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Volumn 178, Issue 7, 1996, Pages 1821-1828

Systematic mutagenesis of the active site omega loop of TEM-I β-lactamase

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEFTAZIDIME;

EID: 0029927342     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.7.1821-1828.1996     Document Type: Article
Times cited : (79)

References (36)
  • 1
    • 85042932791 scopus 로고
    • An enzyme from bacteria able to destroy penicillin
    • Abraham, E. P., and E. Chain. 1940. An enzyme from bacteria able to destroy penicillin. Nature (London) 1-46:837.
    • (1940) Nature (London) , vol.1-46 , pp. 837
    • Abraham, E.P.1    Chain, E.2
  • 2
    • 0025801845 scopus 로고
    • Site-directed mutants, at position 166. of RTEM-1 β-lactamase that form a stable acyl-enzyme intermediate with penicillin
    • Adachi, H., T. Ohta, and H. Matsuzawa. 1991 Site-directed mutants, at position 166. of RTEM-1 β-lactamase that form a stable acyl-enzyme intermediate with penicillin. Biol. Chem. 266:3186-3191.
    • (1991) Biol. Chem. , vol.266 , pp. 3186-3191
    • Adachi, H.1    Ohta, T.2    Matsuzawa, H.3
  • 5
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 6
    • 0025363874 scopus 로고
    • Patterns and mechanisms of β-lactam resistance among isolates of Escherichia coli from hospitals in the United States
    • Cooksey, R., J. Swenson, N. Clark, E. Gay, and C. Thornsberry. 1990. Patterns and mechanisms of β-lactam resistance among isolates of Escherichia coli from hospitals in the United States. Antimicrob. Agents Chemother. 34:739-745.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 739-745
    • Cooksey, R.1    Swenson, J.2    Clark, N.3    Gay, E.4    Thornsberry, C.5
  • 7
    • 0028986292 scopus 로고
    • TEM- and SHV-derived extended-spectrum beta-Lactamases: Relationship between selection, structure and function
    • Du Bois, S. K., M. S. Marriott, and S. G, B. Amyes. 1995. TEM- and SHV-derived extended-spectrum beta-Lactamases: relationship between selection, structure and function. J. Antimicrob. Chemother. 35:7-22.
    • (1995) J. Antimicrob. Chemother. , vol.35 , pp. 7-22
    • Du Bois, S.K.1    Marriott, M.S.2    Amyes, S.G.B.3
  • 8
    • 0026342155 scopus 로고
    • Site-directed mutagenesis of β-lactamase leading to accumulation of an acyl-enzyme intermediate
    • Escobar, W. A., A. K. Tan, and A. L. Fink. 1991 Site-directed mutagenesis of β-lactamase leading to accumulation of an acyl-enzyme intermediate. Biochemistry 30:10783-10787.
    • (1991) Biochemistry , vol.30 , pp. 10783-10787
    • Escobar, W.A.1    Tan, A.K.2    Fink, A.L.3
  • 9
    • 0019164846 scopus 로고
    • β-Lactamase proceeds via an acyl-enzyme intermediate: Interaction of Escherichia coli rTEM enzyme with cefoxitin
    • Fisher, J., J. Belasco, S. Khosla, and J. Knowles. 1980 β-Lactamase proceeds via an acyl-enzyme intermediate: interaction of Escherichia coli rTEM enzyme with cefoxitin. Biochemistry 19:2895-2901.
    • (1980) Biochemistry , vol.19 , pp. 2895-2901
    • Fisher, J.1    Belasco, J.2    Khosla, S.3    Knowles, J.4
  • 10
    • 0026016867 scopus 로고
    • Refined crystal structure of β-lactamase from 5 aureus at 2 a resolution
    • Herzberg, O. 1991. Refined crystal structure of β-lactamase from 5 aureus at 2 A resolution. J. Mol. Biol. 217:701-719.
    • (1991) J. Mol. Biol. , vol.217 , pp. 701-719
    • Herzberg, O.1
  • 11
    • 0025998489 scopus 로고
    • Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1
