메뉴 건너뛰기




Volumn 263, Issue 2, 1999, Pages 478-485

Terminal truncations in Amp C β-lactamase from a clinical isolate of Pseudomonas aeruginosa

Author keywords

lactamase; C terminal truncation; N terminal truncation; pI different variants

Indexed keywords

ALANINE; ARGININE; BACTERIAL ENZYME; BETA LACTAMASE;

EID: 0033565729     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00529.x     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0019326853 scopus 로고
    • The structure of β-lactamases
    • 1. Ambler, R.P. (1980) The structure of β-lactamases. Phil. Trans. R. Soc. Lond. 289, 321-331.
    • (1980) Phil. Trans. R. Soc. Lond. , vol.289 , pp. 321-331
    • Ambler, R.P.1
  • 2
    • 0000908299 scopus 로고
    • AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of β-lactamases of the penicillinase type
    • 2. Jaurin, B. & Grundström, T. (1981) AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of β-lactamases of the penicillinase type. Proc. Natl Acad. Sci. USA 78, 4897-4901.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4897-4901
    • Jaurin, B.1    Grundström, T.2
  • 3
    • 0022401654 scopus 로고
    • Sequence of the OXA-2 β-lactamase: Comparison with other penicillin-reactive enzymes
    • 3. Dale, J.W., Godwin, D., Mossakowska, D., Stephenson, P. & Wall, S. (1985) Sequence of the OXA-2 β-lactamase: comparison with other penicillin-reactive enzymes. FEBS Lett. 191, 39-44.
    • (1985) FEBS Lett. , vol.191 , pp. 39-44
    • Dale, J.W.1    Godwin, D.2    Mossakowska, D.3    Stephenson, P.4    Wall, S.5
  • 4
    • 0028032168 scopus 로고
    • Sequence analysis of PER-1 extended-spectrum β-lactamase from Pseudomonas aeruginosa and comparison with class A β-lactamases
    • 4. Nordmann, P. & Naas, T. (1994) Sequence analysis of PER-1 extended-spectrum β-lactamase from Pseudomonas aeruginosa and comparison with class A β-lactamases. Antimicrob. Agents Chemother. 38, 104-114.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 104-114
    • Nordmann, P.1    Naas, T.2
  • 5
  • 6
    • 0025600978 scopus 로고
    • Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC β-lactamase
    • 6. Lodge, J.M., Minchin, S.D., Piddock, L.J.V. & Busby, J.W. (1990) Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC β-lactamase. Biochem. J. 272, 627-631.
    • (1990) Biochem. J. , vol.272 , pp. 627-631
    • Lodge, J.M.1    Minchin, S.D.2    Piddock, L.J.V.3    Busby, J.W.4
  • 7
    • 0030939635 scopus 로고    scopus 로고
    • OXA-15, an extended-spectrum variant of OXA-2 β-lactamase isolated from a Pseudomonas aeruginosa strain
    • 7. Danel, F., Hall, L.M.C., Gur, D. & Livermore, D.M. (1997) OXA-15, an extended-spectrum variant of OXA-2 β-lactamase isolated from a Pseudomonas aeruginosa strain. Antimicrob. Agents Chemother. 41, 785-790.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 785-790
    • Danel, F.1    Hall, L.M.C.2    Gur, D.3    Livermore, D.M.4
  • 8
    • 0017134749 scopus 로고
    • Identification of β-lactamases by analytical isoelectric focusing: Correlation with bacterial taxonomy
    • 8. Matthew, M. & Harris, A.M. (1976) Identification of β-lactamases by analytical isoelectric focusing: correlation with bacterial taxonomy. J. Gen. Microbiol. 94, 55-67.
    • (1976) J. Gen. Microbiol. , vol.94 , pp. 55-67
    • Matthew, M.1    Harris, A.M.2
  • 9
    • 0023798518 scopus 로고
    • Heterogeneity of class I β-lactamase expression in clinical isolates of Pseudomonas aeruginosa
    • 9. Sanders, C.C., Gates, M.L. & Sanders, W.E. Jr (1988) Heterogeneity of class I β-lactamase expression in clinical isolates of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 32, 1893-1895.
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1893-1895
