메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

The molecular basis for the broad substrate specificity of human sulfotransferase 1A1

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; ISOLEUCINE; LYSINE; PHENYLALANINE; SULFOTRANSFERASE 1A1; VALINE;

EID: 80055109953     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026794     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 4544226091 scopus 로고    scopus 로고
    • Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility
    • Chapman E, Best MD, Hanson SR, Wong CH, (2004) Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed Engl 43: 3526-3548.
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 3526-3548
    • Chapman, E.1    Best, M.D.2    Hanson, S.R.3    Wong, C.H.4
  • 4
    • 0036165473 scopus 로고    scopus 로고
    • Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis
    • Wang Y, Spitz MR, Tsou AM, Zhang K, Makan N, et al. (2002) Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis. Lung Cancer 35: 137-142.
    • (2002) Lung Cancer , vol.35 , pp. 137-142
    • Wang, Y.1    Spitz, M.R.2    Tsou, A.M.3    Zhang, K.4    Makan, N.5
  • 6
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany CN, (1997) Enzymology of human cytosolic sulfotransferases. Faseb J 11: 206-216.
    • (1997) Faseb J , vol.11 , pp. 206-216
    • Falany, C.N.1
  • 10
    • 0037470234 scopus 로고    scopus 로고
    • Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition
    • Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, et al. (2003) Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem 278: 7655-7662.
    • (2003) J Biol Chem , vol.278 , pp. 7655-7662
    • Gamage, N.U.1    Duggleby, R.G.2    Barnett, A.C.3    Tresillian, M.4    Latham, C.F.5
  • 11
    • 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 NU, Tsvetanov S, Duggleby RG, McManus ME, Martin JL, (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
  • 13
    • 0033621476 scopus 로고    scopus 로고
    • 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
    • Dajani R, Cleasby A, Neu M, Wonacott AJ, Jhoti H, et al. (1999) 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 274: 37862-37868.
    • (1999) J Biol Chem , vol.274 , pp. 37862-37868
    • Dajani, R.1    Cleasby, A.2    Neu, M.3    Wonacott, A.J.4    Jhoti, H.5
  • 14
    • 51249176217 scopus 로고
    • Affinities of organic compounds for solvent water; hydrophilic and hydrophobic character
    • Wolfenden R, (1985) Affinities of organic compounds for solvent water; hydrophilic and hydrophobic character. J Chem Scie 94: 121-138.
    • (1985) J Chem Scie , vol.94 , pp. 121-138
    • Wolfenden, R.1
  • 15
    • 13844250741 scopus 로고    scopus 로고
    • High-throughput screens and selections of enzyme-encoding genes
    • Aharoni A, Griffiths AD, Tawfik DS, (2005) High-throughput screens and selections of enzyme-encoding genes. Curr Opin Chem Biol 9: 210-216.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 210-216
    • Aharoni, A.1    Griffiths, A.D.2    Tawfik, D.S.3
  • 17
    • 0036897839 scopus 로고    scopus 로고
    • Milestones in directed enzyme evolution
    • Tao H, Cornish VW, (2002) Milestones in directed enzyme evolution. Curr Opin Chem Biol 6: 858-864.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 858-864
    • Tao, H.1    Cornish, V.W.2
  • 18
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS, (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19 (5): 596-604.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.5 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 19
    • 44349161622 scopus 로고    scopus 로고
    • Intense neutral drifts yield robust and evolvable consensus proteins
    • Bershtein S, Goldin K, Tawfik DS, (2008) Intense neutral drifts yield robust and evolvable consensus proteins. J Mol Biol 379: 1029-1044.
    • (2008) J Mol Biol , vol.379 , pp. 1029-1044
    • Bershtein, S.1    Goldin, K.2    Tawfik, D.S.3
  • 20
    • 34548014497 scopus 로고    scopus 로고
    • Incorporating Synthetic Oligonucleotides via Gene Reassembly (ISOR): a versatile tool for generating targeted libraries
    • Herman A, Tawfik DS, (2007) Incorporating Synthetic Oligonucleotides via Gene Reassembly (ISOR): a versatile tool for generating targeted libraries. Protein Eng Des Sel 20: 219-226.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 219-226
    • Herman, A.1    Tawfik, D.S.2
  • 21
    • 2442500557 scopus 로고    scopus 로고
    • Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3
    • Barnett AC, Tsvetanov S, Gamage N, Martin JL, Duggleby RG, et al. (2004) Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3. J Biol Chem 279: 18799-18805.
    • (2004) J Biol Chem , vol.279 , pp. 18799-18805
    • Barnett, A.C.1    Tsvetanov, S.2    Gamage, N.3    Martin, J.L.4    Duggleby, R.G.5
  • 22
    • 80051669875 scopus 로고    scopus 로고
    • Directed Evolution of Sulfotransferases and Paraoxonases by Ancestral Libraries
    • Alcolombri U, Elias M, Tawfik DS, (2011) Directed Evolution of Sulfotransferases and Paraoxonases by Ancestral Libraries. J Mol Biol 411 (4): 837-53.
    • (2011) J Mol Biol , vol.411 , Issue.4 , pp. 837-853
    • Alcolombri, U.1    Elias, M.2    Tawfik, D.S.3
  • 23
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang X, Minasov G, Shoichet BK, (2002) Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. J Mol Biol 320: 85-95.
    • (2002) J Mol Biol , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 27
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P, (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62: 72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N, Peitsch MC, (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 34
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures
    • Ho BK, Gruswitz F, (2008) HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct Biol 8: 49.
    • (2008) BMC Struct Biol , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 35
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo M, Williams DM, Brown DM, Gherardi E, (1996) An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues. J Mol Biol 255: 589-603.
    • (1996) J Mol Biol , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.