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Volumn 59, Issue 12, 2002, Pages 2136-2143

Active-site mutants of class B β-lactamases: Substrate binding and mechanistic study

Author keywords

Catalytic mechanism; Metallo lactamase; Molecular mechanics; Molecular modeling; Penicillin binding; Zinc enzyme

Indexed keywords

BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; LIGAND; PENICILLIN G; ZINC;

EID: 0036971224     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180200013     Document Type: Article
Times cited : (8)

References (25)
  • 2
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J. M. et al. (1995) The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14: 4914-4921
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duee, E.3    Galleni, M.4    Duez, C.5    Frere, J.M.6
  • 5
    • 0032497362 scopus 로고    scopus 로고
    • Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 Å resolution: Binuclear active site with features of a mononuclear enzyme
    • Fabiane S. M., Sohi M. K., Wan T., Payne D. J., Bateson J. H., Mitchell T. et al. (1998) Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 Å resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry 37: 12404-12411
    • (1998) Biochemistry , vol.37 , pp. 12404-12411
    • Fabiane, S.M.1    Sohi, M.K.2    Wan, T.3    Payne, D.J.4    Bateson, J.H.5    Mitchell, T.6
  • 6
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis
    • Concha N. O., Rasmussen B. A., Bush K. and Herzberg O. (1996) Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure 4: 823-836
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 7
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • Concha N. O., Janson C. A., Rowling P., Pearson S., Cheever C. A., Clarke B. P. et al. (2000) Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39: 4288-4298
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3    Pearson, S.4    Cheever, C.A.5    Clarke, B.P.6
  • 8
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution
    • Ullah J. H., Walsh T. R., Taylor I. A., Emery D. C., Verma C. S., Gamblin S. J. et al. (1998) The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J. Mol. Biol. 284: 125-136
    • (1998) J. Mol. Biol. , vol.284 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3    Emery, D.C.4    Verma, C.S.5    Gamblin, S.J.6
  • 10
    • 0035976958 scopus 로고    scopus 로고
    • Metal ion binding and coordination geometry for wild type and mutants of metallo-β-lactamase from Bacillus cereus 569/H/9 (BcII): A combined thermodynamic, kinetic, and spectroscopic approach
    • Seny D. de, Heinz U., Wommer S., Kiefer M., Meyer-Klaucke W., Galleni M. et al. (2001) Metal ion binding and coordination geometry for wild type and mutants of metallo-β-lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach. J. Biol. Chem. 276: 45065-45078
    • (2001) J. Biol. Chem. , vol.276 , pp. 45065-45078
    • De Seny, D.1    Heinz, U.2    Wommer, S.3    Kiefer, M.4    Meyer-Klaucke, W.5    Galleni, M.6
  • 11
    • 0036566439 scopus 로고    scopus 로고
    • Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-βlactamase
    • Seny D. de, Prosperi-Meys C., Bebrone C., Rossolini G.M., Page M., Noel E et al. (2002) Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-βlactamase. Biochem. J. 363: 687-696
    • (2002) Biochem. J. , vol.363 , pp. 687-696
    • De Seny, D.1    Prosperi-Meys, C.2    Bebrone, C.3    Rossolini, G.M.4    Page, M.5    Noel, E.6
  • 12
    • 0035664075 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of class B β-lactamases: A molecular modelling study
    • Prosperi-Meys C., Wouters J., Galleni M. and Lamotte-Brasseur J. (2001) Substrate binding and catalytic mechanism of class B β-lactamases: a molecular modelling study. Cell. Mol. Life Sci. 58: 2136-2143
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 2136-2143
    • Prosperi-Meys, C.1    Wouters, J.2    Galleni, M.3    Lamotte-Brasseur, J.4
  • 15
    • 0032951167 scopus 로고    scopus 로고
    • Structural consequences of the active site substitution Cys181 Ser in metallo-β-lactamase from Bacteroides fragilis
    • Li Z., Rasmussen B. A. and Herzberg O. (1999) Structural consequences of the active site substitution Cys181 Ser in metallo-β-lactamase from Bacteroides fragilis. Protein Sci. 8: 249-252
    • (1999) Protein Sci. , vol.8 , pp. 249-252
    • Li, Z.1    Rasmussen, B.A.2    Herzberg, O.3
  • 16
    • 0345125154 scopus 로고
    • Structure of proteins with single-site mutations: A minimum perturbation approach
    • Shih H. H. L., Brady J. and Karplus M. (1985) Structure of proteins with single-site mutations: a minimum perturbation approach. Proc. Natl. Acad. Sci. USA 82: 1697-1700
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1697-1700
    • Shih, H.H.L.1    Brady, J.2    Karplus, M.3
  • 17
    • 0842341771 scopus 로고
    • Development and use of quantum mechanical molecular models. 76. AM1: A new general purpose quantum mechanical molecular model
    • Dewar M. J. S., Zoebisch E. G., Healy E. F. and Stewart J. J. P. (1985) Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model. J. Am. Chem. Soc. 107: 3902-3909
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3902-3909
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 18
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins
    • Schrauber H., Eisenhaber F. and Argos P. (1993) Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins. J. Mol. Biol. 230: 592-612
    • (1993) J. Mol. Biol. , vol.230 , pp. 592-612
    • Schrauber, H.1    Eisenhaber, F.2    Argos, P.3
  • 19
    • 0342323748 scopus 로고    scopus 로고
    • Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-β-lactamase
    • Chantalat L., Duee E., Galleni M., Frere J.-M. and Dideberg O. (2000) Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-β-lactamase. Protein Sci. 9: 1402-1406
    • (2000) Protein Sci. , vol.9 , pp. 1402-1406
    • Chantalat, L.1    Duee, E.2    Galleni, M.3    Frere, J.-M.4    Dideberg, O.5
  • 20
    • 0033056949 scopus 로고    scopus 로고
    • Kinetic properties and metal content of the metalloβ-lactamase CcrA harboring selective amino acid substitutions
    • Yang Y., Keeney D., Tang X.-J., Canfield N. and Rasmussen B. A. (1999) Kinetic properties and metal content of the metalloβ-lactamase CcrA harboring selective amino acid substitutions. J. Biol. Chem. 274: 15706-15711
    • (1999) J. Biol. Chem. , vol.274 , pp. 15706-15711
    • Yang, Y.1    Keeney, D.2    Tang, X.-J.3    Canfield, N.4    Rasmussen, B.A.5
  • 22
    • 0032879868 scopus 로고    scopus 로고
    • Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases
    • Nagano R., Adachi Y., Imamura H., Yamada K., Hashizume T. and Morishima H. (1999) Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases. Antimicrob. Agents Chemother. 43: 2497-2503
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2497-2503
    • Nagano, R.1    Adachi, Y.2    Imamura, H.3    Yamada, K.4    Hashizume, T.5    Morishima, H.6
  • 25
    • 13144295022 scopus 로고    scopus 로고
    • Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase
    • Toney J. H., Fitzgerald P. M., Grover-Sharma N., Olson S. H., May W. J., Sundelof J. G. et al. (1998) Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase. Chem. Biol. 5: 185-196
    • (1998) Chem. Biol. , vol.5 , pp. 185-196
    • Toney, J.H.1    Fitzgerald, P.M.2    Grover-Sharma, N.3    Olson, S.H.4    May, W.J.5    Sundelof, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.