    • Sanders, C.C.1    Gates, M.L.2    Sanders W.E., Jr.3
  • 10
    • 0027716709 scopus 로고
    • Evaluation of five different methods to prepare bacterial extracts for the identification of β-lactamases by isoelectric focusing
    • 10. Arstila, T., Jacoby, G.A. & Huovinen, P. (1993) Evaluation of five different methods to prepare bacterial extracts for the identification of β-lactamases by isoelectric focusing. J. Antimicrob. Chemother. 32, 809-816.
    • (1993) J. Antimicrob. Chemother. , vol.32 , pp. 809-816
    • Arstila, T.1    Jacoby, G.A.2    Huovinen, P.3
  • 12
    • 0026086673 scopus 로고
    • Ragged N-termini and other variants of class A β-lactamases analysed by chromatofocusing
    • 12. Matagne, A., Joris, B., van Beeumen, J. & Frère, J.-M. (1991) Ragged N-termini and other variants of class A β-lactamases analysed by chromatofocusing. Biochem. J. 273, 503-510.
    • (1991) Biochem. J. , vol.273 , pp. 503-510
    • Matagne, A.1    Joris, B.2    Van Beeumen, J.3    Frère, J.-M.4
  • 14
    • 0017709583 scopus 로고
    • Microheterogeneity of plasmid coded β-lactamases in isoelectric focusing
    • 14. Brive, C., Barthélémy, M., Bouanchaud, D.H. & Labia, R. (1977) Microheterogeneity of plasmid coded β-lactamases in isoelectric focusing. Ann. Microbiol. 128B, 309-317.
    • (1977) Ann. Microbiol. , vol.128 B , pp. 309-317
    • Brive, C.1    Barthélémy, M.2    Bouanchaud, D.H.3    Labia, R.4
  • 15
    • 0016139742 scopus 로고
    • R-factor-mediated β-lactamases that hydrolyze oxacillin: Evidence for two distinct groups
    • 15. Dale, J.W. & Smith, J.T. (1974) R-factor-mediated β-lactamases that hydrolyze oxacillin: evidence for two distinct groups. J. Bacteriol. 119, 351-356.
    • (1974) J. Bacteriol. , vol.119 , pp. 351-356
    • Dale, J.W.1    Smith, J.T.2
  • 16
    • 0020965793 scopus 로고
    • The origin and properties of β-lactamase satellite hands seen in isoelectric focusing
    • 16. Simpson, I.N. & Plested, S.J. (1983) The origin and properties of β-lactamase satellite hands seen in isoelectric focusing. J. Antimicrob. Chemother. 12, 127-131.
    • (1983) J. Antimicrob. Chemother. , vol.12 , pp. 127-131
    • Simpson, I.N.1    Plested, S.J.2
  • 17
    • 0022509039 scopus 로고
    • Evidence for multiple forms of type I chromosomal β-lactamases in Pseudomonas aeruginosa
    • 17. Gates, M.L., Sanders, C.C., Goering, R.V. & Sanders, W.E. Jr (1986) Evidence for multiple forms of type I chromosomal β-lactamases in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 30, 453-457.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 453-457
    • Gates, M.L.1    Sanders, C.C.2    Goering, R.V.3    Sanders W.E., Jr.4
  • 20
    • 0030976201 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa isolates from patients with cystic fibrosis have different β-lactamase expression phenotypes but are homogeneous in the ampC-ampR genetic region
    • 20. Campbell, J.I.A., Ciofu, O. & Hoiby, N. (1997) Pseudomonas aeruginosa isolates from patients with cystic fibrosis have different β-lactamase expression phenotypes but are homogeneous in the ampC-ampR genetic region. Antimicrob. Agents Chemother. 41, 1380-1384.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1380-1384
    • Campbell, J.I.A.1    Ciofu, O.2    Hoiby, N.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 21. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • 22. Morrissey, J.H. (1981) Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117, 307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 23
    • 0015878020 scopus 로고
    • Immunization, isolation of immunoglobulins, estimation of antibody titre
    • Axelsen, N.H., Krøll, J. & Weeke, B., eds, Universitetsforlaget, Oslo
