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Volumn 8, Issue 10, 2013, Pages 2112-2116

Binding of (5 S)-penicilloic acid to penicillin binding protein 3

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM ANTIBIOTIC; ENZYME; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 3; PENICILLOIC ACID; PIPERACILLIN; UNCLASSIFIED DRUG; COORDINATION COMPOUND; PENICILLANIC ACID;

EID: 84886452514     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400200h     Document Type: Article
Times cited : (22)

References (24)
  • 1
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of β-lactamase inhibitors
    • Drawz, S. M. and Bonomo, R. A. (2010) Three decades of β-lactamase inhibitors Clin. Microbiol. Rev. 23, 160-201
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 2
    • 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. U.S.A. 54, 1133-1141
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 3
    • 38349156636 scopus 로고    scopus 로고
    • Trapping of an acyl-enzyme intermediate in a penicillin-binding protein (PBP)-catalyzed reaction
    • Macheboeuf, P., Lemaire, D., Dos Santos Martins, A., Dideberg, O., Jamin, M., and Dessen, A. (2008) Trapping of an acyl-enzyme intermediate in a penicillin-binding protein (PBP)-catalyzed reaction J. Mol. Biol. 376, 405-413
    • (2008) J. Mol. Biol. , vol.376 , pp. 405-413
    • Macheboeuf, P.1    Lemaire, D.2    Dos Santos Martins, A.3    Dideberg, O.4    Jamin, M.5    Dessen, A.6
  • 4
    • 80053247739 scopus 로고    scopus 로고
    • Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from Gram-negative bacteria
    • Bush, K. and Fisher, J. F. (2011) Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from Gram-negative bacteria Annu. Rev. Microbiol. 65, 455-478
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 455-478
    • Bush, K.1    Fisher, J.F.2
  • 6
    • 0026049801 scopus 로고
    • Serine β-lactamases and penicillin-binding proteins
    • Ghuysen, J.-M. (1991) Serine β-lactamases and penicillin-binding proteins Annu. Rev. Microbiol. 45, 37-67
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 37-67
    • Ghuysen, J.-M.1
  • 8
    • 78650417877 scopus 로고    scopus 로고
    • Crystal structures of penicillin- binding protein 3 from Pseudomonas aeruginosa: Comparison of native and antibiotic-bound forms
    • Sainsbury, S., Bird, L., Rao, V., Shepherd, S. M., Stuart, D. I., Hunter, W. N., Owens, R. J., and Ren, J. (2011) Crystal structures of penicillin- binding protein 3 from Pseudomonas aeruginosa: comparison of native and antibiotic-bound forms J. Mol. Biol. 405, 173-184
    • (2011) J. Mol. Biol. , vol.405 , pp. 173-184
    • Sainsbury, S.1    Bird, L.2    Rao, V.3    Shepherd, S.M.4    Stuart, D.I.5    Hunter, W.N.6    Owens, R.J.7    Ren, J.8
  • 9
    • 84867082602 scopus 로고    scopus 로고
    • Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant Staphylococcus aureus in the Apo and Cefotaxime-bound forms
    • Yoshida, H., Kawai, F., Obayashi, E., Akashi, S., Roper, D. I., Tame, J. R. H., and Park, S.-Y. (2012) Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant Staphylococcus aureus in the Apo and Cefotaxime-bound forms J. Mol. Biol. 423, 351-364
    • (2012) J. Mol. Biol. , vol.423 , pp. 351-364
    • Yoshida, H.1    Kawai, F.2    Obayashi, E.3    Akashi, S.4    Roper, D.I.5    Tame, J.R.H.6    Park, S.-Y.7
  • 11
    • 0036121221 scopus 로고    scopus 로고
    • Structural milestones in the pathway of an amide hydrolase: Substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase
    • Beadle, B. M., Trehan, I., Focia, P. J., and Shoichet, B. K. (2002) Structural milestones in the pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase Structure 10, 413-424
    • (2002) Structure , vol.10 , pp. 413-424
    • Beadle, B.M.1    Trehan, I.2    Focia, P.J.3    Shoichet, B.K.4
  • 12
    • 0036965578 scopus 로고    scopus 로고
    • Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins
    • McDonough, M. A., Anderson, J. W., Silvaggi, N. R., Pratt, R. F., Knox, J. R., and Kelly, J. A. (2002) Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins J. Mol. Biol. 322, 111-122
