메뉴 건너뛰기




Volumn 10, Issue 6, 2001, Pages 1254-1259

Interaction energies between β-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation

Author keywords

lactam; lactamase; Denaturation; Enzyme stability; PBP 5; Penicillin binding protein

Indexed keywords

BETA LACTAM ANTIBIOTIC; PENICILLIN BINDING PROTEIN;

EID: 0035019658     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.52001     Document Type: Article
Times cited : (21)

References (23)
  • 1
    • 0032872887 scopus 로고    scopus 로고
    • Functional analyses of AmpC beta-lactamase through differential stability
    • Beadle, B.M., McGovern, S.L., Patera, A., and Shoichet, B.K. 1999. Functional analyses of AmpC beta-lactamase through differential stability. Protein Sci. 8: 1816-1824.
    • (1999) Protein Sci. , vol.8 , pp. 1816-1824
    • Beadle, B.M.1    McGovern, S.L.2    Patera, A.3    Shoichet, B.K.4
  • 2
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W.J. and Schellman, J.A. 1987. Protein stability curves. Biopolymers 26: 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 3
    • 0035808477 scopus 로고    scopus 로고
    • Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3
    • in press
    • Davies, C., White, S.W., and Nicholas, R.A. 2001. Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3 A resolution. J. Biol. Chem. (in press).
    • (2001) A Resolution. J. Biol. Chem.
    • Davies, C.1    White, S.W.2    Nicholas, R.A.3
  • 4
    • 0033618429 scopus 로고    scopus 로고
    • The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of Streptomyces K15
    • Fonze, E., Vermeire, M., Nguyen-Disteche, M., Brasseur, R., and Charlier, P. 1999. The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of Streptomyces K15. J. Biol. Chem. 274: 21853-21860.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21853-21860
    • Fonze, E.1    Vermeire, M.2    Nguyen-Disteche, M.3    Brasseur, R.4    Charlier, P.5
  • 5
    • 0016753853 scopus 로고
    • Interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, substrate and beta-lactam antibiotics. A choice of models
    • Frere, J.M., Ghuysen, J.M., and Perkins, H.R. 1975. Interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, substrate and beta-lactam antibiotics. A choice of models. Eur. J. Biochem. 57: 353-359.
    • (1975) Eur. J. Biochem. , vol.57 , pp. 353-359
    • Frere, J.M.1    Ghuysen, J.M.2    Perkins, H.R.3
  • 7
    • 0003607510 scopus 로고
    • eds. J. Ghuysen and R. Hakenbeck, Amsterdam: Elsevier Science B.V.
    • Ghuysen, J.-M. and Dive, G. 1994. In Bacterial cell walls (eds. J. Ghuysen and R. Hakenbeck), pp. 103-130. Amsterdam: Elsevier Science B.V.
    • (1994) Bacterial Cell Walls , pp. 103-130
    • Ghuysen, J.-M.1    Dive, G.2
  • 8
    • 0032526053 scopus 로고    scopus 로고
    • Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with beta-lactams and acyclic substrates: Kinetics in homogeneous solution
    • Graves-Woodward, K. and Pratt, R.F. 1998. Reaction of soluble penicillin-binding protein 2a of methicillin- resistant Staphylococcus aureus with beta-lactams and acyclic substrates: Kinetics in homogeneous solution. Biochem. J. 332: 755-761.
    • (1998) Biochem. J. , vol.332 , pp. 755-761
    • Graves-Woodward, K.1    Pratt, R.F.2
  • 9
    • 0027198156 scopus 로고
    • Penicillin-binding protein 2x of Streptococcus pneumoniae: Enzymic activities and interactions with beta-lactams
    • Jamin, M., Damblon, C., Millier, S., Hakenbeck, R., and Frere, J.M. 1993. Penicillin-binding protein 2x of Streptococcus pneumoniae: Enzymic activities and interactions with beta-lactams. Biochem. J. 292: 735-741.
    • (1993) Biochem. J. , vol.292 , pp. 735-741
    • Jamin, M.1    Damblon, C.2    Millier, S.3    Hakenbeck, R.4    Frere, J.M.5
  • 11
    • 0024450592 scopus 로고
    • Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
    • Kelly, J.A., Knox, J.R., Zhao, H., Frere, J.M., and Ghuysen, J.M. 1989. Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme. J. Mol. Biol. 209: 281-295.
