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Volumn 61, Issue 4, 2008, Pages 792-797

Structure - Function studies of arginine at position 276 in CTX-M β-lactamases

Author keywords

lactamase inhibition; Cefotaxime hydrolysis; Clavulanate

Indexed keywords

AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; ARGININE; ASPARAGINE; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE INHIBITOR; CEFALOTIN; CEFEPIME; CEFOTAXIME; CEFTAZIDIME; CEFUROXIME; CLAVULANIC ACID; CYSTEINE; EXTENDED SPECTRUM BETA LACTAMASE; GLYCINE; HISTIDINE; IMIPENEM; NITROCEFIN; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; SERINE; TRYPTOPHAN;

EID: 41149170260     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkn031     Document Type: Article
Times cited : (21)

References (23)
  • 1
    • 0347362476 scopus 로고    scopus 로고
    • Growing group of extended-spectrum β-lactamases: The CTX-M enzymes
    • Bonnet R. Growing group of extended-spectrum β-lactamases: The CTX-M enzymes. Antimicrob Agents Chemother 2004; 48: 1-14.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1-14
    • Bonnet, R.1
  • 2
    • 0035191066 scopus 로고    scopus 로고
    • CTX-M-type extended-spectrum β-lactamase that hydrolyzes ceftazidime through a single amino acid substitution in the omega loop
    • Poirel L, Naas T, Le Thomas I et al. CTX-M-type extended-spectrum β-lactamase that hydrolyzes ceftazidime through a single amino acid substitution in the omega loop. Antimicrob Agents Chemother 2001; 45: 3355-61.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3355-3361
    • Poirel, L.1    Naas, T.2    Le Thomas, I.3
  • 3
    • 0034913238 scopus 로고    scopus 로고
    • Novel cefotaximase (CTX-M-16) with increased catalytic efficiency due to substitution Asp-240→Gly
    • Bonnet R, Dutour C, Sampaio JL et al. Novel cefotaximase (CTX-M-16) with increased catalytic efficiency due to substitution Asp-240→Gly. Antimicrob Agents Chemother 2001; 8: 2269-75.
    • (2001) Antimicrob Agents Chemother , vol.8 , pp. 2269-2275
    • Bonnet, R.1    Dutour, C.2    Sampaio, J.L.3
  • 4
    • 0037587290 scopus 로고    scopus 로고
    • Effect of D240G substitution in a novel ESBL CTX-M-27
    • Bonnet R, Recule C, Baraduc R et al. Effect of D240G substitution in a novel ESBL CTX-M-27. J Antimicrob Chemother 2003; 52: 29-35.
    • (2003) J Antimicrob Chemother , vol.52 , pp. 29-35
    • Bonnet, R.1    Recule, C.2    Baraduc, R.3
  • 5
    • 2542495992 scopus 로고    scopus 로고
    • High-level resistance to ceftazidime conferred by a novel enzyme, CTX-M-32, derived from CTX-M-1 through a single Asp240-Gly substitution
    • Cartelle M, Tomas M, Molina F et al. High-level resistance to ceftazidime conferred by a novel enzyme, CTX-M-32, derived from CTX-M-1 through a single Asp240-Gly substitution. Antimicrob Agents Chemother 2004; 48: 2308-13.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2308-2313
    • Cartelle, M.1    Tomas, M.2    Molina, F.3
  • 6
    • 31944442275 scopus 로고    scopus 로고
    • Prediction of the evolution of ceftazidime resistance in extended-spectrum β-lactamase CTX-M-9
    • Delmas J, Robin F, Carvalho F et al. Prediction of the evolution of ceftazidime resistance in extended-spectrum β-lactamase CTX-M-9. Antimicrob Agents Chemother 2006; 50: 731-8.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 731-738
    • Delmas, J.1    Robin, F.2    Carvalho, F.3
  • 7
    • 0032816956 scopus 로고    scopus 로고
    • Construction and characterization of mutants of the TEM-1 β-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to β-lactamase inhibitors
    • Stapleton PD, Shannon KP, French GL. Construction and characterization of mutants of the TEM-1 β-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to β-lactamase inhibitors. Antimicrob Agents Chemother 1999; 43 1881-7.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1881-1887
    • Stapleton, P.D.1    Shannon, K.P.2    French, G.L.3
  • 8
    • 17144463688 scopus 로고    scopus 로고
    • Amino acid substitutions causing inhibitor resistance in TEM β-lactamases compromise the extended-spectrum phenotype in SHV extended-spectrum β-lactamases
    • Randegger CC, Hachler H. Amino acid substitutions causing inhibitor resistance in TEM β-lactamases compromise the extended-spectrum phenotype in SHV extended-spectrum β-lactamases. J Antimicrob Chemother 2001; 47: 547-54.
    • (2001) J Antimicrob Chemother , vol.47 , pp. 547-554
    • Randegger, C.C.1    Hachler, H.2
  • 9
    • 0032466176 scopus 로고    scopus 로고
    • Effect of substitution of Asn for Arg-276 in the cefotaxime-hydrolyzing class A β-lactamase CTX-M-4
    • Gazouli M, Legakis NJ, Tzouvelekis LS. Effect of substitution of Asn for Arg-276 in the cefotaxime-hydrolyzing class A β-lactamase CTX-M-4. FEMS Microbiol Lett 1998; 169: 289-93.
    • (1998) FEMS Microbiol Lett , vol.169 , pp. 289-293
