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Volumn 344, Issue 3, 2004, Pages 653-663

Analysis of the context dependent sequence requirements of active site residues in the metallo-β-lactamase IMP-1

Author keywords

information content; randomization; selection; substrate specificity; lactamase

Indexed keywords

AMPICILLIN; CEFALORIDINE; CEFOTAXIME; IMIPENEM; PENICILLINASE;

EID: 7944238165     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.074     Document Type: Article
Times cited : (56)

References (52)
  • 2
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • K. Bush, G.A. Jacoby, and A.A. Medeiros A functional classification scheme for β-lactamases and its correlation with molecular structure Antimicrob. Agents Chemother. 39 1995 1211 1233
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 3
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • N.O. Concha, C.A. Janson, P. Rowling, S. Pearson, C.A. Cheever, and B.P. Clarke Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor Biochemistry 39 2000 4288 4298
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3    Pearson, S.4    Cheever, C.A.5    Clarke, B.P.6
  • 5
    • 0032926983 scopus 로고    scopus 로고
    • Carbapenem resistance in Escherichia coli associated with plasmid-determined CMY-4 β-lactamase production and loss of an outer membrane protein
    • P.D. Stapleton, K.P. Shannon, and G.L. French Carbapenem resistance in Escherichia coli associated with plasmid-determined CMY-4 β-lactamase production and loss of an outer membrane protein Antimicrob. Agents Chemother. 43 1999 1206 1210
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1206-1210
    • Stapleton, P.D.1    Shannon, K.P.2    French, G.L.3
  • 6
    • 0033988342 scopus 로고    scopus 로고
    • Sequence analysis of ARI-1, a novel OXA β-lactamase, responsible for imipenem resistance in Acinetobacter baumannii 6B92
    • H.M. Donald, W. Scaife, S.G. Amyes, and H.K. Young Sequence analysis of ARI-1, a novel OXA β-lactamase, responsible for imipenem resistance in Acinetobacter baumannii 6B92 Antimicrob. Agents Chemother. 44 2000 196 199
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 196-199
    • Donald, H.M.1    Scaife, W.2    Amyes, S.G.3    Young, H.K.4
  • 7
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • A. Carfi, S. Pares, E. Duee, M. Galleni, C. Duez, J.M. Frere, and O. Dideberg The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold EMBO J. 14 1995 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
  • 8
    • 0031833739 scopus 로고    scopus 로고
    • 1.85 Å resolution structure of the zinc (II) β-lactamase from Bacillus cereus
    • A. Carfi, E. Duee, M. Galleni, J.M. Frere, and O. Dideberg 1.85 Å resolution structure of the zinc (II) β-lactamase from Bacillus cereus Acta Crystallog. sect. D 54 1998 313 323
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 313-323
    • Carfi, A.1    Duee, E.2    Galleni, M.3    Frere, J.M.4    Dideberg, O.5
  • 9
    • 0031887008 scopus 로고    scopus 로고
    • X-ray structure of the ZnII β-lactamase from Bacteroides fragilis in an orthorhombic crystal form
    • A. Carfi, E. Duee, R. Paul-Soto, M. Galleni, J.M. Frere, and O. Dideberg X-ray structure of the ZnII β-lactamase from Bacteroides fragilis in an orthorhombic crystal form Acta Crystallog. sect. D 54 1998 45 57
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 45-57
    • Carfi, A.1    Duee, E.2    Paul-Soto, R.3    Galleni, M.4    Frere, J.M.5    Dideberg, O.6
  • 10
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • N.O. Concha, B.A. Rasmussen, K. Bush, and O. Herzberg Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis Structure 4 1996 823 836
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 11
    • 0032497362 scopus 로고    scopus 로고
    • Crystal structure of the zinc-dependent β-lactamase from Bacillus cereus at 1.9 Å resolution: Binuclear active site with features of a mononuclear enzyme
    • S.M. Fabiane, M.K. Sohi, T. Wan, D.J. Payne, J.H. Bateson, T. Mitchell, and B.J. Sutton Crystal structure of the zinc-dependent β-lactamase from Bacillus cereus at 1.9 Å resolution: binuclear active site with features of a mononuclear enzyme Biochemistry 37 1998 12404 12411
