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Volumn 41, Issue 9, 1997, Pages 1940-1943

Construction and characterization of an OHIO-1 β-lactamase bearing Met69Ile and Gly238Ser mutations

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CEFOTAXIME; CEFTAZIDIME; CLAVULANIC ACID; SULBACTAM;

EID: 0030875916     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.41.9.1940     Document Type: Article
Times cited : (11)

References (28)
  • 2
    • 0027370236 scopus 로고
    • Characterization of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli
    • Blazquez, J., M. R. Baquero, R. Canton, I. Alos, and F. Baquero. 1993. Characterization of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli. Antimicrob. Agents Chemother. 37:2059-2063.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2059-2063
    • Blazquez, J.1    Baquero, M.R.2    Canton, R.3    Alos, I.4    Baquero, F.5
  • 4
    • 0028985358 scopus 로고
    • β-Lactamase mutations far from the active site influence inhibitor binding
    • Bonomo, R. A., C. G. Dawes, J. R. Knox, and D. M. Shlaes. 1995. β-Lactamase mutations far from the active site influence inhibitor binding. Biochem. Biophys. Acta 1247:121-125.
    • (1995) Biochem. Biophys. Acta , vol.1247 , pp. 121-125
    • Bonomo, R.A.1    Dawes, C.G.2    Knox, J.R.3    Shlaes, D.M.4
  • 5
    • 0028954421 scopus 로고
    • Complementary roles of mutations at positions 69 and 242 in a class A β-lactamase
    • Bonomo, R. A., C. G. Dawes, J. R. Knox, and D. M. Shlaes. 1995. Complementary roles of mutations at positions 69 and 242 in a class A β-lactamase. Biochem. Biophys. Acta 1247:113-120.
    • (1995) Biochem. Biophys. Acta , vol.1247 , pp. 113-120
    • Bonomo, R.A.1    Dawes, C.G.2    Knox, J.R.3    Shlaes, D.M.4
  • 7
    • 0028246175 scopus 로고
    • Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with decreased susceptibility to β-lactamase inhibitors
    • Brun, T., J. Peduzzi, M. M. Canica, G. Paul, P. Nevot, M. Barthelemy, and R. Labia. 1994. Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with decreased susceptibility to β-lactamase inhibitors. FEMS Microbiol. Lett. 120:111-117.
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 111-117
    • Brun, T.1    Peduzzi, J.2    Canica, M.M.3    Paul, G.4    Nevot, P.5    Barthelemy, M.6    Labia, R.7
  • 8
    • 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
  • 9
    • 0025027840 scopus 로고
    • Molecular evolution of ubiquitous β-lactamases towards extended-spectrum enzymes active against newer β-lactam antibiotics
    • Collatz, E., R. Labia, and L. Gutmann. 1990. Molecular evolution of ubiquitous β-lactamases towards extended-spectrum enzymes active against newer β-lactam antibiotics. Mol. Microbiol. 4:1615-1620.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1615-1620
    • Collatz, E.1    Labia, R.2    Gutmann, L.3
  • 10
    • 0028798040 scopus 로고
    • Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli
    • Henquell, C., C. Chanal, D. Sirot, R. Labia, and J. Sirot. 1995. Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli. Antimicrob. Agents Chemother. 39:427-430.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 427-430
    • Henquell, C.1    Chanal, C.2    Sirot, D.3    Labia, R.4    Sirot, J.5
  • 11
    • 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., J. R. Knox, and R. C. Levesque. 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
  • 12
    • 0027316253 scopus 로고
    • Inactivation of class A β-lactamases by clavulanic acid: The role of arginine-244 in a proposed nonconcerted sequence of events
    • Imtiaz, U., E. Billings, J. R. Knox, E. K. Manavathu, S. A. Lerner, and S. Mobashery. 1993. Inactivation of class A β-lactamases by clavulanic acid: the role of arginine-244 in a proposed nonconcerted sequence of events. J. Am. Chem. Soc. 115:4435-4442.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4435-4442
    • Imtiaz, U.1    Billings, E.2    Knox, J.R.3    Manavathu, E.K.4    Lerner, S.A.5    Mobashery, S.6
  • 13
    • 0028357710 scopus 로고
    • A structure-based analysis of the inhibition of class A β-lactamases by sulbactam
    • Imtiaz, U., E. M. Billings, J. R. Knox, and S. Mobashery. 1994. A structure-based analysis of the inhibition of class A β-lactamases by sulbactam. Biochemistry 33:5728-5738.
    • (1994) Biochemistry , vol.33 , pp. 5728-5738
    • Imtiaz, U.1    Billings, E.M.2    Knox, J.R.3    Mobashery, S.4
  • 14
    • 0343011735 scopus 로고
    • Crystallography of penicillin-building enzymes
    • P. H. Bentley and R. Pondsford (ed.), Special Publication 119. Royal Society of Chemistry, London, United Kingdom
    • Knox, J. R. 1993. Crystallography of penicillin-building enzymes, p. 36-49. In P. H. Bentley and R. Pondsford (ed.), Recent advances in the chemistry of anti-infective agents. Special Publication 119. Royal Society of Chemistry, London, United Kingdom.
    • (1993) Recent Advances in the Chemistry of Anti-infective Agents , pp. 36-49
    • Knox, J.R.1
  • 15
