메뉴 건너뛰기




Volumn 581, Issue 18, 2007, Pages 3449-3454

Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method

Author keywords

Angiotensin I converting enzyme; Binding constants; Inhibitors; Isothermal titration calorimetry

Indexed keywords

CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENALAPRILAT; LISINOPRIL;

EID: 34447283577     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.06.048     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 0038163054 scopus 로고
    • The preparation and function of the hypertensin-converting enzyme
    • Skeggs L.T., Kahn J.R., and Shumway N.P. The preparation and function of the hypertensin-converting enzyme. J. Exp. Med. 103 (1956) 295-299
    • (1956) J. Exp. Med. , vol.103 , pp. 295-299
    • Skeggs, L.T.1    Kahn, J.R.2    Shumway, N.P.3
  • 2
    • 0037699010 scopus 로고    scopus 로고
    • The discovery of captopril
    • Smith C.G., and Vane J.R. The discovery of captopril. FASEB J. 17 (2003) 788-789
    • (2003) FASEB J. , vol.17 , pp. 788-789
    • Smith, C.G.1    Vane, J.R.2
  • 3
    • 0021780973 scopus 로고
    • The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin-converting enzyme
    • Patchett A.A., and Cordes E.H. The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin-converting enzyme. Adv. Enzymol. Relat. Areas Mol. Biol. 57 (1985) 1-84
    • (1985) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.57 , pp. 1-84
    • Patchett, A.A.1    Cordes, E.H.2
  • 4
    • 0032828165 scopus 로고    scopus 로고
    • Design of angiotensin converting enzyme inhibitors
    • Cushman D.W., and Ondetti M.A. Design of angiotensin converting enzyme inhibitors. Nat. Med. 5 (1999) 1110-1113
    • (1999) Nat. Med. , vol.5 , pp. 1110-1113
    • Cushman, D.W.1    Ondetti, M.A.2
  • 6
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • Natesh R., Schwager S.L., Sturrock E.D., and Acharya K.R. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421 (2003) 551-554
    • (2003) Nature , vol.421 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.2    Sturrock, E.D.3    Acharya, K.R.4
  • 7
    • 3042732126 scopus 로고    scopus 로고
    • Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme
    • Natesh R., Schwager S.L., Evans H.R., Sturrock E.D., and Acharya K.R. Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry 43 (2004) 8718-8724
    • (2004) Biochemistry , vol.43 , pp. 8718-8724
    • Natesh, R.1    Schwager, S.L.2    Evans, H.R.3    Sturrock, E.D.4    Acharya, K.R.5
  • 8
    • 33644945546 scopus 로고    scopus 로고
    • Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design
    • Corradi H.R., Schwager S.L., Nchinda A.T., Sturrock E.D., and Acharya K.R. Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. J. Mol. Biol. 357 (2006) 964-974
    • (2006) J. Mol. Biol. , vol.357 , pp. 964-974
    • Corradi, H.R.1    Schwager, S.L.2    Nchinda, A.T.3    Sturrock, E.D.4    Acharya, K.R.5
  • 9
    • 4644361124 scopus 로고    scopus 로고
    • A calorimetric study of the binding of lisinopril, enalaprilat and captopril to angiotensin-converting enzyme
    • Andujar-Sanchez M., Camara-Artigas A., and Jara-Perez V. A calorimetric study of the binding of lisinopril, enalaprilat and captopril to angiotensin-converting enzyme. Biophys. Chem. 111 (2004) 183-189
    • (2004) Biophys. Chem. , vol.111 , pp. 183-189
    • Andujar-Sanchez, M.1    Camara-Artigas, A.2    Jara-Perez, V.3
  • 10
    • 0142102525 scopus 로고    scopus 로고
    • Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme
    • Binevski P.V., Sizova E.A., Pozdnev V.F., and Kost O.A. Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme. FEBS Lett. 550 (2003) 84-88
    • (2003) FEBS Lett. , vol.550 , pp. 84-88
    • Binevski, P.V.1    Sizova, E.A.2    Pozdnev, V.F.3    Kost, O.A.4
  • 11
    • 0242569193 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence
    • Guy J.L., Jackson R.M., Acharya K.R., Sturrock E.D., Hooper N.M., and Turner A.J. Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence. Biochemistry 42 (2003) 13185-13192
    • (2003) Biochemistry , vol.42 , pp. 13185-13192
    • Guy, J.L.1    Jackson, R.M.2    Acharya, K.R.3    Sturrock, E.D.4    Hooper, N.M.5    Turner, A.J.6
  • 12
    • 22544481731 scopus 로고    scopus 로고
    • Identification of critical active-site residues in angiotensin-converting enzyme-2 (ACE2) by site-directed mutagenesis
    • Guy J.L., Jackson R.M., Jensen H.A., Hooper N.M., and Turner A.J. Identification of critical active-site residues in angiotensin-converting enzyme-2 (ACE2) by site-directed mutagenesis. FEBS J. 272 (2005) 3512-3520
    • (2005) FEBS J. , vol.272 , pp. 3512-3520
    • Guy, J.L.1    Jackson, R.M.2    Jensen, H.A.3    Hooper, N.M.4    Turner, A.J.5
  • 13
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S., and Freire E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11 (2001) 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 14
    • 14744271960 scopus 로고    scopus 로고
    • ITC in the post-genomic era...? Priceless
    • Velazquez Campoy A., and Freire E. ITC in the post-genomic era...? Priceless. Biophys. Chem. 115 (2005) 115-124
    • (2005) Biophys. Chem. , vol.115 , pp. 115-124
    • Velazquez Campoy, A.1    Freire, E.2
  • 15
    • 0026643458 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
    • Wei L., Clauser E., Alhenc-Gelas F., and Corvol P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267 (1992) 13398-13405