    • (1998) Biochemistry , vol.37 , pp. 12404-12411
    • Fabiane, S.M.1    Sohi, M.K.2    Wan, T.3    Payne, D.J.4    Bateson, J.H.5    Mitchell, T.6    Sutton, B.J.7
  • 12
    • 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
    • I. Garcia-Saez, P.S. Mercuri, C. Papamicael, R. Kahn, J.M. Frere, and M. Galleni 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 J. Mol. Biol. 325 2003 651 660
    • (2003) J. Mol. Biol. , vol.325 , pp. 651-660
    • Garcia-Saez, I.1    Mercuri, P.S.2    Papamicael, C.3    Kahn, R.4    Frere, J.M.5    Galleni, M.6
  • 13
    • 0037592222 scopus 로고    scopus 로고
    • The 1.5 Å structure of Chryseobacterium meningospeticum zinc β-lactamase in complex with the inhibitor, d-captopril
    • I. Garcia-Saez, J. Hopkins, C. Papamicael, N. Franceschini, G. Amicosante, and G.M. Rossolini The 1.5 Å structure of Chryseobacterium meningospeticum zinc β-lactamase in complex with the inhibitor, d-captopril J. Biol. Chem. 278 2003 23868 23873
    • (2003) J. Biol. Chem. , vol.278 , pp. 23868-23873
    • Garcia-Saez, I.1    Hopkins, J.2    Papamicael, C.3    Franceschini, N.4    Amicosante, G.5    Rossolini, G.M.6
  • 14
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution
    • J.H. Ullah, T.R. Walsh, I.A. Taylor, D.C. Emery, C.S. Verma, S.J. Gamblin, and J. Spencer The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution J. Mol. Biol. 284 1998 125 136
    • (1998) J. Mol. Biol. , vol.284 , 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
    • 0035190707 scopus 로고    scopus 로고
    • Identification of residues critical for metallo-β-lactamase function by codon randomization and selection
    • I.C. Materon, and T. Palzkill Identification of residues critical for metallo-β-lactamase function by codon randomization and selection Protein Sci. 10 2001 2556 2565
    • (2001) Protein Sci. , vol.10 , pp. 2556-2565
    • Materon, I.C.1    Palzkill, T.2
  • 17
    • 0038648570 scopus 로고    scopus 로고
    • Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-β-lactamase
    • J.J.A. Huntley, W. Fast, S.J. Benkovic, P.E. Wright, and H.J. Dyson Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-β-lactamase Protein Sci. 12 2003 1368 1375
    • (2003) Protein Sci. , vol.12 , pp. 1368-1375
    • Huntley, J.J.A.1    Fast, W.2    Benkovic, S.J.3    Wright, P.E.4    Dyson, H.J.5
  • 18
    • 0037399075 scopus 로고    scopus 로고
    • Analysis of the importance of the metallo-β-lactamase active site loop in substrate binding and catalysis
    • C. Moali, C. Anne, J. Lamotte-Brasseur, S. Groslambert, B. Devreese, and J. Van Beeuman Analysis of the importance of the metallo-β-lactamase active site loop in substrate binding and catalysis Chem. Biol. 10 2003 319 329
    • (2003) Chem. Biol. , vol.10 , pp. 319-329
    • Moali, C.1    Anne, C.2    Lamotte-Brasseur, J.3    Groslambert, S.4    Devreese, B.5    Van Beeuman, J.6
  • 19
    • 0033056949 scopus 로고    scopus 로고
    • Kinetic properties and metal content of the metallo-β-lactamase CcrA harboring selective amino acid substitutions
    • Y. Yang, D. Keeney, X. Tang, N. Canfield, and B.A. Rasmussen Kinetic properties and metal content of the metallo-β-lactamase CcrA harboring selective amino acid substitutions J. Biol. Chem. 274 1999 15706 15711
    • (1999) J. Biol. Chem. , vol.274 , pp. 15706-15711
    • Yang, Y.1    Keeney, D.2    Tang, X.3    Canfield, N.4    Rasmussen, B.A.5
  • 22
    • 0032588069 scopus 로고    scopus 로고
    • Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes
    • N. Laraki, M. Galleni, I. Thamm, M.L. Riccio, G. Amicosante, J.M. Frere, and G.M. Rossolini Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes Antimicrob. Agents Chemother. 43 1999 890 901
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 890-901
    • Laraki, N.1    Galleni, M.2    Thamm, I.3    Riccio, M.L.4    Amicosante, G.5    Frere, J.M.6    Rossolini, G.M.7
  • 23
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • J.U. Bowie, J.F. Reidhaar-Olson, W.A. Lim, and R.T. Sauer Deciphering the message in protein sequences: tolerance to amino acid substitutions Science 27 1990 1306 1310