    • Herzberg, O., G. Kapadia, B. Blanco, T. S. Smith, and A. Coulson. 1991. Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1. Biochemistry 30:9503-9509.
    • (1991) Biochemistry , vol.30 , pp. 9503-9509
    • Herzberg, O.1    Kapadia, G.2    Blanco, B.3    Smith, T.S.4    Coulson, A.5
  • 12
    • 0027408874 scopus 로고
    • Role of Ser-238 and Lys-240 m the hydrolysis of third-generation cephalosporins by SHV-type β-lactamases probed by site-directed mutagenesis and three-dimensional modeling
    • Huletsky, A., J. R. Knox, and R. C. Levesque. 1993. Role of Ser-238 and Lys-240 m 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
  • 13
    • 0027275788 scopus 로고
    • Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 A resolution
    • Jelsch, C., L. Mourey, J.-M. Masson, and J.-P. Samama. 1993. Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 A resolution. Proteins 16:364-383.
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Masson, J.-M.3    Samama, J.-P.4
  • 14
    • 0021024916 scopus 로고
    • Transferable resistance to cefotaxime, cefoxitin, cefamandole, and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens
    • Knothe, H., P. Shah, V. Kremery, M. Antal, and S. Mitsuhashi. 1983. Transferable resistance to cefotaxime, cefoxitin, cefamandole, and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens. Infection 11:315-317.
    • (1983) Infection , vol.11 , pp. 315-317
    • Knothe, H.1    Shah, P.2    Kremery, V.3    Antal, M.4    Mitsuhashi, S.5
  • 15
    • 0025923511 scopus 로고
    • β-Lactamase of Bacillus licheniformis 749/C: Refinement at 2 a resolution and analysis of hydration
    • Knox, J. R., and P. C. Moews. 1991. β-Lactamase of Bacillus licheniformis 749/C: refinement at 2 A resolution and analysis of hydration J. Mol. Biol. 220:435-455.
    • (1991) J. Mol. Biol. , vol.220 , pp. 435-455
    • Knox, J.R.1    Moews, P.C.2
  • 16
    • 0026244229 scopus 로고
    • MOLSCRIPT a program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. 1991. MOLSCRIPT a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 17
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 18
  • 19
    • 0039591262 scopus 로고
    • Extracting information from protein sequences using random replacement mutagenesis
    • Palzkill, T., and D. Botstein. 1991. Extracting information from protein sequences using random replacement mutagenesis. Methods 3:155-164.
    • (1991) Methods , vol.3 , pp. 155-164
    • Palzkill, T.1    Botstein, D.2
  • 20
    • 0026703217 scopus 로고
    • Identification of amino acid substitutions that alter the substrate specificity of TEM-1 β-lactamase
    • Palzkill, T., and D. Botstein. 1992. Identification of amino acid substitutions that alter the substrate specificity of TEM-1 β-lactamase. J. Bacteriol. 174: 5237-5243.
    • (1992) J. Bacteriol. , vol.174 , pp. 5237-5243
    • Palzkill, T.1    Botstein, D.2
  • 21
    • 0026639254 scopus 로고
    • Probing β-lactamase structure and function using random replacement mutagenesis
    • Palzkill, T., and D. Botstein. 1992. Probing β-lactamase structure and function using random replacement mutagenesis. Proteins 14:29-44.
    • (1992) Proteins , vol.14 , pp. 29-44
    • Palzkill, T.1    Botstein, D.2
  • 22
    • 0028200978 scopus 로고
    • Evolution of antibiotic resistance: Several different amino acid substitutions in an active site loop alter the substrate profile of β-lactamase
