메뉴 건너뛰기




Volumn 289, Issue 3, 2014, Pages 1798-1814

Molecular and thermodynamic mechanisms of the chloride-dependent human angiotensin-I-converting enzyme (ACE)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN-CONVERTING ENZYME; CHLORIDE CONCENTRATIONS; ISOTHERMAL TITRATION CALORIMETRY; SUBSTRATE COMPOSITION; SUBSTRATE INTERACTION; SUBSTRATE SPECIFICITY; THERMODYNAMIC MECHANISM; X RAY CRYSTAL STRUCTURES;

EID: 84892628652     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.512335     Document Type: Article
Times cited : (27)

References (42)
  • 2
    • 70350006638 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme New insights into structure, biological significance and prospects for domain-selective inhibitors
    • Watermeyer, J. M., Kroger, W. L., Sturrock, E. D., and Ehlers, M. R. (2009) Angiotensin-converting enzyme New insights into structure, biological significance and prospects for domain-selective inhibitors. Curr. Enzyme Inhib. 5, 134-147
    • (2009) Curr. Enzyme Inhib. , vol.5 , pp. 134-147
    • Watermeyer, J.M.1    Kroger, W.L.2    Sturrock, E.D.3    Ehlers, M.R.4
  • 3
    • 84857520077 scopus 로고    scopus 로고
    • Structure based drug design of angiotensin-I converting enzyme inhibitors
    • Anthony, C. S., Masuyer, G., Sturrock, E. D., Acharya, K. R. (2012) Structure based drug design of angiotensin-I converting enzyme inhibitors. Curr. Med. Chem. 19, 845-855
    • (2012) Curr. Med. Chem. , vol.19 , pp. 845-855
    • Anthony, C.S.1    Masuyer, G.2    Sturrock, E.D.3    Acharya, K.R.4
  • 4
    • 84944073735 scopus 로고    scopus 로고
    • (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds), Elsevier Academic Press, San Diego
    • Corvol, P., Eyries, M., and Soubrier F (2004) Handbook of Proteolytic Enzymes, (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds) pp. 332-346, Elsevier Academic Press, San Diego
    • (2004) Handbook of Proteolytic Enzymes , pp. 332-346
    • Corvol, P.1    Eyries, M.2    Soubrier, F.3
  • 5
    • 0025824349 scopus 로고
    • Structure of the angiotensin I-converting enzyme gene: Two alternate promoters correspond to evolutionary steps of a duplicated gene
    • Hubert, C., Houot, A. M., Corvol, P., Soubrier, F. (1991) Structure of the angiotensin I-converting enzyme gene. Two alternate promoters correspond to evolutionary steps of a duplicated gene. J. Biol. Chem. 266, 15377-15383 (Pubitemid 21907658)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.23 , pp. 15377-15383
    • Hubert, C.1    Houot, A.-M.2    Corvol, P.3    Soubrier, F.4
  • 6
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • DOI 10.1038/nature01370
    • Natesh, R., Schwager, S. L., Sturrock, E. D., and Acharya, K. R. (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421, 551-554 (Pubitemid 36168450)
    • (2003) Nature , vol.421 , Issue.6922 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.U.2    Sturrock, E.D.3    Acharya, K.R.4
  • 7
    • 33644945546 scopus 로고    scopus 로고
    • Crystal structure of the N domain of human 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. (2006) Crystal structure of the N domain of human angiotensin I-converting enzyme provides a structural basis for domain specific inhibitor design. J. Mol. Biol. 357, 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
  • 8
    • 33750291932 scopus 로고    scopus 로고
    • Structure of testis ACE glycosylation mutants and evidence for conserved domain movement
    • DOI 10.1021/bi061146z
    • Watermeyer, J. M., Sewell, B. T., Schwager, S. L., Natesh, R., Corradi, H. R., Acharya, K. R., and Sturrock, E. D. (2006) Structure of testis ACE glycosylation mutants and evidence for conserved domain movement. Biochemistry 45, 12654-12663 (Pubitemid 44630850)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12654-12663
    • Watermeyer, J.M.1    Sewell, B.T.2    Schwager, S.L.3    Natesh, R.4    Corradi, H.R.5    Acharya, K.R.6    Sturrock, E.D.7
  • 9
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews, B. W. (1988) Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21, 333-340
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 11
    • 0020593991 scopus 로고
    • Anion activation of angiotensin converting enzyme. Dependence on nature of substrate
    • Shapiro, R., Holmquist, B., and Riordan, J. F. (1983) Anion activation of angiotensin converting enzyme. Dependence on nature of substrate. Biochemistry 22, 3850-3857 (Pubitemid 13035557)
    • (1983) Biochemistry , vol.22 , Issue.16 , pp. 3850-3857
    • Shapiro, R.1    Holmquist, B.2    Riordan, J.F.3
  • 12
    • 33745845825 scopus 로고    scopus 로고
    • Physiology of local reninangiotensin systems