    • (1992) J. Biol. Chem. , vol.267 , pp. 13398-13405
    • Wei, L.1    Clauser, E.2    Alhenc-Gelas, F.3    Corvol, P.4
  • 16
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J.F., and Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179 (1989) 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 17
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • Sigurskjold B.W. Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal. Biochem. 277 (2000) 260-266
    • (2000) Anal. Biochem. , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 20
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., and Record Jr. M.T. Coupling of local folding to site-specific binding of proteins to DNA. Science 263 (1994) 777-784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 22
    • 0021834953 scopus 로고
    • A metabolite of aspartame inhibits angiotensin converting enzyme
    • Grobelny D., and Galardy R.E. A metabolite of aspartame inhibits angiotensin converting enzyme. Biochem. Biophys. Res. Commun. 128 (1985) 960-964
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 960-964
    • Grobelny, D.1    Galardy, R.E.2
  • 23
    • 0020434523 scopus 로고
    • Inhibition of angiotensin converting enzyme by phosphoramidates and polyphosphates
    • Galardy R.E. Inhibition of angiotensin converting enzyme by phosphoramidates and polyphosphates. Biochemistry 21 (1982) 5777-5781
    • (1982) Biochemistry , vol.21 , pp. 5777-5781
    • Galardy, R.E.1
  • 24
    • 0029395478 scopus 로고
    • Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz J.D. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2 (1995) 709-712
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 25
    • 27744603304 scopus 로고    scopus 로고
    • Kinetic probes for inter-domain co-operation in human somatic angiotensin-converting enzyme
    • Skirgello O.E., Binevski P.V., Pozdnev V.F., and Kost O.A. Kinetic probes for inter-domain co-operation in human somatic angiotensin-converting enzyme. Biochem. J. 391 (2005) 641-647
    • (2005) Biochem. J. , vol.391 , pp. 641-647
    • Skirgello, O.E.1    Binevski, P.V.2    Pozdnev, V.F.3    Kost, O.A.4
  • 26
    • 0025739667 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
    • Wei L., Alhenc-Gelas F., Corvol P., and Clauser E. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266 (1991) 9002-9008
    • (1991) J. Biol. Chem. , vol.266 , pp. 9002-9008
    • Wei, L.1    Alhenc-Gelas, F.2    Corvol, P.3    Clauser, E.4
  • 27
    • 0027175193 scopus 로고
    • Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides
    • Jaspard E., Wei L., and Alhenc-Gelas F. Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268 (1993) 9496-9503
    • (1993) J. Biol. Chem. , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 28
    • 0037076516 scopus 로고    scopus 로고
    • Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides
    • Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D., De Camargo A.C., and Dive V. Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry 41 (2002) 6065-6071
    • (2002) Biochemistry , vol.41 , pp. 6065-6071
    • Cotton, J.1    Hayashi, M.A.2    Cuniasse, P.3    Vazeux, G.4    Ianzer, D.5    De Camargo, A.C.6    Dive, V.7
  • 29
    • 0023657755 scopus 로고
    • Sulfate potentiation of the chloride activation of angiotensin converting enzyme
    • Bunning P., and Riordan J.F. Sulfate potentiation of the chloride activation of angiotensin converting enzyme. Biochemistry 26 (1987) 3374-3377
    • (1987) Biochemistry , vol.26 , pp. 3374-3377
    • Bunning, P.1    Riordan, J.F.2
  • 30
    • 0037032612 scopus 로고    scopus 로고
    • a values of pharmaceuticals by pressure-assisted capillary electrophoresis combined with short-end injection
    • a values of pharmaceuticals by pressure-assisted capillary electrophoresis combined with short-end injection. J. Chromatogr. A 979 (2002) 369-377
    • (2002) J. Chromatogr. A , vol.979 , pp. 369-377
    • Wan, H.1    Holmen, A.2    Nagard, M.3    Lindberg, W.4
  • 31
    • 2342418543 scopus 로고    scopus 로고
    • ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis
    • Towler P., et al. ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J. Biol. Chem. 279 (2004) 17996-18007
    • (2004) J. Biol. Chem. , vol.279 , pp. 17996-18007
    • Towler, P.1
  • 33
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar R.S., Livingstone J.R., and Record Jr. M.T. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31 (1992) 3947-3955
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record Jr., M.T.3
  • 34
    • 0025788169 scopus 로고
    • Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
    • Ehlers M.R., and Riordan J.F. Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry 30 (1991) 7118-7126
    • (1991) Biochemistry , vol.30 , pp. 7118-7126
    • Ehlers, M.R.1    Riordan, J.F.2
  • 35
    • 23644435174 scopus 로고    scopus 로고
    • The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity
    • Woodman Z.L., Schwager S.L., Redelinghuys P., Carmona A.K., Ehlers M.R., and Sturrock E.D. The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity. Biochem. J. 389 (2005) 739-744
    • (2005) Biochem. J. , vol.389 , pp. 739-744
    • Woodman, Z.L.1    Schwager, S.L.2    Redelinghuys, P.3    Carmona, A.K.4    Ehlers, M.R.5    Sturrock, E.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.