메뉴 건너뛰기




Volumn 42, Issue 4, 1998, Pages 921-926

Overexpression, purification, and characterization of the cloned metallo-β-lactamase L1 from Stenotrophomonas maltophilia

Author keywords

[No Author keywords available]

Indexed keywords

6 (1 METHYL 1,2,3 TRIAZOL 4 YLMETHYLENE)PENEM 3 CARBOXYLIC ACID; AMPICILLIN; ANTIBIOTIC AGENT; BACTERIAL ENZYME; BETA LACTAM DERIVATIVE; BETA LACTAMASE; BIAPENEM; CEFACLOR; CEFADROXIL; CEFALORIDINE; CEFALOTIN; CEFEPIME; CEFMETAZOLE; CEFOTAXIME; CEFOXITIN; CEFPROZIL; CEFRADINE; CEFTIZOXIME; CEFUROXIME; CEPHALOSPORIN DERIVATIVE; CLAVULANIC ACID; MUTANT PROTEIN; NITROCEFIN; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; RECOMBINANT PROTEIN; TICARCILLIN; UNINDEXED DRUG; ZINC;

EID: 0031978726     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.4.921     Document Type: Article
Times cited : (166)

References (31)
  • 1
    • 0026520788 scopus 로고
    • Conjugal transfer of imipenem resistance in Bacteriodes fragilis
    • Bandoh, K., K. Watanabe, Y. Muto, Y. Tanaka, N. Kato, and K. Ueno. 1992. Conjugal transfer of imipenem resistance in Bacteriodes fragilis. J. Antibiot. 45:542-547.
    • (1992) J. Antibiot. , vol.45 , pp. 542-547
    • Bandoh, K.1    Watanabe, K.2    Muto, Y.3    Tanaka, Y.4    Kato, N.5    Ueno, K.6
  • 2
    • 0021952587 scopus 로고
    • The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275
    • Bicknell, R., E. L. Emanuel, J. Gagnon, and S. G. Waley. 1985. The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275. Biochem. J. 229:791-797.
    • (1985) Biochem. J. , vol.229 , pp. 791-797
    • Bicknell, R.1    Emanuel, E.L.2    Gagnon, J.3    Waley, S.G.4
  • 3
    • 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
  • 4
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi, A., S. Pares, E. Duee, M. Galleni, C. Duez, J. M. Frere, and O. Dideberg. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14:4914-4921.
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duee, E.3    Galleni, M.4    Duez, C.5    Frere, J.M.6    Dideberg, O.7
  • 5
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • Concha, N. O., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 6
    • 0029808391 scopus 로고    scopus 로고
    • Characterization of the metal binding sites of the β-lactamase from Bacteroides fragilis
    • Crowder, M. W., Z. Wang, S. L. Franklin, E. P. Zovinka, and S. J. Benkovic. 1996. Characterization of the metal binding sites of the β-lactamase from Bacteroides fragilis. Biochemistry 35:12126-12132.
    • (1996) Biochemistry , vol.35 , pp. 12126-12132
    • Crowder, M.W.1    Wang, Z.2    Franklin, S.L.3    Zovinka, E.P.4    Benkovic, S.J.5
  • 7
    • 0024043984 scopus 로고
    • Molecular cloning and expression of the imipenem-hydrolyzing β-lactamase gene from Pseudomonas maltophilia in Escherichia coli
    • Dufresne, J., G. Vezina, and R. C. Levesque. 1988. Molecular cloning and expression of the imipenem-hydrolyzing β-lactamase gene from Pseudomonas maltophilia in Escherichia coli. Rev. Infect. Dis. 10:806-817.
    • (1988) Rev. Infect. Dis. , vol.10 , pp. 806-817
    • Dufresne, J.1    Vezina, G.2    Levesque, R.C.3
  • 9
    • 0028837277 scopus 로고
    • Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases
    • Felici, A., and G. Amicosante. 1995. Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases. Antimicrob. Agents Chemother. 39:192-199.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 192-199
    • Felici, A.1    Amicosante, G.2
  • 14
    • 0029801962 scopus 로고    scopus 로고
    • Characterization of specific noncovalent protein complexes by UV matrix-assisted laser desorption ionization mass spectrometry
