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Volumn 55, Issue 5, 2012, Pages 2163-2172

Structure-based design of potent and ligand-efficient inhibitors of CTX-M class A β-lactamase

Author keywords

[No Author keywords available]

Indexed keywords

6 TRIFLUOROMETHYL 3H BENZOIMIDAZOLE 4 CARBOXYLIC ACID[3 (1H TETRAZOL 5 YL)PHENYL]AMIDE; BETA LACTAMASE CTX M; BETA LACTAMASE INHIBITOR; CEFOTAXIME; EXTENDED SPECTRUM BETA LACTAMASE; TETRAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84863274415     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm2014138     Document Type: Article
Times cited : (35)

References (43)
  • 3
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl- d -alanyl- d -alanine
    • Tipper, D. J.; Strominger, J. L. 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. 1965, 54, 1133-1141
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 4
    • 0037432016 scopus 로고    scopus 로고
    • The crystal structure of phosphonate-inhibited d -Ala- d -Ala peptidase reveals an analogue of a tetrahedral transition state
    • Silvaggi, N. R.; Anderson, J. W.; Brinsmade, S. R.; Pratt, R. F.; Kelly, J. A. The crystal structure of phosphonate-inhibited d -Ala- d -Ala peptidase reveals an analogue of a tetrahedral transition state Biochemistry 2003, 42, 1199-1208
    • (2003) Biochemistry , vol.42 , pp. 1199-1208
    • Silvaggi, N.R.1    Anderson, J.W.2    Brinsmade, S.R.3    Pratt, R.F.4    Kelly, J.A.5
  • 5
    • 0029019031 scopus 로고
    • Beta-lactamases and bacterial resistance to antibiotics
    • Frere, J. M. Beta-lactamases and bacterial resistance to antibiotics Mol. Microbiol. 1995, 16, 385-395
    • (1995) Mol. Microbiol. , vol.16 , pp. 385-395
    • Frere, J.M.1
  • 6
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to beta-lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher, J. F.; Meroueh, S. O.; Mobashery, S. Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity Chem. Rev. 2005, 105, 395-424
    • (2005) Chem. Rev. , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 7
    • 47749093130 scopus 로고    scopus 로고
    • The bacteria fight back
    • Taubes, G. The bacteria fight back Science 2008, 321, 356-361
    • (2008) Science , vol.321 , pp. 356-361
    • Taubes, G.1
  • 8
    • 0029071785 scopus 로고
    • A functional classification scheme for beta-lactamases and its correlation with molecular structure
    • Bush, K.; Jacoby, G. A.; Medeiros, A. A. A functional classification scheme for beta-lactamases and its correlation with molecular structure Antimicrob. Agents Chemother. 1995, 39, 1211-1233
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 9
    • 0028883511 scopus 로고
    • Beta-Lactamases in laboratory and clinical resistance
    • Livermore, D. M. beta-Lactamases in laboratory and clinical resistance Clin. Microbiol. Rev. 1995, 8, 557-584
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 10
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M beta-lactamases: Extended spectrum activities from increased mobility and decreased stability
    • Chen, Y.; Delmas, J.; Sirot, J.; Shoichet, B.; Bonnet, R. Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability J. Mol. Biol. 2005, 348, 349-362
    • (2005) J. Mol. Biol. , vol.348 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, J.3    Shoichet, B.4    Bonnet, R.5
  • 11
    • 77953729075 scopus 로고    scopus 로고
    • Structural insights into substrate recognition and product expulsion in CTX-M enzymes
    • Delmas, J.; Leyssene, D.; Dubois, D.; Birck, C.; Vazeille, E.; Robin, F.; Bonnet, R. Structural insights into substrate recognition and product expulsion in CTX-M enzymes J. Mol. Biol. 2010, 400, 108-120
    • (2010) J. Mol. Biol. , vol.400 , pp. 108-120
    • Delmas, J.1    Leyssene, D.2    Dubois, D.3    Birck, C.4    Vazeille, E.5    Robin, F.6    Bonnet, R.7
  • 12
    • 17644390560 scopus 로고    scopus 로고
    • Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases
    • Chen, Y.; Shoichet, B.; Bonnet, R. Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases J. Am. Chem. Soc. 2005, 127, 5423-5434
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5423-5434
    • Chen, Y.1    Shoichet, B.2    Bonnet, R.3
  • 13
    • 0347362476 scopus 로고    scopus 로고