    • (2002) J. Mol. Biol. , vol.322 , pp. 111-122
    • McDonough, M.A.1    Anderson, J.W.2    Silvaggi, N.R.3    Pratt, R.F.4    Knox, J.R.5    Kelly, J.A.6
  • 13
    • 37049088665 scopus 로고
    • Thiazolidine ring opening in penicillin derivatives. Part 1. Imine formation
    • Davis, A. M., Jones, M., and Page, M. I. (1991) Thiazolidine ring opening in penicillin derivatives. Part 1. Imine formation J. Chem. Soc., Perkin Trans. 2, 1219-1223
    • (1991) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1219-1223
    • Davis, A.M.1    Jones, M.2    Page, M.I.3
  • 14
    • 80155198751 scopus 로고    scopus 로고
    • Structural characterization of the tobramycin-piperacillin reaction product formed at pH 6.0
    • Pagano, T. G., Gong, Y., Kong, F., Tsao, R., Fawzi, M., and Zhu, T. (2011) Structural characterization of the tobramycin-piperacillin reaction product formed at pH 6.0 J. Antibiot. 64, 673-677
    • (2011) J. Antibiot. , vol.64 , pp. 673-677
    • Pagano, T.G.1    Gong, Y.2    Kong, F.3    Tsao, R.4    Fawzi, M.5    Zhu, T.6
  • 15
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M. and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy Angew. Chem., Int. Ed. 38, 1784-1788
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 16
    • 43049095602 scopus 로고    scopus 로고
    • Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multi-angle or static light scattering
    • Nettleship, J. E., Brown, J., Groves, M. R., and Geerlof, A. (2008) Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multi-angle or static light scattering Methods Mol. Biol. 426, 299-318
    • (2008) Methods Mol. Biol. , vol.426 , pp. 299-318
    • Nettleship, J.E.1    Brown, J.2    Groves, M.R.3    Geerlof, A.4
  • 17
    • 0032526053 scopus 로고    scopus 로고
    • Reaction of soluble penicillin-binding protein 2a of methicillin- resistant Staphylococcus aureus with β-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 β-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
  • 18
    • 0021336341 scopus 로고
    • Epimerization of benzylpenicilloic acid in alkaline media
    • Ghebre-Sellassie, I., Hem, S. L., and Knevel, A. M. (1984) Epimerization of benzylpenicilloic acid in alkaline media J. Pharm. Sci. 73, 125-128
    • (1984) J. Pharm. Sci. , vol.73 , pp. 125-128
    • Ghebre-Sellassie, I.1    Hem, S.L.2    Knevel, A.M.3
  • 19
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 20
    • 31444452744 scopus 로고
    • Automatic generation of 3D atomic coordinates for organic molecules
    • Gasteiger, J., Rudolph, C., and Sadowski, J. (1990) Automatic generation of 3D atomic coordinates for organic molecules Tetrahedron Comput. Methodol. 3, 537-547
    • (1990) Tetrahedron Comput. Methodol. , vol.3 , pp. 537-547
    • Gasteiger, J.1    Rudolph, C.2    Sadowski, J.3
  • 21
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gasteiger, J. and Marsili, M. (1980) Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges Tetrahedron 36, 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 23
    • 0015613437 scopus 로고
    • Metabolism of penicillins to penicilloic acids and 6-aminopenicillanic acid in man and its significance in assessing penicillin absorption
    • Cole, M., Kenig, M. D., and Hewitt, V. A. (1973) Metabolism of penicillins to penicilloic acids and 6-aminopenicillanic acid in man and its significance in assessing penicillin absorption Antimicrob. Agents Chemother. 3, 463-468
    • (1973) Antimicrob. Agents Chemother. , vol.3 , pp. 463-468
    • Cole, M.1    Kenig, M.D.2    Hewitt, V.A.3
  • 24
    • 20544440614 scopus 로고    scopus 로고
    • Inhibitors of metallo-β-lactamase generated from β-lactam antibiotics
    • Badarau, A., Llinás, A., Laws, A. P., Damblon, C., and Page, M. I. (2005) Inhibitors of metallo-β-lactamase generated from β-lactam antibiotics Biochemistry 44, 8578-8589
    • (2005) Biochemistry , vol.44 , pp. 8578-8589
    • Badarau, A.1    Llinás, A.2    Laws, A.P.3    Damblon, C.4    Page, M.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.