    • (1990) Science , vol.27 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 24
    • 0037665961 scopus 로고    scopus 로고
    • Molecular messages
    • J.W. Szostak Molecular messages Nature 423 2003 689
    • (2003) Nature , vol.423 , pp. 689
    • Szostak, J.W.1
  • 25
    • 0347314981 scopus 로고    scopus 로고
    • Physical complexity of symbolic sequences
    • C. Adami, and N.J. Cerf Physical complexity of symbolic sequences Physica D 137 2000 62 69
    • (2000) Physica D , vol.137 , pp. 62-69
    • Adami, C.1    Cerf, N.J.2
  • 26
    • 0036905397 scopus 로고    scopus 로고
    • What is complexity?
    • C. Adami What is complexity? BioEssays 24 2002 1085 1094
    • (2002) BioEssays , vol.24 , pp. 1085-1094
    • Adami, C.1
  • 27
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 28
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection
    • W.O. Bullock, J.M. Fernandez, and J.M. Short XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection BioTechniques 5 1987 376 379
    • (1987) BioTechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 30
    • 0029962946 scopus 로고    scopus 로고
    • Amino acid sequence determinants of β-lactamase structure and activity
    • W. Huang, J. Petrosino, M. Hirsch, P.S. Shenkin, and T. Palzkill Amino acid sequence determinants of β-lactamase structure and activity J. Mol. Biol. 258 1996 688 703
    • (1996) J. Mol. Biol. , vol.258 , pp. 688-703
    • Huang, W.1    Petrosino, J.2    Hirsch, M.3    Shenkin, P.S.4    Palzkill, T.5
  • 32
    • 0033517787 scopus 로고    scopus 로고
    • NMR characterization of the metallo-β-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop
    • S.D. Scrofani, J. Chung, J.J. Huntley, S.J. Benkovic, P.E. Wright, and H.J. Dyson NMR characterization of the metallo-β-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop Biochemistry 38 1999 14507 14514
    • (1999) Biochemistry , vol.38 , pp. 14507-14514
    • Scrofani, S.D.1    Chung, J.2    Huntley, J.J.3    Benkovic, S.J.4    Wright, P.E.5    Dyson, H.J.6
  • 33
    • 0035451514 scopus 로고    scopus 로고
    • Modeling of the metallo-β-lactamase from B. fragilis: Structural and dynamic effects of inhibitor binding
    • F.R. Salsbury Jr, M.F. Crowley, and C.L. Brooks III Modeling of the metallo-β-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding Proteins: Struct. Funct. Genet. 44 2001 448 459
    • (2001) Proteins: Struct. Funct. Genet. , vol.44 , pp. 448-459
    • Salsbury Jr., F.R.1    Crowley, M.F.2    Brooks III, C.L.3
  • 34
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the β-lactamase fold
    • H. Daiyasu, K. Osaka, Y. Ishino, and H. Toh Expansion of the zinc metallo-hydrolase family of the β-lactamase fold FEBS Letters 503 2001 1 6
    • (2001) FEBS Letters , vol.503 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 35
    • 0035313529 scopus 로고    scopus 로고
    • Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase
    • S. Haruta, E.T. Yamamoto, Y. Eriguchi, and T. Sawai Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase FEMS Microbiol. Letters 197 2001 85 89
    • (2001) FEMS Microbiol. Letters , vol.197 , pp. 85-89
    • Haruta, S.1    Yamamoto, E.T.2    Eriguchi, Y.3    Sawai, T.4
  • 36
    • 0033520073 scopus 로고    scopus 로고
    • On the mechanism of the metallo-β-lactamase from Bacteroides fragilis
    • Z. Wang, W. Fast, and S.J. Benkovic On the mechanism of the metallo-β-lactamase from Bacteroides fragilis Biochemistry 38 1999 10013 10023
    • (1999) Biochemistry , vol.38 , pp. 10013-10023
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 37
    • 0024253532 scopus 로고
    • Evidence for an oxyanion hole in β-lactamases and DD-peptidases
    • B.P. Murphy, and R.F. Pratt Evidence for an oxyanion hole in β-lactamases and DD-peptidases Biochem. J. 256 1988 669 672
    • (1988) Biochem. J. , vol.256 , pp. 669-672
    • Murphy, B.P.1    Pratt, R.F.2
  • 38
    • 0034732962 scopus 로고    scopus 로고
    • Enzyme-induced strain/distortion in the ground-state ES complex in β-lactamase catalysis revealed by FTIR
    • M.J. Hokenson, G.A. Cope, E.R. Lewis, K.A. Oberg, and A.L. Fink Enzyme-induced strain/distortion in the ground-state ES complex in β-lactamase catalysis revealed by FTIR Biochemistry 39 2000 6538 6545
