메뉴 건너뛰기




Volumn 48, Issue 41, 2009, Pages 9912-9920

Why the extended-spectrum β-lactamases SHV-2 and SHV-5 are "hypersusceptible" to mechanism-based inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING POCKETS; CEFOTAXIME; CEFTAZIDIME; CLAVULANIC ACID; COMPARATIVE ANALYSIS; CRYSTALLOGRAPHIC DATA; ENAMINE INTERMEDIATES; ENAMINES; LACTAMASES; RAMAN BAND SHAPE ANALYSIS; RAMAN SPECTROSCOPIC; SITE-SPECIFIC; STOPPED-FLOW KINETICS; TAZOBACTAM; TEM; WILD TYPES;

EID: 70350042195     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9012098     Document Type: Article
Times cited : (17)

References (27)
  • 1
    • 27144490073 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases: A clinical update
    • Paterson, D. L., and Bonomo, R. A. (2005) Extended-spectrum β-lactamases: A clinical update. Clin. Microbiol. Rev. 18, 657-686.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 657-686
    • Paterson, D.L.1    Bonomo, R.A.2
  • 4
    • 55249126864 scopus 로고    scopus 로고
    • Clinical significance of extended-spectrum β-lactamases
    • Rodriguez-Bano, J., and Pascual, A. (2008) Clinical significance of extended-spectrum β-lactamases. Expert Rev. Anti-Infect. Ther. 6, 671-683.
    • (2008) Expert Rev. Anti-Infect. Ther. , vol.6 , pp. 671-683
    • Rodriguez-Bano, J.1    Pascual, A.2
  • 6
    • 0021024916 scopus 로고
    • Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens
    • Knothe, H., Shah, P., Krcmery, V., Antal, M., and Mitsuhashi, S. (1983) Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens. Infection 11, 315-317. (Pubitemid 14213754)
    • (1983) Infection , vol.11 , Issue.6 , pp. 315-317
    • Knothe, H.1    Shah, P.2    Krcmery, V.3
  • 7
    • 0031438322 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases and other enzymes providing resistance to oxyimino-β-lactams
    • Jacoby, G. A. (1997) Extended-spectrum β-lactamases and other enzymes providing resistance to oxyimino-β-lactams. Infect. Dis. Clin. North Am. 11, 875-887.
    • (1997) Infect. Dis. Clin. North Am. , vol.11 , pp. 875-887
    • Jacoby, G.A.1
  • 11
    • 24644495150 scopus 로고    scopus 로고
    • CTX-M: Changing the face of ESBLs in the UK
    • Livermore, D. M., and Hawkey, P. M. (2005) CTX-M: Changing the face of ESBLs in the UK. J. Antimicrob. Chemother. 56, 451-454.
    • (2005) J. Antimicrob. Chemother. , vol.56 , pp. 451-454
    • Livermore, D.M.1    Hawkey, P.M.2
  • 12
    • 0028821830 scopus 로고
    • Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure
    • Knox, J. R. (1995) Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure. Antimicrob. Agents Chemother. 39, 2593-2601.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2593-2601
    • Knox, J.R.1
  • 13
    • 0027408874 scopus 로고
    • Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type β-lactamases probed by site-directed mutagenesis and three-dimensional modeling
    • Huletsky, A., Knox, J. R., and Levesque, R. C. (1993) Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type β-lactamases probed by site-directed mutagenesis and three-dimensional modeling. J. Biol. Chem. 268, 3690-3697.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3690-3697
    • Huletsky, A.1    Knox, J.R.2    Levesque, R.C.3
  • 14
    • 0037453313 scopus 로고    scopus 로고
    • Ultrahigh resolution structure of a class a β-lactamase: On the mechanism and specificity of the extended-spectrum SHV-2 enzyme
    • Nukaga, M., Mayama, K., Hujer, A. M., Bonomo, R. A., and Knox, J. R. (2003) Ultrahigh resolution structure of a class A β-lactamase: On the mechanism and specificity of the extended-spectrum SHV-2 enzyme. J. Mol. Biol. 328, 289-301.
    • (2003) J. Mol. Biol. , vol.328 , pp. 289-301
    • Nukaga, M.1    Mayama, K.2    Hujer, A.M.3    Bonomo, R.A.4    Knox, J.R.5
  • 15
    • 0035122917 scopus 로고    scopus 로고
    • Predicting the emergence of antibiotic resistance by directed evolution and structural analysis
    • Orencia, M. C., Yoon, J. S., Ness, J. E., Stemmer, W. P., and Stevens, R. C. (2001) Predicting the emergence of antibiotic resistance by directed evolution and structural analysis. Nat. Struct. Biol. 8, 238-242.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 238-242
    • Orencia, M.C.1    Yoon, J.S.2    Ness, J.E.3    Stemmer, W.P.4    Stevens, R.C.5
  • 16
    • 24344498687 scopus 로고    scopus 로고
    • Current challenges in antimicrobial chemotherapy: The impact of extended-spectrum β-lactamases and metallo-β-lactamases on the treatment of resistant Gram-negative pathogens
    • Helfand, M. S., and Bonomo, R. A. (2005) Current challenges in antimicrobial chemotherapy: The impact of extended-spectrum β-lactamases and metallo-β-lactamases on the treatment of resistant Gram-negative pathogens. Curr. Opin. Pharmacol. 5, 452-458.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 452-458
    • Helfand, M.S.1    Bonomo, R.A.2
  • 17
    • 0345254956 scopus 로고    scopus 로고
