메뉴 건너뛰기




Volumn 278, Issue 8, 2011, Pages 1252-1263

Broad antibiotic resistance profile of the subclass B3 metallo-β- lactamase GOB-1, a di-zinc enzyme

Author keywords

lactamase; antibiotic resistance; GOB; metallo lactamase; zinc binding site

Indexed keywords

BETA LACTAM ANTIBIOTIC; CEFALOTIN; CEFOXITIN; CHLORAMPHENICOL; GLUTAMINE; IMIPENEM; KANAMYCIN; MEROPENEM; METALLO BETA LACTAMASE; NITROCEFIN; PENICILLIN G; ZINC ION;

EID: 79953695364     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08046.x     Document Type: Article
Times cited : (20)

References (36)
  • 1
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new-type of protein fold
    • Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, &, Dideberg O, (1995) The 3-D structure of a zinc metallo-beta-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
  • 2
    • 0029019031 scopus 로고
    • Beta-lactamases and bacterial-resistance to antibiotics
    • Frere JM, (1995) Beta-lactamases and bacterial-resistance to antibiotics. Mol Microbiol 16, 385-395.
    • (1995) Mol Microbiol , vol.16 , pp. 385-395
    • Frere, J.M.1
  • 3
    • 0033082703 scopus 로고    scopus 로고
    • The β-lactamase cycle: A tale of selective pressure and bacterial ingenuity
    • DOI 10.1039/a705983c
    • Matagne A, Dubus A, Galleni M, &, Frere JM, (1999) The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity. Nat Prod Rep 16, 1-19. (Pubitemid 29092067)
    • (1999) Natural Product Reports , vol.16 , Issue.1 , pp. 1-19
    • Matagne, A.1    Dubus, A.2    Galleni, M.3    Frere, J.-M.4
  • 5
    • 0019326853 scopus 로고
    • The structure of beta-lactamases
    • Ambler RP, (1980) The structure of beta-lactamases. Philos Trans R Soc Lond B 289, 321-331.
    • (1980) Philos Trans R Soc Lond B , vol.289 , pp. 321-331
    • Ambler, R.P.1
  • 6
    • 0029071785 scopus 로고
    • A functional classification scheme for beta-lactamases and its correlation with molecular-structure
    • Bush K, Jacoby GA, &, Medeiros AA, (1995) A functional classification scheme for beta-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
  • 8
    • 0034698266 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036 (FEBS 23250) [FEBS Lett 467 (2000) 221-225]
    • Valladares MH, Kiefer M, Heinz U, Soto RP, Meyer-Klaucke W, Nolting HF, Zeppezauer M, Galleni M, Frere JM, Rossolini GM, et al. (2000) Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036 (FEBS 23250) [FEBS Lett 467 (2000) 221-225]. FEBS Lett 477, 285-285.
    • (2000) FEBS Lett , vol.477 , pp. 285-285
    • Valladares, M.H.1    Kiefer, M.2    Heinz, U.3    Soto, R.P.4    Meyer-Klaucke, W.5    Nolting, H.F.6    Zeppezauer, M.7    Galleni, M.8    Frere, J.M.9    Rossolini, G.M.10
  • 9
    • 0031978726 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the cloned metallo-β-lactamase L1 from Stenotrophomonas maltophilia
    • Crowder MW, Walsh TR, Banovic L, Pettit M, &, Spencer J, (1998) Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia. Antimicrob Agents Chemother 42, 921-926. (Pubitemid 28216380)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.4 , pp. 921-926
    • Crowder, M.W.1    Walsh, T.R.2    Banovic, L.3    Pettit, M.4    Spencer, J.5
  • 12
    • 0025975453 scopus 로고
    • Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis
    • Bandoh K, Muto Y, Watanabe K, Katoh N, &, Ueno K, (1991) Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis. Antimicrob Agents Chemother 35, 371-372.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 371-372
    • Bandoh, K.1    Muto, Y.2    Watanabe, K.3    Katoh, N.4    Ueno, K.5
  • 13
    • 0025875773 scopus 로고
    • The Aeromonas hydrophila Cpha gene - Molecular heterogeneity among class-B metallo-beta-lactamases
    • Massidda O, Rossolini GM, &, Satta G, (1991) The Aeromonas hydrophila Cpha gene-molecular heterogeneity among class-B metallo-beta-lactamases. J Bacteriol 173, 4611-4617.
    • (1991) J Bacteriol , vol.173 , pp. 4611-4617
    • Massidda, O.1    Rossolini, G.M.2    Satta, G.3
  • 14
    • 0029871720 scopus 로고    scopus 로고
    • Enzyme kinetics and biochemical analysis of ImiS, the metallo-β-lactamase from Aeromonas sobria 163a
