메뉴 건너뛰기




Volumn 24, Issue 6, 1998, Pages 972-980

Selection strategy for site-directed mutagenesis based on altered β- lactamase specificity

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE;

EID: 0031749757     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/98246st03     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 2642590750 scopus 로고
    • Amino acid sequences of β-lactamases
    • J.M.T. Hamilton- Miller and J.T. Smith (Eds.), Academic Press, London
    • Ambler, R.P. 1979. Amino acid sequences of β-lactamases, p. 99-125. In J.M.T. Hamilton- Miller and J.T. Smith (Eds.), β-Lacatamse. Academic Press, London.
    • (1979) Β-Lacatamse , pp. 99-125
    • Ambler, R.P.1
  • 2
    • 0029829133 scopus 로고    scopus 로고
    • Selection and characterization of amino acid substitutions at residues 237-240 of TEM-I β-lactamase with altered substrate specificity for aztreonam and ceftazidime
    • Cantu, III, C., W. Huang and T. Palzkill. 1996. Selection and characterization of amino acid substitutions at residues 237-240 of TEM-I β-lactamase with altered substrate specificity for aztreonam and ceftazidime J. Biol. Chem. 271:22538-22545.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22538-22545
    • Cantu III, C.1    Huang, W.2    Palzkill, T.3
  • 3
    • 0026779284 scopus 로고
    • Site-directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase
    • Delaire, M., R. Labia, J.P. Samama and J.M. Masson. 1992. Site-directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase. J. Biol. Chem. 267:20600- 20606.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20600-20606
    • Delaire, M.1    Labia, R.2    Samama, J.P.3    Masson, J.M.4
  • 4
    • 0026052572 scopus 로고
    • Site-directed mutagenesis on TEM-1 β-lactamase: Role of Glu166 in catalysis and substrate binding
    • Delaire, M., M.F. Lenfant, R. Labia and J.M. Masson. 1991. Site-directed mutagenesis on TEM-1 β-lactamase: role of Glu166 in catalysis and substrate binding. Protein Eng. 4:805-810.
    • (1991) Protein Eng. , vol.4 , pp. 805-810
    • Delaire, M.1    Lenfant, M.F.2    Labia, R.3    Masson, J.M.4
  • 5
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W.P. and J.A. Nickoloff. 1992. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200:81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 6
    • 0028222371 scopus 로고
    • Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 β-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime
    • Imtiaz, U., E. Manavathu, S. Mobashery and S.A. Lerner. 1994. Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 β-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime. Antimicrob. Agents Chemother. 38:1134-1139.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1134-1139
    • Imtiaz, U.1    Manavathu, E.2    Mobashery, S.3    Lerner, S.A.4
  • 7
    • 0021687639 scopus 로고
    • Different base/base mismatches are corrected with different efficiences by the methyl-directed DNA mismatch repair system of E. coli
    • Kramer, B., W. Kramer and H.J. Fritz. 1984. Different base/base mismatches are corrected with different efficiences by the methyl-directed DNA mismatch repair system of E. coli. Cell 38:879-887.
    • (1984) Cell , vol.38 , pp. 879-887
    • Kramer, B.1    Kramer, W.2    Fritz, H.J.3
  • 8
    • 2642699794 scopus 로고
    • Rapid and efficient site- Specific mutagenesis without phenotypic selection
    • Kunkle, T.A. 1985. Rapid and efficient site- specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488- 492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkle, T.A.1
  • 10
    • 0029715645 scopus 로고    scopus 로고
    • Site-directed mutagenesis of double-stranded plasmids, domain substitution, and marker rescue by co-mutagenesis of restriction sites
    • A. Harwood (Ed.), Humana Press, Totowa, NJ
    • Nickoloff, J.A., E.M. Miller, W.P. Deng and F.A. Ray. 1996. Site-directed mutagenesis of double-stranded plasmids, domain substitution, and marker rescue by co-mutagenesis of restriction sites, p. 455-468. In A. Harwood (Ed.), Basic DNA and RNA Protocols. Humana Press, Totowa, NJ.
    • (1996) Basic DNA and RNA Protocols , pp. 455-468
    • Nickoloff, J.A.1    Miller, E.M.2    Deng, W.P.3    Ray, F.A.4
  • 11
    • 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
  • 12
    • 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: Structure, Function, Genetics 14:29-44.
    • (1992) Proteins: Structure, Function, Genetics , vol.14 , pp. 29-44
    • Palzkill, T.1    Botstein, D.2
  • 13
    • 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
  • 14
    • 0028896077 scopus 로고
    • Multiple substitutions at position 104 of β-lactamase TEM-1: Assessing the role of this residue in substrate specificity
    • Petit, A., L. Maveyraud, F. Lenfant, J.P. Samama, R. Labia and J.M. Masson. 1995. Multiple substitutions at position 104 of β-lactamase TEM-1: assessing the role of this residue in substrate specificity. Biochem. J. 305:33-40.
    • (1995) Biochem. J. , vol.305 , pp. 33-40
    • Petit, A.1    Maveyraud, L.2    Lenfant, F.3    Samama, J.P.4    Labia, R.5    Masson, J.M.6
  • 16
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W.P. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 17
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
    • Taylor, J.W., J. Ott and F. Eckstein. 1985. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Res. 73:8764-8785.
    • (1985) Nucleic Acids Res. , vol.73 , pp. 8764-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 18
    • 0004524478 scopus 로고    scopus 로고
    • Methods in molecular biology
    • Humana Press, Totowa, NJ
    • Trower, M.K. 1996. Methods in molecular biology, Vol. 57. In In Vitro Mutagenesis Protocols. Humana Press, Totowa, NJ.
    • (1996) Vitro Mutagenesis Protocols , vol.57
    • Trower, M.K.1
  • 19
    • 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. Hating, 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    Hating, W.2    Larocco, M.3    Palzkill, T.4
  • 20
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner, M.P., G.L. Costa, W. Schoettlin, J. Cline, E. Mathur and J.C. Bauer. 1994. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151:119-123.
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 21
    • 0023462730 scopus 로고
    • Site-specific mutagenesis and protein engineering
    • Zoller, M.J. and M. Smith. 1987. Site-specific mutagenesis and protein engineering. Methods Enzymol. 154:329-414.
    • (1987) Methods Enzymol. , vol.154 , pp. 329-414
    • Zoller, M.J.1    Smith, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.