    • Glocker, M., S. H. J. Bauer, J. Kast, J. Volz, and M. Przybylski. 1996. Characterization of specific noncovalent protein complexes by UV matrix-assisted laser desorption ionization mass spectrometry. J. Mass Spectrometry 31:1221-1227.
    • (1996) J. Mass Spectrometry , vol.31 , pp. 1221-1227
    • Glocker, M.1    Bauer, S.H.J.2    Kast, J.3    Volz, J.4    Przybylski, M.5
  • 17
    • 0027966925 scopus 로고
    • Biochemical properties of inducible β-lactamases produced from Xanthomonas maltophilia
    • Paton, R., R. S. Miles, and S. G. B. Amyes. 1994. Biochemical properties of inducible β-lactamases produced from Xanthomonas maltophilia. Antimicrob. Agents Chemother. 38:2143-2149.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2143-2149
    • Paton, R.1    Miles, R.S.2    Amyes, S.G.B.3
  • 18
    • 0027284501 scopus 로고
    • Metallo-β-lactamases - A new therapeutic challenge
    • Payne, D. J. 1993. Metallo-β-lactamases - a new therapeutic challenge. J. Med. Microbiol. 39:93-99.
    • (1993) J. Med. Microbiol. , vol.39 , pp. 93-99
    • Payne, D.J.1
  • 21
    • 0029927028 scopus 로고    scopus 로고
    • The Aeromonas metallo-β-lactamases: Genetics, enzymology, and contribution to drug resistance
    • Rossolini, G. M., T. Walsh, and G. Amicosante. 1996. The Aeromonas metallo-β-lactamases: genetics, enzymology, and contribution to drug resistance. Microb. Drug Resist. 2:245-252.
    • (1996) Microb. Drug Resist. , vol.2 , pp. 245-252
    • Rossolini, G.M.1    Walsh, T.2    Amicosante, G.3
  • 22
    • 0020370569 scopus 로고
    • Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia
    • Saino, Y., F. Kobayashi, M. Inoue, and S. Mitsuhashi. 1982. Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia. Antimicrob. Agents Chemother. 22:564-570.
    • (1982) Antimicrob. Agents Chemother. , vol.22 , pp. 564-570
    • Saino, Y.1    Kobayashi, F.2    Inoue, M.3    Mitsuhashi, S.4
  • 23
    • 0003518480 scopus 로고
    • John Wiley and Sons, Inc., New York, N.Y.
    • Segel, I. H. 1993. Enzyme kinetics. John Wiley and Sons, Inc., New York, N.Y.
    • (1993) Enzyme Kinetics
    • Segel, I.H.1
  • 24
    • 0030071472 scopus 로고    scopus 로고
    • Multifocal outbreaks of metallo-β-lactamase producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems
    • Senda, K., Y. Arakawa, K. Nakashima, H. Ito, S. Ichiyama, K. Shimokata, N. Kato, and M. Ohta. 1996. Multifocal outbreaks of metallo-β-lactamase producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems. Antimicrob. Agents Chemother. 40:349-353.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 349-353
    • Senda, K.1    Arakawa, Y.2    Nakashima, K.3    Ito, H.4    Ichiyama, S.5    Shimokata, K.6    Kato, N.7    Ohta, M.8
  • 25
    • 85054116916 scopus 로고    scopus 로고
    • Unpublished data
    • 24a. Spencer, J. Unpublished data.
    • Spencer, J.1
  • 27
    • 0025803775 scopus 로고
    • Spectroscopic and kinetics studies of a high-salt stabilized form of the purple acid phosphatase from bovine spleen
    • Vincent, J. B., M. W. Crowder, and B. A. Averill. 1991. Spectroscopic and kinetics studies of a high-salt stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry 30:3025-3034.
    • (1991) Biochemistry , vol.30 , pp. 3025-3034
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 31
    • 0026651129 scopus 로고
    • Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636
    • Yang, Y., B. A. Rasmussen, and K. Bush. 1992. Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636. Antimicrob. Agents Chemother. 36:1155-1157.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1155-1157
    • Yang, Y.1    Rasmussen, B.A.2    Bush, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.