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Volumn 391, Issue 3, 2005, Pages 641-647

Kinetic probes for inter-domain co-operation in human somatic angiotensin-converting enzyme

Author keywords

Active site titration; Angiotensin converting enzyme; Negative co operativity; Simultaneous hydrolysis of two substrates

Indexed keywords

ENZYMES; HYDROLYSIS; SUBSTRATES;

EID: 27744603304     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050702     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0029041265 scopus 로고
    • Peptidyl dipeptidase A: Angiotensin I-converting enzyme
    • Corvol, P., Williams, T. A. and Soubrier, F. (1995) Peptidyl dipeptidase A: angiotensin I-converting enzyme. Methods Enzymol. 248, 283-305
    • (1995) Methods Enzymol , vol.248 , pp. 283-305
    • Corvol, P.1    Williams, T.A.2    Soubrier, F.3
  • 3
    • 0042908657 scopus 로고
    • Molecular cloning of human testicular angiotensin-converting enzyme: The testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme
    • Ehlers, M. R. W., Fox, E. A., Strydom, D. J. and Riordan, J. F. (1989) Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin- converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 86, 7741-7745
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7741-7745
    • Ehlers, M.R.W.1    Fox, E.A.2    Strydom, D.J.3    Riordan, J.F.4
  • 4
    • 0022005455 scopus 로고
    • Angiotensin-converting enzyme in the testis and epididymis: Differential development and pituitary regulation of isozymes
    • Strittmatter, S. M., Thiele, E. A., De Souza, E. B. and Snyder, S. H. (1985) Angiotensin-converting enzyme in the testis and epididymis: differential development and pituitary regulation of isozymes. Endocrinology (Baltimore) 117, 1374-1379
    • (1985) Endocrinology (Baltimore) , vol.117 , pp. 1374-1379
    • Strittmatter, S.M.1    Thiele, E.A.2    De Souza, E.B.3    Snyder, S.H.4
  • 7
    • 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. (1993) 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, 9496-9503
    • (1993) J. Biol. Chem. , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 8
    • 0028967315 scopus 로고
    • The nemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme
    • Rousseau, A., Michaud, A., Chauvet, M. T., Lenfant, M. and Corvol, P. (1995) The nemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J. Biol. Chem. 270, 3656-3661
    • (1995) J. Biol. Chem. , vol.270 , pp. 3656-3661
    • Rousseau, A.1    Michaud, A.2    Chauvet, M.T.3    Lenfant, M.4    Corvol, P.5
  • 9
    • 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. (1991) The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266, 9002-9008
    • (1991) J. Biol. Chem. , vol.266 , pp. 9002-9008
    • Wei, L.1    Alhenc-Gelas, F.2    Corvol, P.3    Clauser, E.4
  • 10
    • 0042490795 scopus 로고    scopus 로고
    • Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: Insights from selective inhibitors
    • Georgiadis, D., Beau, F., Czarny, B., Cotton, J., Yiotakis, A. and Dive, V. (2003) Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: insights from selective inhibitors. Circ. Res. 93, 148-154
    • (2003) Circ. Res. , vol.93 , pp. 148-154
    • Georgiadis, D.1    Beau, F.2    Czarny, B.3    Cotton, J.4    Yiotakis, A.5    Dive, V.6
  • 11
    • 0027051423 scopus 로고
    • Two binding sites on angiotensin-converting enzyme: Evidence from radioligand binding studies
    • Perich, R. B., Jackson, B., Rogerson, F., Mendelsohn, F. A., Paxton, D. and Johnston, C. I. (1992) Two binding sites on angiotensin-converting enzyme: evidence from radioligand binding studies. Mol. Pharmacol. 42, 286-293
    • (1992) Mol. Pharmacol. , vol.42 , pp. 286-293
    • Perich, R.B.1    Jackson, B.2    Rogerson, F.3    Mendelsohn, F.A.4    Paxton, D.5    Johnston, C.I.6
  • 12
    • 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. (1992) The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267, 13398-13405
    • (1992) J. Biol. Chem. , vol.267 , pp. 13398-13405
    • Wei, L.1    Clauser, E.2    Alhenc-Gelas, F.3    Corvol, P.4
  • 14
    • 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. (2002) Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry 41, 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
  • 15
    • 0034713884 scopus 로고    scopus 로고
    • Peptidase specificity characterization of C- And N-terminal catalytic sites of angiotensin I-converting enzyme