    • (2000) Biochemistry , vol.39 , pp. 6538-6545
    • Hokenson, M.J.1    Cope, G.A.2    Lewis, E.R.3    Oberg, K.A.4    Fink, A.L.5
  • 39
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • J. Kraut Serine proteases: structure and mechanism of catalysis Annu. Rev. Biochem. 46 1977 331 358
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 40
    • 0042666843 scopus 로고    scopus 로고
    • Modeling domino effects in enzymes: Molecular basis of the substrate specificity of the bacterial metallo-β-lactamases IMP-1 and IMP-6
    • P. Oelschlaeger, R.D. Schmid, and J. Pleiss Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-β-lactamases IMP-1 and IMP-6 Biochemistry 42 2003 8945 8956
    • (2003) Biochemistry , vol.42 , pp. 8945-8956
    • Oelschlaeger, P.1    Schmid, R.D.2    Pleiss, J.3
  • 41
    • 0032882552 scopus 로고    scopus 로고
    • Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes
    • D.W. Christianson, and J.D. Cox Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes Annu. Rev. Biochem. 68 1999 33 57
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 33-57
    • Christianson, D.W.1    Cox, J.D.2
  • 42
    • 0029989461 scopus 로고    scopus 로고
    • Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II
    • C.C. Huang, C.A. Lesburg, L.L. Kiefer, C.A. Fierke, and D.W. Christianson Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II Biochemistry 35 1996 3439 3446
    • (1996) Biochemistry , vol.35 , pp. 3439-3446
    • Huang, C.C.1    Lesburg, C.A.2    Kiefer, L.L.3    Fierke, C.A.4    Christianson, D.W.5
  • 45
    • 0021019879 scopus 로고
    • Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli
    • E. Amann, J. Brosius, and M. Ptashne Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli Gene 25 1983 167 178
    • (1983) Gene , vol.25 , pp. 167-178
    • Amann, E.1    Brosius, J.2    Ptashne, M.3
  • 46
    • 0019586165 scopus 로고
    • Mechanism of action of the lexA gene product
    • R. Brent, and M. Ptashne Mechanism of action of the lexA gene product Proc. Natl Acad. Sci. USA 78 1981 4204 4208
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4204-4208
    • Brent, R.1    Ptashne, M.2
  • 47
    • 0033593437 scopus 로고    scopus 로고
    • Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of β-lactamases
    • J. Petrosino, G. Rudgers, H. Gilbert, and T. Palzkill Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of β-lactamases J. Biol. Chem. 274 1999 2394 2400
    • (1999) J. Biol. Chem. , vol.274 , pp. 2394-2400
    • Petrosino, J.1    Rudgers, G.2    Gilbert, H.3    Palzkill, T.4
  • 48
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • W. Schaffner, and C. Weissmann A rapid, sensitive, and specific method for the determination of protein in dilute solution Anal. Biochem. 56 1973 502 514
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 49
    • 0034595379 scopus 로고    scopus 로고
    • Lysine-73 is involved in the acylation and deacylation of β-lactamase
    • E.J. Lietz, H. Truher, D. Kahn, M.J. Hokenson, and A.L. Fink Lysine-73 is involved in the acylation and deacylation of β-lactamase Biochemistry 39 2000 4971 4981
    • (2000) Biochemistry , vol.39 , pp. 4971-4981
    • Lietz, E.J.1    Truher, H.2    Kahn, D.3    Hokenson, M.J.4    Fink, A.L.5
  • 50
    • 0032925064 scopus 로고    scopus 로고
    • Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli
    • N. Laraki, N. Franceschini, G.M. Rossolini, P. Santucci, C. Meunier, and E. de Pauw Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli Antimicrob. Agents Chemother. 43 1999 902 906
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 902-906
    • Laraki, N.1    Franceschini, N.2    Rossolini, G.M.3    Santucci, P.4    Meunier, C.5    De Pauw, E.6
  • 51
    • 0032803407 scopus 로고    scopus 로고
    • Class C β-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates
    • A. Bulychev, and S. Mobashery Class C β-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates Antimicrob. Agents Chemother. 43 1999 1743 1746
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1743-1746
    • Bulychev, A.1    Mobashery, S.2


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