko, M.7    Liu, M.C.8
  • 28
    • 77958476945 scopus 로고    scopus 로고
    • A Comprehensive Tissue Properties Database Provided for the Thermal Assessment of a Human at Rest
    • McIntosh, R. L. and Anderson, V. (2010) A Comprehensive Tissue Properties Database Provided for the Thermal Assessment of a Human at Rest Biophys. Rev. Lett. 5, 129
    • (2010) Biophys. Rev. Lett. , vol.5 , pp. 129
    • McIntosh, R.L.1    Anderson, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.