    • Araujo, M. C., Melo, R. L., Cesari, M. H., Juliano, M. A., Juliano, L and Carmona, A. K. (2000) Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry, 39, 8519-8525
    • (2000) Biochemistry , vol.39 , pp. 8519-8525
    • Araujo, M.C.1    Melo, R.L.2    Cesari, M.H.3    Juliano, M.A.4    Juliano, L.5    Carmona, A.K.6
  • 16
    • 0025788169 scopus 로고
    • Angiotensin-converting enzyme: Zinc- And inhibitor-binding stoichiometries of the somatic and testis isozymes
    • Ehlers, M. R. and Riordan, J. F. (1991) Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry 30, 7118-7126
    • (1991) Biochemistry , vol.30 , pp. 7118-7126
    • Ehlers, M.R.1    Riordan, J.F.2
  • 17
    • 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. (2003) Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme. FEBS Lett. 550, 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
  • 18
    • 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. (2004) A calorimetric study of the binding of lisinopril, enalaprilat and captopril to angiotensin-converting enzyme. Biophys. Chem. 111, 183-189
    • (2004) Biophys. Chem. , vol.111 , pp. 183-189
    • Andujar-Sanchez, M.1    Camara-Artigas, A.2    Jara-Perez, V.3
  • 19
    • 23644435174 scopus 로고    scopus 로고
    • The N domain of somatic angiotensin-converting enzyme negatively egulates ectodomain shedding and catalytic activity
    • Woodman, Z. L., Schwager, S. L. U., Redelinghuys, P., Carmona, A. K., Ehlers, M. R. W. and Sturrock, E. D. (2005) The N domain of somatic angiotensin-converting enzyme negatively egulates ectodomain shedding and catalytic activity. Biochem. J. 389, 739-744
    • (2005) Biochem. J. , vol.389 , pp. 739-744
    • Woodman, Z.L.1    Schwager, S.L.U.2    Redelinghuys, P.3    Carmona, A.K.4    Ehlers, M.R.W.5    Sturrock, E.D.6
  • 20
    • 6344246036 scopus 로고    scopus 로고
    • Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism
    • Rice, G. I., Thomas, D. A., Grant, P. J., Turner, A. J. and Hooper, N. M. (2004) Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem. J. 383, 45-51
    • (2004) Biochem. J. , vol.383 , pp. 45-51
    • Rice, G.I.1    Thomas, D.A.2    Grant, P.J.3    Turner, A.J.4    Hooper, N.M.5
  • 21
    • 0041878299 scopus 로고
    • Synthesis of N-furylacryloyl derivatives of aminoacids and peptides - Chromogenic substrates of proteolytic enzymes - with the use of anhydride of furylacrylic acid
    • Pozdnev, V. F. (1986) Synthesis of N-furylacryloyl derivatives of aminoacids and peptides - chromogenic substrates of proteolytic enzymes - with the use of anhydride of furylacrylic acid. Zh. Obshch. Khim. 56, 690-695
    • (1986) Zh. Obshch. Khim. , vol.56 , pp. 690-695
    • Pozdnev, V.F.1
  • 22
    • 0033173853 scopus 로고    scopus 로고
    • Inhibitor analysis of angiotensin I-converting and kinin-degrading activities of bovine lung and testicular angiotensin-converting enzyme
    • Grinshtein, S. V., Binevski, P. V., Gomazkov, O. A., Pozdnev, V. F., Nikolskaya, I. I. and Kost, O. A. (1999) Inhibitor analysis of angiotensin I-converting and kinin-degrading activities of bovine lung and testicular angiotensin-converting enzyme. Biokhimiya (Moscow) 64, 938-944
    • (1999) Biokhimiya (Moscow) , vol.64 , pp. 938-944
    • Grinshtein, S.V.1    Binevski, P.V.2    Gomazkov, O.A.3    Pozdnev, V.F.4    Nikolskaya, I.I.5    Kost, O.A.6
  • 24
    • 0033666862 scopus 로고    scopus 로고
    • New feature of angiotensin-converting enzyme: Carbohydrate-recognizing domain
    • Kost, O. A., Bovin, N. V., Chemodanova, E. E., Nasonov, V. V. and Ort, T. A. (2000) New feature of angiotensin-converting enzyme: carbohydrate- recognizing domain. J. Mol. Recog. 13, 360-369
    • (2000) J. Mol. Recog. , vol.13 , pp. 360-369
    • Kost, O.A.1    Bovin, N.V.2    Chemodanova, E.E.3    Nasonov, V.V.4    Ort, T.A.5
  • 25
    • 0034203481 scopus 로고    scopus 로고
    • Isolation and characterization of the N-domain of bovine angiotensin-converting enzyme
    • Binevski, P. V., Nikolskaya, I. I., Pozdnev, V. F. and Kost, O. A. (2000) Isolation and characterization of the N-domain of bovine angiotensin-converting enzyme. Biokhimiya (Moscow) 65, 651-658
    • (2000) Biokhimiya (Moscow) , vol.65 , pp. 651-658
    • Binevski, P.V.1    Nikolskaya, I.I.2    Pozdnev, V.F.3    Kost, O.A.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0024851560 scopus 로고
    • A procedure for eliminating interferences in the Lowry method of protein determination