    • 23. Harboe, N. & Ingild, A. (1973) Immunization, isolation of immunoglobulins, estimation of antibody titre. In A Manual of Quantitative Immunoelectrophoresis. Methods and Applications (Axelsen, N.H., Krøll, J. & Weeke, B., eds), pp. 161-164. Universitetsforlaget, Oslo.
    • (1973) A Manual of Quantitative Immunoelectrophoresis. Methods and Applications , pp. 161-164
    • Harboe, N.1    Ingild, A.2
  • 24
    • 0024492170 scopus 로고
    • Immunoblotting techniques with picogram sensitivity in cerebrospinal fluid protein detection
    • 24. Nespolo, A., Bianchi, G., Salmaggi, A., Lazzaroni, M., Cerrato, D. & Tajoli, L.M. (1989) Immunoblotting techniques with picogram sensitivity in cerebrospinal fluid protein detection. Electrophoresis 10, 34-40.
    • (1989) Electrophoresis , vol.10 , pp. 34-40
    • Nespolo, A.1    Bianchi, G.2    Salmaggi, A.3    Lazzaroni, M.4    Cerrato, D.5    Tajoli, L.M.6
  • 25
    • 0009576261 scopus 로고
    • Colloidal metal staining of blots
    • Bjerrum, O.J. & Heegaard, N.H.H., eds, CRC Press, Inc., Orlando
    • 25. Moeremans, M., Daneels, G., de Raeymaeker, M., de Mey, J. (1988) Colloidal Metal Staining of Blots. In Handbook of Immunoblotting of Proteins, Vol. 1. (Bjerrum, O.J. & Heegaard, N.H.H., eds), pp. 137-144. CRC Press, Inc., Orlando.
    • (1988) Handbook of Immunoblotting of Proteins , vol.1 , pp. 137-144
    • Moeremans, M.1    Daneels, G.2    De Raeymaeker, M.3    De Mey, J.4
  • 26
    • 0015327122 scopus 로고
    • A novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate
    • 26. O'Callaghan, C.H., Morris, A., Kirby, S.M. & Shingler, A.H. (1972) A novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob. Agents Chemother. 1, 283-288.
    • (1972) Antimicrob. Agents Chemother. , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.H.4
  • 27
    • 0023777977 scopus 로고
    • A survey of the kinetic parameters of class C β-lactamases: Cephalosporins and other β-lactam compounds
    • 27. Galleni, M., Amicosante, G., Frère, J.-M. (1988) A survey of the kinetic parameters of class C β-lactamases: cephalosporins and other β-lactam compounds. Biochem. J. 255, 123-129.
    • (1988) Biochem. J. , vol.255 , pp. 123-129
    • Galleni, M.1    Amicosante, G.2    Frère, J.-M.3
  • 29
    • 0000432721 scopus 로고
    • Blue dextransepharose: An affinity column for the dinucleotide fold in proteins
    • 29. Thompson, S.T., Cass, K.H. & Stellwagen, E. (1975) Blue dextransepharose: an affinity column for the dinucleotide fold in proteins. Proc. Natl Acad. Sci. USA 72, 669-672.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 669-672
    • Thompson, S.T.1    Cass, K.H.2    Stellwagen, E.3
  • 30
    • 0018592586 scopus 로고
    • Purification of β-lactamase from Streptomyces cellulosae by affinity chromatography on blue sepharose
    • 30. Ogawara, H. & Horikawa, S. (1979) Purification of β-lactamase from Streptomyces cellulosae by affinity chromatography on blue sepharose. J. Antibiot. 32, 1328-1335.
    • (1979) J. Antibiot. , vol.32 , pp. 1328-1335
    • Ogawara, H.1    Horikawa, S.2
  • 31
    • 0028068225 scopus 로고
    • Isolation and partial purification of a carbapenem-hydrolyzing metallo-β-lactamase from Pseudomonas cepacia
    • 31. Baxter, I.A. & Lambert, P.A. (1994) Isolation and partial purification of a carbapenem-hydrolyzing metallo-β-lactamase from Pseudomonas cepacia. FEMS Microbiol. Lett. 122, 251-256.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 251-256
    • Baxter, I.A.1    Lambert, P.A.2
  • 32
    • 0028817346 scopus 로고
    • Cloning, sequencing, and site-directed mutagenesis of β-lactamase gene from Streptomyces fradiae Y59
