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Volumn 273, Issue 1, 2006, Pages 159-169

The natural mutation by deletion of Lys9 in the thrombin A-chain affects the pKa value of catalytic residues, the overall enzyme's stability and conformational transitions linked to Na+ binding

Author keywords

Allostery; Molecular dynamics; pKa values; Stability; Thrombin

Indexed keywords

LYSINE; SODIUM; THROMBIN; UREA;

EID: 33644876813     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05052.x     Document Type: Article
Times cited : (27)

References (22)
  • 2
    • 1842529273 scopus 로고    scopus 로고
    • A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin
    • De Cristofaro R Akhavan S Altomare C Carotti A Peyvandi F Mannucci PM 2004 A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin J Biol Chem 279 13035 13043
    • (2004) J Biol Chem , vol.279 , pp. 13035-13043
    • De Cristofaro, R.1    Akhavan, S.2    Altomare, C.3    Carotti, A.4    Peyvandi, F.5    Mannucci, P.M.6
  • 3
    • 0025887321 scopus 로고
    • Linkage between proton binding and amidase activity in human α-thrombin: Effect of ions and temperature
    • Di Cera E De Cristofaro R Albright DJ Fenton JW II. 1991 Linkage between proton binding and amidase activity in human α-thrombin: effect of ions and temperature Biochemistry 30 7913 7924
    • (1991) Biochemistry , vol.30 , pp. 7913-7924
    • Di Cera, E.1    De Cristofaro, R.2    Albright, D.J.3    Fenton, I.I.J.W.4
  • 4
    • 0025646461 scopus 로고
    • Effect of protons on the amidase activity of human α-thrombin. Analysis in terms of a general linkage scheme
    • De Cristofaro R Di Cera E 1990 Effect of protons on the amidase activity of human α-thrombin. Analysis in terms of a general linkage scheme J Mol Biol 216 1077 1086
    • (1990) J Mol Biol , vol.216 , pp. 1077-1086
    • De Cristofaro, R.1    Di Cera, E.2
  • 5
    • 0026005785 scopus 로고
    • Mechanistic studies on thrombin catalysis
    • Stone SR Betz A Hofsteenge J 1991 Mechanistic studies on thrombin catalysis Biochemistry 30 9841 9848
    • (1991) Biochemistry , vol.30 , pp. 9841-9848
    • Stone, S.R.1    Betz, A.2    Hofsteenge, J.3
  • 6
    • 2442461173 scopus 로고    scopus 로고
    • Proton inventory studies of alpha-thrombin-catalyzed reactions of substrates with selected P and P' sites
    • Enyedy EJ Kovach IM 2004 Proton inventory studies of alpha-thrombin- catalyzed reactions of substrates with selected P and P' sites J Am Chem Soc 126 6017 6024
    • (2004) J Am Chem Soc , vol.126 , pp. 6017-6024
    • Enyedy, E.J.1    Kovach, I.M.2
  • 8
    • 0028292789 scopus 로고
    • Thermodynamics of substrates and reversible inhibitors binding to the active site cleft of human alpha-thrombin
    • De Cristofaro R Landolfi R 1994 Thermodynamics of substrates and reversible inhibitors binding to the active site cleft of human alpha-thrombin J Mol Biol 239 569 577
    • (1994) J Mol Biol , vol.239 , pp. 569-577
    • De Cristofaro, R.1    Landolfi, R.2
  • 10
    • 0037387204 scopus 로고    scopus 로고
    • The molecular basis of thrombin allostery revealed by a 1.8 Å structure of the 'slow' form
    • Huntington JA Esmon CT 2003 The molecular basis of thrombin allostery revealed by a 1.8 Å structure of the 'slow' form Structure 11 469 479
    • (2003) Structure , vol.11 , pp. 469-479
    • Huntington, J.A.1    Esmon, C.T.2
  • 14
    • 0034636749 scopus 로고    scopus 로고
    • Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C
    • Arosio D Ayala YM Di Cera E 2000 Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C Biochemistry 39 8095 8101
    • (2000) Biochemistry , vol.39 , pp. 8095-8101
    • Arosio, D.1    Ayala, Y.M.2    Di Cera, E.3
  • 15
    • 25144446242 scopus 로고    scopus 로고
    • + binding on the conformation, stability and molecular recognition properties of thrombin
    • + binding on the conformation, stability and molecular recognition properties of thrombin Biochem J 390 485 492
    • (2005) Biochem J , vol.390 , pp. 485-492
    • De Filippis, V.1    De Dea, E.2    Lucatello, F.3    Frasson, R.4
  • 16
    • 1242296243 scopus 로고    scopus 로고
    • Structural stability of α-thrombin studied by disulfide reduction and scrambling
    • Singh RR Chang J-Y 2003 Structural stability of α-thrombin studied by disulfide reduction and scrambling Biochim Biophys Acta 1651 85 92
    • (2003) Biochim Biophys Acta , vol.1651 , pp. 85-92
    • Singh, R.R.1    Chang, J.-Y.2
  • 17
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of
    • d-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W Turk D Karshikov A 1992 The refined 1.9-Å X-ray crystal structure of d -Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships Protein Sci 1 426 471
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 18
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis KJ Morrison JF 1982 Buffers of constant ionic strength for studying pH-dependent processes Methods Enzymol 87 405 426
    • (1982) Methods Enzymol , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 19
    • 0016405364 scopus 로고
    • The mechanism of the aminolysis of acetate esters
    • Satterthwait AC Jencks WP 1974 The mechanism of the aminolysis of acetate esters J Am Chem Soc 96 7018 7031
    • (1974) J Am Chem Soc , vol.96 , pp. 7018-7031
    • Satterthwait, A.C.1    Jencks, W.P.2
  • 20
    • 0016207947 scopus 로고
    • Acylation of alpha-chymotrypsin by oxygen and sulfur esters of specific substrates: Kinetic evidence for a tetrahedral intermediate
    • Hiroara H Bender ML Stark RS 1974 Acylation of alpha-chymotrypsin by oxygen and sulfur esters of specific substrates: kinetic evidence for a tetrahedral intermediate Proc Natl Acad Sci USA 71 1643 1647
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1643-1647
    • Hiroara, H.1    Bender, M.L.2    Stark, R.S.3
  • 22
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E Hess B van der Spoel D 2001 Gromacs 3.0: a package for molecular simulation and trajectory analysis J Mol Mod 7 306 317
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.