    • Rodriguez-Vico, F. (1989) A procedure for eliminating interferences in the Lowry method of protein determination. Anal. Biochem. 183, 275-278
    • (1989) Anal. Biochem. , vol.183 , pp. 275-278
    • Rodriguez-Vico, F.1
  • 29
    • 0001169698 scopus 로고
    • Some kinetic consequences of the tight binding of protein-proteinase- inhibitors to proteolytic enzymes and their application to the determination of dissociation constants
    • (Fritz, H., Tschesche, H. and Greene, L. J., eds.), Springer-Verlag, Berlin, Heidelberg, New York
    • Bieth, J. (1974) Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In Proteinase-Inhibitors: Bayer-Symposium V (Fritz, H., Tschesche, H. and Greene, L. J., eds.), pp. 463-469, Springer-Verlag, Berlin, Heidelberg, New York
    • (1974) Proteinase-Inhibitors: Bayer-Symposium V , pp. 463-469
    • Bieth, J.1
  • 30
    • 0018398672 scopus 로고
    • A continuous spectrophotometric assay for angiotensin converting enzyme
    • Holmquist, B., Bünning, P. and Riordan, J. F. (1979) A continuous spectrophotometric assay for angiotensin converting enzyme. Anal. Biochem. 95, 540-548
    • (1979) Anal. Biochem. , vol.95 , pp. 540-548
    • Holmquist, B.1    Bünning, P.2    Riordan, J.F.3
  • 31
    • 0014958429 scopus 로고
    • Studies on the angiotensin converting enzyme with different substrates
    • Piquilloud, Y., Reinharz, A. and Roth, M. (1970) Studies on the angiotensin converting enzyme with different substrates. Biochim. Biophys. Acta 206, 136-142
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 136-142
    • Piquilloud, Y.1    Reinharz, A.2    Roth, M.3
  • 34
    • 0030981239 scopus 로고    scopus 로고
    • Substrate dependence of angiotensin I-converting enzyme inhibition: Captopril displays a partial selectivity for inhibition of N-acetyl-seryl- aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I
    • Michaud, A., Williams, T. A., Chauvet, M.-T. and Corvol, P. (1997) Substrate dependence of angiotensin I-converting enzyme inhibition: captopril displays a partial selectivity for inhibition of N-acetyl-seryl-aspartyl-lysyl- proline hydrolysis compared with that of angiotensin I. Mol. Pharmacol. 51, 1070-1076
    • (1997) Mol. Pharmacol. , vol.51 , pp. 1070-1076
    • Michaud, A.1    Williams, T.A.2    Chauvet, M.-T.3    Corvol, P.4
  • 35
    • 0030029914 scopus 로고    scopus 로고
    • A study of chimerads constructed with the two domains of angiotensin I-converting enzyme
    • Williams, T. A., Danilov, S., Alhenc-Gelas, F. and Soubrier, F. (1996) A study of chimerads constructed with the two domains of angiotensin I-converting enzyme. Biochem. Pharmacol. 51, 11-14
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 11-14
    • Williams, T.A.1    Danilov, S.2    Alhenc-Gelas, F.3    Soubrier, F.4
  • 36
    • 0028029798 scopus 로고
    • Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies
    • Danilov, S., Jaspard, E., Churakova, T., Towbin, H., Savoie, F., Wei, L. and Alhen-Gelas, F. (1994) Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies. J. Biol. Chem. 269, 26806-26814
    • (1994) J. Biol. Chem. , vol.269 , pp. 26806-26814
    • Danilov, S.1    Jaspard, E.2    Churakova, T.3    Towbin, H.4    Savoie, F.5    Wei, L.6    Alhen-Gelas, F.7
  • 37
    • 0017605510 scopus 로고
    • Angiotensin I converting enzyme from human plasma
    • Lanzillo, J. J. and Fanburg, B. L. (1977) Angiotensin I converting enzyme from human plasma. Biochemistry 16, 5491-5495
    • (1977) Biochemistry , vol.16 , pp. 5491-5495
    • Lanzillo, J.J.1    Fanburg, B.L.2
  • 39
    • 0035384673 scopus 로고    scopus 로고
    • Fluorescence polarization studies of different forms of angiotensin-converting enzyme
    • Voronov, S. V., Binevski, P. V., Eremin, S. A. and Kost, O. A. (2001) Fluorescence polarization studies of different forms of angiotensin-converting enzyme. Biokhimiya (Moscow) 66, 788-794
    • (2001) Biokhimiya (Moscow) , vol.66 , pp. 788-794
    • Voronov, S.V.1    Binevski, P.V.2    Eremin, S.A.3    Kost, O.A.4
  • 40
    • 0014501356 scopus 로고
    • Competition of two substrates for a single enzyme. A simple kinetic theorem exemplified by a hydroxy steroid dehydrogenase reaction
    • Pocklington, T. and Jeffery, J. (1969) Competition of two substrates for a single enzyme. A simple kinetic theorem exemplified by a hydroxy steroid dehydrogenase reaction. Biochem. J. 112, 331-334
    • (1969) Biochem. J. , vol.112 , pp. 331-334
    • Pocklington, T.1    Jeffery, J.2


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