    • 32. Kurai, S., Urabe, H. & Ogawara, H. (1995) Cloning, sequencing, and site-directed mutagenesis of β-lactamase gene from Streptomyces fradiae Y59. Antimicrob. Agents Chemother. 39, 260-263.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 260-263
    • Kurai, S.1    Urabe, H.2    Ogawara, H.3
  • 33
    • 0025216609 scopus 로고
    • Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo
    • 33. Fikes, J.D., Barkocy-Gallagher, G.A., Klapper, D.G. & Bassford, P.J. Jr (1990) Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. J. Biol. Chem. 265, 3417-3423.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3417-3423
    • Fikes, J.D.1    Barkocy-Gallagher, G.A.2    Klapper, D.G.3    Bassford P.J., Jr.4
  • 34
    • 0020050039 scopus 로고
    • Isolation and properties of an inducible and a constitutive β-lactamase from Pseudomonas aeruginosa
    • 34. Berks, M., Redhead, K. & Abraham, E.P. (1982) Isolation and properties of an inducible and a constitutive β-lactamase from Pseudomonas aeruginosa. J. Gen. Microbiol. 128, 155-159.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 155-159
    • Berks, M.1    Redhead, K.2    Abraham, E.P.3
  • 35
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • 35. Lobkovsky, E., Moews, P.C., Liu, H., Zhao, H., Frère, J.-M. & Knox, J.R. (1993) Evolution of an enzyme activity: crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl Acad. Sci. USA 90, 11257-11261.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frère, J.-M.5    Knox, J.R.6
  • 36
    • 0022509177 scopus 로고
    • Structural and kinetic studies on β-lactamase K1 from Klebsiella aerogenes
    • 36. Emanuel, E.L., Gagnon, J. & Waley, S.G. (1986) Structural and kinetic studies on β-lactamase K1 from Klebsiella aerogenes. Biochem. J. 234, 343-347.
    • (1986) Biochem. J. , vol.234 , pp. 343-347
    • Emanuel, E.L.1    Gagnon, J.2    Waley, S.G.3
  • 37
    • 0024287069 scopus 로고
    • Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products
    • 37. Galleni, M., Lindberg, F., Normark, S., Cole, S., Honore, N., Joris, B. & Frère, J.-M. (1988) Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products. Biochem. J. 250, 753-760.
    • (1988) Biochem. J. , vol.250 , pp. 753-760
    • Galleni, M.1    Lindberg, F.2    Normark, S.3    Cole, S.4    Honore, N.5    Joris, B.6    Frère, J.-M.7
  • 38
    • 0017764513 scopus 로고
    • Escherichia coli K-12 mutants hyperproducing chromosomal β-lactamase by gene repetitions
    • 38. Normark, S., Edlund, T., Grundström, T., Bergström, S. & Wolf-Watz, H. (1977) Escherichia coli K-12 mutants hyperproducing chromosomal β-lactamase by gene repetitions. J. Bacteriol. 132, 912-922.
    • (1977) J. Bacteriol. , vol.132 , pp. 912-922
    • Normark, S.1    Edlund, T.2    Grundström, T.3    Bergström, S.4    Wolf-Watz, H.5
  • 39
    • 0018692230 scopus 로고
    • Isolation and characterization of DNA repetitions carrying the chromosomal β-lactamase gene of Escherichia coli K-12
    • 39. Edlund, T., Grundström, T. & Normark, S. (1979) Isolation and characterization of DNA repetitions carrying the chromosomal β-lactamase gene of Escherichia coli K-12. Mol. Gen. Genet. 173, 115-125.
    • (1979) Mol. Gen. Genet. , vol.173 , pp. 115-125
    • Edlund, T.1    Grundström, T.2    Normark, S.3
  • 40
    • 0021930629 scopus 로고
    • Processing of Bacillus cereus 569/H β-lactamase I in Escherichia coli and Bacillus subtilis
    • 40. Mèzes, P.S.F., Blacher, R.W., Lampen, J.O. (1985) Processing of Bacillus cereus 569/H β-lactamase I in Escherichia coli and Bacillus subtilis. J. Biol. Chem. 260, 1218-1223.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1218-1223
    • Mèzes, P.S.F.1    Blacher, R.W.2    Lampen, J.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.