    • Growing group of extended-spectrum beta-lactamases: The CTX-M enzymes
    • Bonnet, R. Growing group of extended-spectrum beta-lactamases: the CTX-M enzymes Antimicrob. Agents Chemother. 2004, 48, 1-14
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1-14
    • Bonnet, R.1
  • 14
    • 0034763241 scopus 로고    scopus 로고
    • Extended-spectrum beta-lactamases in the 21st century: Characterization, epidemiology, and detection of this important resistance threat
    • Bradford, P. A. Extended-spectrum beta-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat Clin. Microbiol. Rev. 2001, 14, 933-951
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 933-951
    • Bradford, P.A.1
  • 15
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • Drawz, S. M.; Bonomo, R. A. Three decades of beta-lactamase inhibitors Clin. Microbiol. Rev. 2010, 23, 160-201
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 16
    • 0027513336 scopus 로고
    • Molecular basis of beta-lactamase induction in bacteria
    • Bennett, P. M.; Chopra, I. Molecular basis of beta-lactamase induction in bacteria Antimicrob. Agents Chemother. 1993, 37, 153-158
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 153-158
    • Bennett, P.M.1    Chopra, I.2
  • 17
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria
    • Jacobs, C.; Frere, J. M.; Normark, S. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria Cell 1997, 88, 823-832
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frere, J.M.2    Normark, S.3
  • 21
    • 69749123316 scopus 로고    scopus 로고
    • Inhibition of class A and C beta-lactamases by diaroyl phosphates
    • Majumdar, S.; Pratt, R. F. Inhibition of class A and C beta-lactamases by diaroyl phosphates Biochemistry 2009, 48, 8285-8292
    • (2009) Biochemistry , vol.48 , pp. 8285-8292
    • Majumdar, S.1    Pratt, R.F.2
  • 23
    • 0029760859 scopus 로고    scopus 로고
    • Structure-based design of a potent transition state analogue for TEM-1 beta-lactamase
    • Strynadka, N. C.; Martin, R.; Jensen, S. E.; Gold, M.; Jones, J. B. Structure-based design of a potent transition state analogue for TEM-1 beta-lactamase Nature Struct. Biol. 1996, 3, 688-695
    • (1996) Nature Struct. Biol. , vol.3 , pp. 688-695
    • Strynadka, N.C.1    Martin, R.2    Jensen, S.E.3    Gold, M.4    Jones, J.B.5
  • 24
    • 16844378060 scopus 로고    scopus 로고
    • Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture
    • Tondi, D.; Morandi, F.; Bonnet, R.; Costi, M. P.; Shoichet, B. K. Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture J. Am. Chem. Soc. 2005, 127, 4632-4639
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4632-4639
    • Tondi, D.1    Morandi, F.2    Bonnet, R.3    Costi, M.P.4    Shoichet, B.K.5
  • 25
    • 65349195698 scopus 로고    scopus 로고
    • Molecular docking and ligand specificity in fragment-based inhibitor discovery
    • Chen, Y.; Shoichet, B. K. Molecular docking and ligand specificity in fragment-based inhibitor discovery Nature Chem. Biol. 2009, 5, 358-364
    • (2009) Nature Chem. Biol. , vol.5 , pp. 358-364
    • Chen, Y.1    Shoichet, B.K.2
  • 28
    • 43949129098 scopus 로고    scopus 로고
    • Physicochemical properties of antibacterial compounds: Implications for drug discovery
    • O'Shea, R.; Moser, H. E. Physicochemical properties of antibacterial compounds: implications for drug discovery J. Med. Chem. 2008, 51, 2871-2878
    • (2008) J. Med. Chem. , vol.51 , pp. 2871-2878
    • O'Shea, R.1    Moser, H.E.2
  • 30
    • 34247857459 scopus 로고    scopus 로고
    • The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution
    • Chen, Y.; Bonnet, R.; Shoichet, B. K. The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution J. Am. Chem. Soc. 2007, 129, 5378-5380
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5378-5380
    • Chen, Y.1    Bonnet, R.2    Shoichet, B.K.3
  • 31
    • 23844444239 scopus 로고    scopus 로고
    • Hierarchical docking of databases of multiple ligand conformations
    • Lorber, D. M.; Shoichet, B. K. Hierarchical docking of databases of multiple ligand conformations Curr. Top. Med. Chem. 2005, 5, 739-749
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 739-749
    • Lorber, D.M.1    Shoichet, B.K.2
  • 32
    • 13844312649 scopus 로고    scopus 로고