    • Following the reactions of mechanism-based inhibitors with β-lactamase by Raman crystallography
    • Helfand, M. S., Totir, M. A., Carey, M. P., Hujer, A. M., Bonomo, R. A., and Carey, P. R. (2003) Following the reactions of mechanism-based inhibitors with β-lactamase by Raman crystallography. Biochemistry 42, 13386-13392.
    • (2003) Biochemistry , vol.42 , pp. 13386-13392
    • Helfand, M.S.1    Totir, M.A.2    Carey, M.P.3    Hujer, A.M.4    Bonomo, R.A.5    Carey, P.R.6
  • 18
    • 27144557330 scopus 로고    scopus 로고
    • High resolution crystal structures of the trans-enamine intermediates formed by sulbactam and clavulanic acid and E166A SHV-1 β-lactamase
    • Padayatti, P. S., Helfand, M. S., Totir, M. A., Carey, M. P., Carey, P. R., Bonomo, R. A., and van den Akker, F. (2005) High resolution crystal structures of the trans-enamine intermediates formed by sulbactam and clavulanic acid and E166A SHV-1 β-lactamase. J. Biol. Chem. 280, 34900-34907.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34900-34907
    • Padayatti, P.S.1    Helfand, M.S.2    Totir, M.A.3    Carey, M.P.4    Carey, P.R.5    Bonomo, R.A.6    Van Den Akker, F.7
  • 19
    • 0942290637 scopus 로고    scopus 로고
    • Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 β-lactamase: 1.63 Å crystal structure
    • Padayatti, P. S., Helfand, M. S., Totir, M. A., Carey, M. P., Hujer, A. M., Carey, P. R., Bonomo, R. A., and van den Akker, F. (2004) Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 β-lactamase: 1.63 Å crystal structure. Biochemistry 43, 843-848.
    • (2004) Biochemistry , vol.43 , pp. 843-848
    • Padayatti, P.S.1    Helfand, M.S.2    Totir, M.A.3    Carey, M.P.4    Hujer, A.M.5    Carey, P.R.6    Bonomo, R.A.7    Van Den Akker, F.8
  • 20
    • 33749349243 scopus 로고    scopus 로고
    • Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine β-lactamase intermediates
    • Totir, M. A., Padayatti, P. S., Helfand, M. S., Carey, M. P., Bonomo, R. A., Carey, P. R., and van den Akker, F. (2006) Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine β-lactamase intermediates. Biochemistry 45, 11895-11904.
    • (2006) Biochemistry , vol.45 , pp. 11895-11904
    • Totir, M.A.1    Padayatti, P.S.2    Helfand, M.S.3    Carey, M.P.4    Bonomo, R.A.5    Carey, P.R.6    Van Den Akker, F.7
  • 21
    • 0035810710 scopus 로고    scopus 로고
    • Mutagenesis of amino acid residues in the SHV-1 β-lactamase: The premier role of Gly238Ser in penicillin and cephalosporin resistance
    • Hujer, A. M., Hujer, K. M., and Bonomo, R. A. (2001) Mutagenesis of amino acid residues in the SHV-1 β-lactamase: The premier role of Gly238Ser in penicillin and cephalosporin resistance. Biochim. Biophys. Acta 1547, 37-50.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 37-50
    • Hujer, A.M.1    Hujer, K.M.2    Bonomo, R.A.3
  • 22
    • 33748632360 scopus 로고    scopus 로고
    • Spectroscopic characterization of distortion in enzyme complexes
    • Carey, P. R. (2006) Spectroscopic characterization of distortion in enzyme complexes. Chem. Rev. 106, 3043-3054.
    • (2006) Chem. Rev. , vol.106 , pp. 3043-3054
    • Carey, P.R.1
  • 23
    • 67849106903 scopus 로고    scopus 로고
    • Different intermediate populations formed by tazobactam, sulbactam, and clavulanate reacting with SHV-1 β-lactamases: Raman crystallographic evidence
    • Kalp, M., Totir, M. A., Buynak, J. D., and Carey, P. R. (2009) Different intermediate populations formed by tazobactam, sulbactam, and clavulanate reacting with SHV-1 β-lactamases: Raman crystallographic evidence. J. Am. Chem. Soc. 131, 2338-2347.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2338-2347
    • Kalp, M.1    Totir, M.A.2    Buynak, J.D.3    Carey, P.R.4
  • 25
    • 0027515959 scopus 로고
    • Kinetic interactions of tazobactam with β-lactamases from all major structural classes
    • Bush, K., Macalintal, C., Rasmussen, B. A., Lee, V. J., and Yang, Y. (1993) Kinetic interactions of tazobactam with β-lactamases from all major structural classes. Antimicrob. Agents Chemother. 37, 851-858.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 851-858
    • Bush, K.1    Macalintal, C.2    Rasmussen, B.A.3    Lee, V.J.4    Yang, Y.5
  • 26
    • 0018341962 scopus 로고
    • A semi-synthetic penicillinase inactivator
    • Cartwright, S. J., and Coulson, A. F. (1979) A semi-synthetic penicillinase inactivator. Nature 278, 360-361.
    • (1979) Nature , vol.278 , pp. 360-361
    • Cartwright, S.J.1    Coulson, A.F.2
  • 27
    • 0024542177 scopus 로고
    • Clavulanate inactivation of Staphylococcus aureus β-lactamase
    • Rizwi, I., Tan, A. K., Fink, A. L., and Virden, R. (1989) Clavulanate inactivation of Staphylococcus aureus β-lactamase. Biochem. J. 258, 205-209. (Pubitemid 19062271)
    • (1989) Biochemical Journal , vol.258 , Issue.1 , pp. 205-209
    • Rizwi, I.1    Tan, A.K.2    Fink, A.L.3    Virden, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.