    • Paul, M., Poyan Mehr, A., and Kreutz, R. (2006) Physiology of local reninangiotensin systems. Physiol. Rev. 86, 747-803
    • (2006) Physiol. Rev. , vol.86 , pp. 747-803
    • Paul, M.1    Poyan Mehr, A.2    Kreutz, R.3
  • 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. (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
  • 17
    • 0031026048 scopus 로고    scopus 로고
    • Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form
    • DOI 10.1074/jbc.272.6.3511
    • Yu, X. C., Sturrock, E. D., Wu, Z., Biemann, K., Ehlers, M. R., and Riordan, J. F. (1997) Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form. J. Biol. Chem. 272, 3511-3519 (Pubitemid 27066852)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3511-3519
    • Sturrock, E.D.1    Wu Zhuchun2    Biemann, K.3    Ehlersu, M.R.W.4    Riordan, J.F.5
  • 18
    • 0037216848 scopus 로고    scopus 로고
    • Monoclonal antibodies to denatured human ACE (CD 143), broad species specificity, reactivity on paraffin sections, and detection of subtle conformational changes in the C-terminal domain of ACE
    • DOI 10.1034/j.1399-0039.2003.610104.x
    • Balyasnikova, I. V., Metzger, R., Franke, F. E., and Danilov, S.M. (2003) Monoclonal antibodies to denatured human ACE (CD 143), broad species specificity, reactivity on paraffin sections, and detection of subtle conformational changes in the C-terminal domain of ACE. Tissue Antigens 61, 49-62 (Pubitemid 36286749)
    • (2003) Tissue Antigens , vol.61 , Issue.1 , pp. 49-62
    • Balyasnikova, I.V.1    Metzger, R.2    Franke, F.E.3    Danilov, S.M.4
  • 19
    • 78149236201 scopus 로고    scopus 로고
    • The N domain of human angiotensin-I converting enzyme. The role of N-glycosylation and the crystal structure in complex with an N-domain-specific phosphinic inhibitor, RXP407
    • Anthony, C. S., Corradi, H. R., Schwager, S. L., Redelinghuys, P., GAdis, D., Dive, V., Acharya, K. R., and Sturrock, E. D. (2010) The N domain of human angiotensin-I converting enzyme. The role of N-glycosylation and the crystal structure in complex with an N-domain-specific phosphinic inhibitor, RXP407. J. Biol. Chem. 285, 35685-35693
    • (2010) J. Biol. Chem. , vol.285 , pp. 35685-35693
    • Anthony, C.S.1    Corradi, H.R.2    Schwager, S.L.3    Redelinghuys, P.4    Georgiadis, D.5    Dive, V.6    Acharya, K.R.7    Sturrock, E.D.8
  • 21
    • 71649092785 scopus 로고    scopus 로고
    • Processing diffraction data with Mosflm
    • (Read, R. J., and Sussman, J. L., eds), Springer, Dordrecht, The Netherlands
    • Leslie, A.G.W., and Powell, H.R. (2007) Processing diffraction data with Mosflm. in Evolving Methods for Macromolecular Crystallography (Read, R. J., and Sussman, J. L., eds) pp. 41-51, Springer, Dordrecht, The Netherlands
    • (2007) Evolving Methods for Macromolecular Crystallography , pp. 41-51
    • Leslie, A.G.W.1    Powell, H.R.2
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computing Project, Number 4
    • Collaborative Computing Project, Number 4 (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
  • 25
    • 0026597444 scopus 로고
    • Free R-value. A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R-value. A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 28
    • 0017194947 scopus 로고
    • A sensitive fluorimetric assay for serum angiotensin-converting enzyme
    • Friedland, J., and Silverstein, E. (1976) A sensitive fluorimetric assay for serum angiotensin-converting enzyme. Am. J. Clin. Pathol. 66, 416-424
    • (1976) Am. J. Clin. Pathol. , vol.66 , pp. 416-424
    • Friedland, J.1    Silverstein, E.2
  • 29
    • 69249106454 scopus 로고    scopus 로고
    • The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine. A thermodynamic analysis
    • Stockbridge, R. B., and Wolfenden, R. (2009) The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine. A thermodynamic analysis. J. Biol. Chem. 284, 22747-22757
    • (2009) J. Biol. Chem. , vol.284 , pp. 22747-22757
    • Stockbridge, R.B.1    Wolfenden, R.2
  • 30
    • 77955843887 scopus 로고    scopus 로고
    • Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model
    • Golicnik, M. (2010) Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model. Anal. Biochem. 406, 94-96
    • (2010) Anal. Biochem. , vol.406 , pp. 94-96
    • Golicnik, M.1
  • 32
    • 3042732126 scopus 로고    scopus 로고
    • Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme
    • DOI 10.1021/bi049480n
    • Natesh, R., Schwager, S. L., Evans, H. R., Sturrock, E. D., and Acharya, K. R. (2004) Structural details on the binding of hypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry 43, 8718-8724 (Pubitemid 38880042)