    • Palzkill, T., Q.-Q. Le, K. V. Venkatachalam, M. LaRocco, and H. Ocera. 1994 Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of β-lactamase. Mol. Microbiol. 12:217-229.
    • (1994) Mol. Microbiol. , vol.12 , pp. 217-229
    • Palzkill, T.1    Le, Q.-Q.2    Venkatachalam, K.V.3    LaRocco, M.4    Ocera, H.5
  • 23
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its protcolytic susceptibility in Eschenchia coli
    • Parsell, D. A., and R. T. Sauer. 1959. The structural stability of a protein is an important determinant of its protcolytic susceptibility in Eschenchia coli. J. Biol Chem. 264:7590-7595.
    • (1959) J. Biol Chem. , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 25
    • 0028170640 scopus 로고
    • TEM beta-lactamase mutants hydrolysing third-generation cephalosporins - A kinetic and molecular modeling analysis
    • Raquet, X., J. Lamotte-Brasseur, E. Fonze, S. Goussard, P. Courvalin, and J. M. Frere. 1994. TEM beta-lactamase mutants hydrolysing third-generation cephalosporins - a kinetic and molecular modeling analysis J. Mol. Microbiol. 244:625-639
    • (1994) J. Mol. Microbiol. , vol.244 , pp. 625-639
    • Raquet, X.1    Lamotte-Brasseur, J.2    Fonze, E.3    Goussard, S.4    Courvalin, P.5    Frere, J.M.6
  • 26
    • 0022051393 scopus 로고
    • Frequency of plasmid-determined β-lactamases in 680 consecutively isolated strains of Enterobacteriaceae
    • Roy, C., C. Segura, M. Tirado, R. Reig, M. Hermida, D. Teruel, and A. Foz. 1985. Frequency of plasmid-determined β-lactamases in 680 consecutively isolated strains of Enterobacteriaceae Eur. J. Clin. Microbiol. 4:146-147.
    • (1985) Eur. J. Clin. Microbiol. , vol.4 , pp. 146-147
    • Roy, C.1    Segura, C.2    Tirado, M.3    Reig, R.4    Hermida, M.5    Teruel, D.6    Foz, A.7
  • 29
    • 0020057063 scopus 로고
    • Mutator mutations in Escherichia coli induced by the insertion of phage Mu and the transposable resistance elements Tn5 and Tn10
    • Siegel, E. C., S. L. Wain, S. F. Meltzer, M. L. Binon, and J. L. Steinberg. 1982. Mutator mutations in Escherichia coli induced by the insertion of phage Mu and the transposable resistance elements Tn5 and Tn10 Mutat. Res 93:25-33.
    • (1982) Mutat. Res , vol.93 , pp. 25-33
    • Siegel, E.C.1    Wain, S.L.2    Meltzer, S.F.3    Binon, M.L.4    Steinberg, J.L.5
  • 32
    • 0000845013 scopus 로고
    • Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBr322
    • Sutcliffe, J. G. 1978. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBr322. Proc. Natl. Acad. Sci. USA 75:3737-3741.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3737-3741
    • Sutcliffe, J.G.1
  • 35
    • 0029054787 scopus 로고
    • Probing the determinants of protein stability comparison of class A β-lactamases
    • Vanhove, M., S. Houba, J. Lamotte-Brasseur, and J.-M. Frere. 1995. Probing the determinants of protein stability comparison of class A β-lactamases Biochem. J. 308:859-864.
    • (1995) Biochem. J. , vol.308 , pp. 859-864
    • Vanhove, M.1    Houba, S.2    Lamotte-Brasseur, J.3    Frere, J.-M.4
  • 36
    • 0028168366 scopus 로고
    • Characterization of TEM-1 β-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime
    • Venkatachalam, K. V., W. Huang, M. LaRocco, and T. Palzkill. 1994 Characterization of TEM-1 β-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime. J. Biol. Chem. 269:23444-23450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23444-23450
    • Venkatachalam, K.V.1    Huang, W.2    LaRocco, M.3    Palzkill, T.4


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