    • DOI 10.1093/jac/37.3.423
    • Walsh TR, Gamblin S, Emery DC, MacGowan AP, &, Bennett PM, (1996) Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a. J Antimicrob Chemother 37, 423-431. (Pubitemid 26116957)
    • (1996) Journal of Antimicrobial Chemotherapy , vol.37 , Issue.3 , pp. 423-431
    • Walsh, T.R.1    Gamblin, S.2    Emery, D.C.3    MacGowan, A.P.4    Bennett, P.M.5
  • 15
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution
    • DOI 10.1006/jmbi.1998.2148
    • Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, &, Spencer J, (1998) The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 angstrom resolution. J Mol Biol 284, 125-136. (Pubitemid 28524001)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.1 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3    Emery, D.C.4    Verma, C.S.5    Gamblin, S.J.6    Spencer, J.7
  • 16
    • 0034128893 scopus 로고    scopus 로고
    • The Legionella (Fluoribacter) gormanii metallo-β-lactamase: A new member of the highly divergent lineage of molecular-subclass B3 β-lactamases
    • DOI 10.1128/AAC.44.6.1538-1543.2000
    • Boschi L, Mercuri PS, Riccio ML, Amicosante G, Galleni M, Frere JM, &, Rossolini GM, (2000) The Legionella (Fluoribacter) gormanii metallo-beta-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 beta-lactamases. Antimicrob Agents Chemother 44, 1538-1543. (Pubitemid 30340791)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.6 , pp. 1538-1543
    • Boschi, L.1    Mercuri, P.S.2    Riccio, M.L.3    Amicosante, G.4    Galleni, M.5    Frere, J.-M.6    Rossolini, G.M.7
  • 17
    • 0033946586 scopus 로고    scopus 로고
    • Molecular and biochemical heterogeneity of class B carbapenem- hydrolyzing β-lactamases in Chryseobacterium meningosepticum
    • DOI 10.1128/AAC.44.7.1878-1886.2000
    • Bellais S, Aubert D, Naas T, &, Nordmann P, (2000) Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum. Antimicrob Agents Chemother 44, 1878-1886. (Pubitemid 30422942)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.7 , pp. 1878-1886
    • Bellais, S.1    Aubert, D.2    Naas, T.3    Nordmann, P.4
  • 21
    • 0035861910 scopus 로고    scopus 로고
    • A novel metallo-β-lactamase, Mbl1b, produced by the environmental bacterium Caulobacter crescentus
    • DOI 10.1016/S0014-5793(01)03152-0, PII S0014579301031520
    • Simm AM, Higgins CS, Pullan ST, Avison MB, Niumsup P, Erdozain O, Bennett PM, &, Walsh TR, (2001) A novel metallo-beta-lactamase, Mb11b, produced by the environmental bacterium Caulobacter crescentus. FEBS Lett 509, 350-354. (Pubitemid 34031959)
    • (2001) FEBS Letters , vol.509 , Issue.3 , pp. 350-354
    • Simm, A.M.1    Higgins, C.S.2    Pullan, S.T.3    Avison, M.B.4    Niumsup, P.5    Erdozain, O.6    Bennett, P.M.7    Walsh, T.R.8
  • 22
    • 33744464764 scopus 로고    scopus 로고
    • Postgenomic scan of metallo-β-lactamase homologues in rhizobacteria: Identification and characterization of BJP-1, a subclass B3 ortholog from Bradyrhizobium japonicum
    • DOI 10.1128/AAC.01551-05
    • Stoczko M, Frere JM, Rossolini GM, &, Docquier JD, (2006) Postgenomic scan of metallo-beta-lactamase homologues in rhizobacteria: identification and characterization of BJP-1, a subclass B3 ortholog from Bradyrhizobium japonicum. Antimicrob Agents Chemother 50, 1973-1981. (Pubitemid 43807514)
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , Issue.6 , pp. 1973-1981
    • Stoczko, M.1    Frere, J.-M.2    Rossolini, G.M.3    Docquier, J.-D.4
  • 23
    • 46249083011 scopus 로고    scopus 로고
    • Functional diversity among metallo-β-lactamases: Characterization of the CAR-1 enzyme of Erwinia carotovora
    • DOI 10.1128/AAC.01062-07
    • Stoczko M, Frere JM, Rossolini GM, &, Docquier JD, (2008) Functional diversity among metallo-beta-lactamases: characterization of the CAR-1 enzyme of Erwinia carotovora. Antimicrob Agents Chemother 52, 2473-2479. (Pubitemid 351915678)
    • (2008) Antimicrobial Agents and Chemotherapy , vol.52 , Issue.7 , pp. 2473-2479
    • Stoczko, M.1    Frere, J.-M.2    Rossolini, G.M.3    Docquier, J.-D.4
  • 24
    • 0021952587 scopus 로고