    • ZINC-a free database of commercially available compounds for virtual screening
    • Irwin, J. J.; Shoichet, B. K. ZINC-a free database of commercially available compounds for virtual screening J. Chem. Inf. Model. 2005, 45, 177-182
    • (2005) J. Chem. Inf. Model. , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 33
    • 67649962669 scopus 로고    scopus 로고
    • Rapid assessment of a novel series of selective CB2 agonists using parallel synthesis protocols: A lipophilic efficiency (LipE) analysis
    • Ryckmans, T.; Edwards, M. P.; Horne, V. A.; Correia, A. M.; Owen, D. R.; Thompson, L. R.; Tran, I.; Tutt, M. F.; Young, T. Rapid assessment of a novel series of selective CB2 agonists using parallel synthesis protocols: a lipophilic efficiency (LipE) analysis Bioorg. Med. Chem. Lett. 2009, 19, 4406-4409
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 4406-4409
    • Ryckmans, T.1    Edwards, M.P.2    Horne, V.A.3    Correia, A.M.4    Owen, D.R.5    Thompson, L.R.6    Tran, I.7    Tutt, M.F.8    Young, T.9
  • 34
    • 84924572198 scopus 로고    scopus 로고
    • Performance Standards for Antimicrobial Susceptibility Testing; 20th Informational Supplement
    • 10020
    • Wayne, P. Performance Standards for Antimicrobial Susceptibility Testing; 20th Informational Supplement Clin. Lab. Stand. Inst. 2010, M100-S20, 1-23
    • (2010) Clin. Lab. Stand. Inst. , pp. 1-23
    • Wayne, P.1
  • 35
    • 0041818050 scopus 로고    scopus 로고
    • Crystal structure of extended-spectrum beta-lactamase Toho-1: Insights into the molecular mechanism for catalytic reaction and substrate specificity expansion
    • Ibuka, A. S.; Ishii, Y.; Galleni, M.; Ishiguro, M.; Yamaguchi, K.; Frere, J. M.; Matsuzawa, H.; Sakai, H. Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for catalytic reaction and substrate specificity expansion Biochemistry 2003, 42, 10634-10643
    • (2003) Biochemistry , vol.42 , pp. 10634-10643
    • Ibuka, A.S.1    Ishii, Y.2    Galleni, M.3    Ishiguro, M.4    Yamaguchi, K.5    Frere, J.M.6    Matsuzawa, H.7    Sakai, H.8
  • 36
    • 77649270363 scopus 로고    scopus 로고
    • Neutron diffraction studies of a class A beta-lactamase Toho-1 E166A/R274N/R276N triple mutant
    • Tomanicek, S. J.; Blakeley, M. P.; Cooper, J.; Chen, Y.; Afonine, P. V.; Coates, L. Neutron diffraction studies of a class A beta-lactamase Toho-1 E166A/R274N/R276N triple mutant J. Mol. Biol. 2010, 396, 1070-1080
    • (2010) J. Mol. Biol. , vol.396 , pp. 1070-1080
    • Tomanicek, S.J.1    Blakeley, M.P.2    Cooper, J.3    Chen, Y.4    Afonine, P.V.5    Coates, L.6
  • 37
    • 2242480185 scopus 로고    scopus 로고
    • Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin
    • Shimamura, T.; Ibuka, A.; Fushinobu, S.; Wakagi, T.; Ishiguro, M.; Ishii, Y.; Matsuzawa, H. Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin J. Biol. Chem. 2002, 277, 46601-46608
    • (2002) J. Biol. Chem. , vol.277 , pp. 46601-46608
    • Shimamura, T.1    Ibuka, A.2    Fushinobu, S.3    Wakagi, T.4    Ishiguro, M.5    Ishii, Y.6    Matsuzawa, H.7
  • 38
    • 0037094114 scopus 로고    scopus 로고
    • An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation
    • Minasov, G.; Wang, X.; Shoichet, B. K. An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation J. Am. Chem. Soc. 2002, 124, 5333-5340
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5333-5340
    • Minasov, G.1    Wang, X.2    Shoichet, B.K.3
  • 39
  • 40
    • 0026667480 scopus 로고
    • Antiallergic and cytoprotective activity of new N -phenylbenzamido acid derivatives
    • Makovec, F.; Peris, W.; Revel, L.; Giovanetti, R.; Redaelli, D.; Rovati, L. C. Antiallergic and cytoprotective activity of new N -phenylbenzamido acid derivatives J. Med. Chem. 1992, 35, 3633-3640
    • (1992) J. Med. Chem. , vol.35 , pp. 3633-3640
    • Makovec, F.1    Peris, W.2    Revel, L.3    Giovanetti, R.4    Redaelli, D.5    Rovati, L.C.6
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 1997, 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0028103275 scopus 로고
    • Collaborative Computational Project, N. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50, 760-763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763


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