    • (1989) J. Mol. Biol. , vol.209 , pp. 281-295
    • Kelly, J.A.1    Knox, J.R.2    Zhao, H.3    Frere, J.M.4    Ghuysen, J.M.5
  • 13
    • 0033580616 scopus 로고    scopus 로고
    • Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: Kinetic characterization of its interactions with beta-lactams using eleclrospray mass spectrometry
    • Lu, W.P., Sun, Y., Bauer, M.D., Paule, S., Koenigs, P.M., and Kraft, W.G. 1999. Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: Kinetic characterization of its interactions with beta-lactams using eleclrospray mass spectrometry. Biochemistry 38: 6537-6546.
    • (1999) Biochemistry , vol.38 , pp. 6537-6546
    • Lu, W.P.1    Sun, Y.2    Bauer, M.D.3    Paule, S.4    Koenigs, P.M.5    Kraft, W.G.6
  • 14
    • 0031973490 scopus 로고    scopus 로고
    • Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases
    • Massova, I. and Mobashery, S. 1998. Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases. Antimicrob. Agents Chemother. 42: 1-17.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1-17
    • Massova, I.1    Mobashery, S.2
  • 15
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4: 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 17
    • 0023878451 scopus 로고
    • Site-directed mutants of a soluble form of penicillin-binding protein 5 from Escherichia coli and their catalytic properties
    • Nicholas, R.A. and Strominger, J.L. 1988. Site-directed mutants of a soluble form of penicillin-binding protein 5 from Escherichia coli and their catalytic properties. J. Biol. Chem. 263: 2034-2040.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2034-2040
    • Nicholas, R.A.1    Strominger, J.L.2
  • 18
    • 0034327676 scopus 로고    scopus 로고
    • Crystal structures of substrate and inhibitor complexes with AmpC beta-lactamase: Possible implications for substrate-assisted catalysis
    • Patera, A., Blaszczak, L.C., and Streichet, B.K. 2000. Crystal structures of substrate and inhibitor complexes with AmpC beta-lactamase: Possible implications for substrate-assisted catalysis. J. Am. Chem. Soc. 122: 10504-10512.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10504-10512
    • Patera, A.1    Blaszczak, L.C.2    Streichet, B.K.3
  • 19
    • 0027976825 scopus 로고
    • Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of a beta-lactamase
    • Rahil, J. and Pratt, R.F. 1994. Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of a beta-lactamase. Biochemistry 33: 116-125.
    • (1994) Biochemistry , vol.33 , pp. 116-125
    • Rahil, J.1    Pratt, R.F.2
  • 20
    • 0017066152 scopus 로고
    • The effect of binding on the melting temperature of biopolymers
    • Schellman, J.A. 1976. The effect of binding on the melting temperature of biopolymers. Biopolymers 15: 999-1018.
    • (1976) Biopolymers , vol.15 , pp. 999-1018
    • Schellman, J.A.1
  • 21
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D.J. and Strominger, J.L. 1965. Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. USA 54: 1133-1141.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 22
    • 0028053461 scopus 로고
    • Site-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coli
    • van der Linden, M.P., de Haan, L., Dideberg, O., and Keck, W. 1994. Site-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coli. Biochem. J. 303: 357-362.
    • (1994) Biochem. J. , vol.303 , pp. 357-362
    • Van Der Linden, M.P.1    De Haan, L.2    Dideberg, O.3    Keck, W.4
  • 23
    • 0013787826 scopus 로고
    • Penicillin: Its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis
    • Wise, E.M., Jr. and Park, J.T. 1965. Penicillin: Its basic site of action as an inhibitor of a peptide cross- linking reaction in cell wall mucopeptide synthesis. Proc. Natl. Acad. Sci. USA 54: 75-81.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 75-81
    • Wise E.M., Jr.1    Park, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.