    • Gazouli, M.1    Legakis, N.J.2    Tzouvelekis, L.S.3
  • 10
    • 0028821830 scopus 로고
    • Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure
    • Knox JR. Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure. Antimicrob Agents Chemother 1995; 39: 2593-601.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 2593-2601
    • Knox, J.R.1
  • 11
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M β-lactamases: Extended spectrum activities from increased mobility and decreased stability
    • Chen Y, Delmas J, Sirot T et al. Atomic resolution structures of CTX-M β-lactamases: Extended spectrum activities from increased mobility and decreased stability. J Mol Biol 2005; 348: 349-62.
    • (2005) J Mol Biol , vol.348 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, T.3
  • 12
    • 0033525223 scopus 로고    scopus 로고
    • Crystal structure of the E166A mutant of extended-spectrum β-lactamase Toho-1 at 1.8 Å resolution
    • Ibuka A, Taguchi A, Ishiguro M et al. Crystal structure of the E166A mutant of extended-spectrum β-lactamase Toho-1 at 1.8 Å resolution. J Mol Biol 1999; 285: 2079-87.
    • (1999) J Mol Biol , vol.285 , pp. 2079-2087
    • Ibuka, A.1    Taguchi, A.2    Ishiguro, M.3
  • 13
    • 0026534561 scopus 로고
    • β-Lactamase TEM1 of E. coli crystal structure determination at 2.5 Å resolution
    • Jelsch C, Lenfant F, Masson JM et al. β-Lactamase TEM1 of E. coli crystal structure determination at 2.5 Å resolution. FEBS Lett 1992; 299: 135-42.
    • (1992) FEBS Lett , vol.299 , pp. 135-142
    • Jelsch, C.1    Lenfant, F.2    Masson, J.M.3
  • 14
    • 0034763241 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases in the 21st century: Characterization, epidemiology, and detection of this important resistance threat
    • Bradford PA. Extended-spectrum β-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat. Clin Microbiol Rev 2001; 14: 933-51.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 933-951
    • Bradford, P.A.1
  • 15
    • 0343686104 scopus 로고    scopus 로고
    • Inhibitor-resistant TEM β-lactamases: Phenotypic, genetic and biochemical characteristics
    • Chaibi EB, Sirot D, Paul G et al. Inhibitor-resistant TEM β-lactamases: Phenotypic, genetic and biochemical characteristics. J Antimicrob Chemother 1999; 43: 447-58.
    • (1999) J Antimicrob Chemother , vol.43 , pp. 447-458
    • Chaibi, E.B.1    Sirot, D.2    Paul, G.3
  • 16
    • 0041421234 scopus 로고    scopus 로고
    • Effects of Ser130Gly and Asp240Lys substitutions in extended-spectrum β-lactamase CTX-M-9
    • Aumeran C, Chanal C, Labia R et al. Effects of Ser130Gly and Asp240Lys substitutions in extended-spectrum β-lactamase CTX-M-9. Antimicrob Agents Chemother 2003; 47: 2958-61.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2958-2961
    • Aumeran, C.1    Chanal, C.2    Labia, R.3
  • 17
    • 0031979654 scopus 로고    scopus 로고
    • Sequence of the gene encoding a plasmid-mediated cefotaxime-hydrolyzing class A β-lactamase (CTX-M-4): Involvement of serine 237 in cephalosporin hydrolysis
    • Gazouli M, Tzelepi E, Sidorenko SV et al. Sequence of the gene encoding a plasmid-mediated cefotaxime-hydrolyzing class A β-lactamase (CTX-M-4): Involvement of serine 237 in cephalosporin hydrolysis. Antimicrob Agents Chemother 1998; 42: 1259-62.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1259-1262
    • Gazouli, M.1    Tzelepi, E.2    Sidorenko, S.V.3
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM et al. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989; 77: 51-9.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3
  • 19
    • 0028303746 scopus 로고
    • Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory β-lactam compounds
    • Galleni M, Francecchini N, Quinting B et al. Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory β-lactam compounds. Antimicrob Agents Chemother 1994; 38: 1608-14.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1608-1614
    • Galleni, M.1    Francecchini, N.2    Quinting, B.3
  • 20
    • 0031009295 scopus 로고    scopus 로고
    • A complex mutant of TEM-1 β-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate
    • Sirot D, Recule C, Chaibi EB et al. A complex mutant of TEM-1 β-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate. Antimicrob Agents Chemother 1997; 41: 1322-5.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1322-1325
    • Sirot, D.1    Recule, C.2    Chaibi, E.B.3
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991; 24: 946-50.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ. Raster 3D: Photorealistic molecular graphics. Methods Enzymol 1997; 277: 505-24.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 23
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, Adams PD, Clore GM et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998; 54: 905-21.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.