    • 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
  • 16
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zkour. 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    Zkour, R.A.3
  • 17
    • 0028802117 scopus 로고
    • Contribution of mutant analysis to the understanding of enzyme catalysis: The case of class A β-lactamases
    • Matagne, A., and J. M. Frere. 1995. Contribution of mutant analysis to the understanding of enzyme catalysis: the case of class A β-lactamases. Biochem. Biophys. Acta 1247:109-127.
    • (1995) Biochem. Biophys. Acta , vol.1247 , pp. 109-127
    • Matagne, A.1    Frere, J.M.2
  • 18
    • 0024625363 scopus 로고
    • Efficient site-directed in vitro mutagenesis using phagemid vectors
    • McClary, J. A., F. Whitney, and J. Geisselsoder. 1989. Efficient site-directed in vitro mutagenesis using phagemid vectors. BioTechniques 7:282-287.
    • (1989) BioTechniques , vol.7 , pp. 282-287
    • McClary, J.A.1    Whitney, F.2    Geisselsoder, J.3
  • 19
    • 0028170640 scopus 로고
    • TEM β-lactamase mutants hydrolyzing third-generation cephalosporins. A kinetic and molecular modelling analysis
    • Raquet, X., J. Lamotte-Brasseur, E. Fonze, S. Goussard, P. Courvalin, and J. M. Frere. 1994. TEM β-lactamase mutants hydrolyzing third-generation cephalosporins. A kinetic and molecular modelling analysis. J. Mol. Biol. 244:625-639.
    • (1994) J. Mol. Biol. , 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
  • 20
    • 0029120340 scopus 로고
    • The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid
    • Saves, I., D. Burlet-Schiltz, P. Swaren, F. Lefevre, J.-M. Masson, J.-C. Prome, and J. P. Samama. 1995. The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid. J. Biol. Chem. 31:18240-18245.
    • (1995) J. Biol. Chem. , vol.31 , pp. 18240-18245
    • Saves, I.1    Burlet-Schiltz, D.2    Swaren, P.3    Lefevre, F.4    Masson, J.-M.5    Prome, J.-C.6    Samama, J.P.7
  • 21
    • 0026748177 scopus 로고
    • Mutations altering substrate specificity in OHIO-1, an SHV-1 family β-lactamase
    • Shlaes, D. M., and C. Currie-McCumber. 1992. Mutations altering substrate specificity in OHIO-1, an SHV-1 family β-lactamase. Biochem. J. 284:411-415.
    • (1992) Biochem. J. , vol.284 , pp. 411-415
    • Shlaes, D.M.1    Currie-McCumber, C.2
  • 23
    • 0028894848 scopus 로고
    • Incidence and mechanisms of resistance to the combination of amoxicillin and clavulanic acid in Escherichia coli
    • Stapleton, P., P.-J. Wu, A. King, K. Shannon, G. French, and I. Phillips. 1995. Incidence and mechanisms of resistance to the combination of amoxicillin and clavulanic acid in Escherichia coli. Antimicrob. Agents Chemother. 39:2478-2483.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2478-2483
    • Stapleton, P.1    Wu, P.-J.2    King, A.3    Shannon, K.4    French, G.5    Phillips, I.6
  • 24
    • 0026828204 scopus 로고
    • TRC-1: Emergence of a clavulanic acid-resistant TEM-β-lactamase in a clinical strain
    • Thomson, C. J., and S. G. B. Amyes. 1992. TRC-1: emergence of a clavulanic acid-resistant TEM-β-lactamase in a clinical strain. FEMS Microbiol. Lett. 70:113-117.
    • (1992) FEMS Microbiol. Lett. , vol.70 , pp. 113-117
    • Thomson, C.J.1    Amyes, S.G.B.2
  • 25
    • 0026437823 scopus 로고
    • Clinical isolates of Escherichia coli producing TRI β-lactamases: Novel TEM-enzymes conferring resistance to β-lactamase inhibitors
    • Vedel, G., A. Belaaouaj, L. Gilly, R. Labia, A. Phillipon, P. Nevot, and G. Paul. 1992. Clinical isolates of Escherichia coli producing TRI β-lactamases: novel TEM-enzymes conferring resistance to β-lactamase inhibitors. J. Antimicrob. Chemother. 30:449-462.
    • (1992) J. Antimicrob. Chemother. , vol.30 , pp. 449-462
    • Vedel, G.1    Belaaouaj, A.2    Gilly, L.3    Labia, R.4    Phillipon, A.5    Nevot, P.6    Paul, G.7
  • 26
    • 0028168366 scopus 로고
    • Characterization of TEM-1 β-lactamase mutants from positions 238 and 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 and 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
  • 27
    • 0026654218 scopus 로고
    • Elucidation of the role of arginine-244 in the turnover processes of class A β-lactamases
    • Zafaralla, G., S. Manavathu, S. A. Lerner, and S. Mobashery. 1992. Elucidation of the role of arginine-244 in the turnover processes of class A β-lactamases. Biochemistry 31:3847-3852.
    • (1992) Biochemistry , vol.31 , pp. 3847-3852
    • Zafaralla, G.1    Manavathu, S.2    Lerner, S.A.3    Mobashery, S.4
  • 28
    • 0028302091 scopus 로고
    • Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistance to β-lactamase inhibitors
    • Zhou, X. Y., F. Bordon, D. Sirot, M.-D. Kitzis, and L. Gutmann. 1994. Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistance to β-lactamase inhibitors. Antimicrob. Agents Chemother. 38:1085-1089.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1085-1089
    • Zhou, X.Y.1    Bordon, F.2    Sirot, D.3    Kitzis, M.-D.4    Gutmann, L.5


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