    • The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275
    • Bicknell R, Emanuel EL, Gagnon J, &, Waley SG, (1985) The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275. Biochem J 229, 791-797. (Pubitemid 15243727)
    • (1985) Biochemical Journal , vol.229 , Issue.3 , pp. 791-797
    • Bicknell, R.1    Emanuel, E.L.2    Gagnon, J.3    Waley, S.G.4
  • 25
    • 0020370569 scopus 로고
    • Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia
    • Saino Y, Kobayashi F, Inoue M, &, Mitsuhashi S, (1982) Purification and properties of inducible penicillin beta-lactamase isolated from Pseudomonas maltophilia. Antimicrob Agents Chemother 22, 564-570. (Pubitemid 13206533)
    • (1982) Antimicrobial Agents and Chemotherapy , vol.22 , Issue.4 , pp. 564-570
    • Saino, Y.1    Kobayashi, F.2    Inoue, M.3    Mitsuhashi, S.4
  • 26
    • 0037462925 scopus 로고    scopus 로고
    • Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
    • DOI 10.1016/S0022-2836(02)01271-8
    • Garcia-Saez I, Mercuri PS, Papamicael C, Kahn R, Frere JM, Galleni M, Rossolini GM, &, Dideberg O, (2003) Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril. J Mol Biol 325, 651-660. (Pubitemid 36268689)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.4 , pp. 651-660
    • Garcia-Saez, I.1    Mercuri, P.S.2    Papamicael, C.3    Kahn, R.4    Frere, J.M.5    Galleni, M.6    Rossolini, G.M.7    Dideberg, O.8
  • 28
    • 0032582569 scopus 로고    scopus 로고
    • Mono- and binuclear Zn-β-lactamase from Bacteroides fragilis: Catalytic and structural roles of the zinc ions
    • DOI 10.1016/S0014-5793(98)01289-7, PII S0014579398012897
    • Paul-Soto R, Hernandez-Valladares M, Galleni M, Bauer R, Zeppezauer M, Frere JM, &, Adolph HW, (1998) Mono- and binuclear Zn-beta-lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions. FEBS Lett 438, 137-140. (Pubitemid 28517851)
    • (1998) FEBS Letters , vol.438 , Issue.1-2 , pp. 137-140
    • Paul-Soto, R.1    Hernandez-Valladares, M.2    Galleni, M.3    Bauer, R.4    Zeppezauer, M.5    Frere, J.-M.6    Adolph, H.-W.7
  • 31
    • 56749107392 scopus 로고    scopus 로고
    • Metal content and localization during turnover in B. cereus metallo-beta-lactamase
    • Llarrull LI, Tioni MF, &, Vila AJ, (2008) Metal content and localization during turnover in B. cereus metallo-beta-lactamase. J Am Chem Soc 130, 15842-15851.
    • (2008) J Am Chem Soc , vol.130 , pp. 15842-15851
    • Llarrull, L.I.1    Tioni, M.F.2    Vila, A.J.3
  • 32
    • 0028174237 scopus 로고
    • Beta-lactamase ragged ends detected by electrospray mass-spectrometry correlates poorly with multiple banding on isoelectric focusing
    • Payne DJ, Skett PW, Aplin RT, Robinson CV, &, Knowles DJC, (1994) Beta-lactamase ragged ends detected by electrospray mass-spectrometry correlates poorly with multiple banding on isoelectric focusing. Biol Mass Spectrom 23, 159-164.
    • (1994) Biol Mass Spectrom , vol.23 , pp. 159-164
    • Payne, D.J.1    Skett, P.W.2    Aplin, R.T.3    Robinson, C.V.4    Knowles, D.J.C.5
  • 34
    • 67649963309 scopus 로고    scopus 로고
    • Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DNAK chaperone system and the sec machinery: Completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm
    • Moran-Barrio J, Limansky AS, &, Viale AM, (2009) Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DNAK chaperone system and the sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm. Antimicrob Agents Chemother 53, 2908-2917.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 2908-2917
    • Moran-Barrio, J.1    Limansky, A.S.2    Viale, A.M.3
  • 35
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-β-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • DOI 10.1016/j.jmb.2004.10.070, PII S0022283604013762
    • Garau G, Bebrone C, Anne C, Galleni M, Frere JM, &, Dideberg O, (2005) A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J Mol Biol 345, 785-795. (Pubitemid 39600934)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.4 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frere, J.-M.5    Dideberg, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.