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8718-8724
    • Natesh, R.1    Schwager, S.L.U.2    Evans, H.R.3    Sturrock, E.D.4    Acharya, K.R.5
  • 33
    • 0242569193 scopus 로고    scopus 로고
    • Angiotensin-Converting Enzyme-2 (ACE2): Comparative Modeling of the Active Site, Specificity Requirements, and Chloride Dependence
    • DOI 10.1021/bi035268s
    • Guy, J. L., Jackson, R. M., Acharya, K. R., Sturrock, E. D., Hooper, N. M., and Turner, A. J. (2003) Angiotensin-converting enzyme-2 (ACE2). Comparative modeling of the active site, specificity requirements, and chloride dependence. Biochemistry 42, 13185-13192 (Pubitemid 37420671)
    • (2003) Biochemistry , vol.42 , Issue.45 , 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
  • 34
    • 55949102926 scopus 로고    scopus 로고
    • Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis
    • Rushworth, C. A., Guy, J. L., and Turner, A. J. (2008) Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis. FEBS J. 275, 6033-6042
    • (2008) FEBS J. , vol.275 , pp. 6033-6042
    • Rushworth, C.A.1    Guy, J.L.2    Turner, A.J.3
  • 35
    • 0035823581 scopus 로고    scopus 로고
    • Arg1098 is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity
    • Liu, X., Fernandez, M., Wouters, M. A., Heyberger, S., and Husain, A. (2001) Arg1098 is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity. J. Biol. Chem. 276, 33518-33525
    • (2001) J. Biol. Chem. , vol.276 , pp. 33518-33525
    • Liu, X.1    Fernandez, M.2    Wouters, M.A.3    Heyberger, S.4    Husain, A.5
  • 36
    • 84868271035 scopus 로고    scopus 로고
    • Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides
    • Masuyer, G., Schwager, S. L., Sturrock, E. D., Isaac, R. E., and Acharya, K. R. (2012) Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides. Sci. Rep. 2, 717
    • (2012) Sci. Rep. , vol.2 , pp. 717
    • Masuyer, G.1    Schwager, S.L.2    Sturrock, E.D.3    Isaac, R.E.4    Acharya, K.R.5
  • 37
    • 1442286037 scopus 로고    scopus 로고
    • - activation and peptide hydrolysis mechanisms
    • Tzakos, A. G., Galanis, A. S., Spyroulias, G. A., Cordopatis, P., Manessi-Zoupa, E., and Gerothanassis, I. P. (2003) Structure-function discrimination of the N- and C-catalytic domains of human angiotensin-converting enzyme. Implications for Cl-activation and peptide hydrolysis mechanisms. Protein Eng. 16, 993-1003 (Pubitemid 38281750)
    • (2003) Protein Engineering , vol.16 , Issue.12 , pp. 993-1003
    • Tzakos, A.G.1    Galanis, A.S.2    Spyroulias, G.A.3    Cordopatis, P.4    Manessi-Zoupa, E.5    Gerothanassis, I.P.6
  • 38
    • 0027378334 scopus 로고
    • Mutations in two specific residues of testicular angiotensin-converting enzyme change its catalytic properties
    • Sen, I., Kasturi, S., Abdul Jabbar, M., and Sen, G. C. (1993) Mutations in two specific residues of testicular angiotensin-converting enzyme change its catalytic properties. J. Biol. Chem. 268, 25748-25754 (Pubitemid 23358190)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.34 , pp. 25748-25754
    • Sen, I.1    Kasturi, S.2    Jabbar, M.A.3    Sen, G.C.4
  • 39
    • 0025222019 scopus 로고
    • Identification of essential tyrosine and lysine residues in angiotensin converting enzyme. Evidence for a single active site
    • Chen, Y. N., and Riordan, J. F. (1990) Identification of essential tyrosine and lysine residues in angiotensin converting enzyme. Evidence for a single active site. Biochemistry 29, 10493-10498
    • (1990) Biochemistry , vol.29 , pp. 10493-10498
    • Chen, Y.N.1    Riordan, J.F.2
  • 40
    • 0035895889 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme transition state stabilization by His1089. Evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases
    • Fernandez, M., Liu, X., Wouters, M. A., Heyberger, S., and Husain, A. (2001) Angiotensin I-converting enzyme transition state stabilization by His1089. Evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases. J. Biol. Chem. 276, 4998-5004
    • (2001) J. Biol. Chem. , vol.276 , pp. 4998-5004
    • Fernandez, M.1    Liu, X.2    Wouters, M.A.3    Heyberger, S.4    Husain, A.5
  • 41
    • 27844506307 scopus 로고    scopus 로고
    • Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme
    • DOI 10.1007/s10541-005-0242-9
    • Moiseeva, N. A., Binevski, P. V., Baskin, I. I., Palyulin, V. A., and Kost, O. A. (2005) Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme. Biochemistry 70, 1167-1172 (Pubitemid 41641423)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.10 , pp. 1167-1172
    • Moiseeva, N.A.1    Binevski, P.V.2    Baskin, I.I.3    Palyulin, V.A.4    Kost, O.A.5
  • 42
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.