메뉴 건너뛰기




Volumn 2008, Issue , 2008, Pages

The mechanisms of catalysis by metallo β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 45349100770     PISSN: 15653633     EISSN: 1687479X     Source Type: Journal    
DOI: 10.1155/2008/576297     Document Type: Review
Times cited : (92)

References (76)
  • 1
    • 0002796008 scopus 로고
    • Structure-activity relationships: Chemical
    • London, UK Blackie
    • Page M. I., Page M. I., Structure-activity relationships: chemical The Chemistry of β-Lactams 1992 London, UK Blackie 79 100
    • (1992) The Chemistry of β-Lactams , pp. 79-100
    • Page, M.I.1    Page, M.I.2
  • 2
    • 0001596755 scopus 로고
    • The mechanisms of reactions of β -lactam antibiotics
    • Page M. I., The mechanisms of reactions of β -lactam antibiotics Advances in Physical Organic Chemistry 1987 23 165 270
    • (1987) Advances in Physical Organic Chemistry , vol.23 , pp. 165-270
    • Page, M.I.1
  • 3
    • 37049087664 scopus 로고
    • The hydrolysis of azetidinyl amidinium salts. Part 1. the unimportance of strain release in the four-membered ring
    • Page M. I., Webster P., Ghosez L., The hydrolysis of azetidinyl amidinium salts. Part 1. The unimportance of strain release in the four-membered ring Journal of the Chemical Society, Perkin Transactions 2 1990 5 805 811
    • (1990) Journal of the Chemical Society, Perkin Transactions 2 , Issue.5 , pp. 805-811
    • Page, M.I.1    Webster, P.2    Ghosez, L.3
  • 5
    • 37049102557 scopus 로고
    • Intramolecular general acid catalysis in the aminolysis of benzylpenicillin. a preferred direction of nucleophilic attack
    • Martin A. F., Morris J. J., Page M. I., Intramolecular general acid catalysis in the aminolysis of benzylpenicillin. A preferred direction of nucleophilic attack Journal of the Chemical Society, Chemical Communications 1979 6 298 299
    • (1979) Journal of the Chemical Society, Chemical Communications , Issue.6 , pp. 298-299
    • Martin, A.F.1    Morris, J.J.2    Page, M.I.3
  • 6
    • 33846474111 scopus 로고
    • The aminolysis of penicillin derivatives. Rate constants for the formation and breakdown of the tetrahedral addition intermediate
    • Gensmantel N. P., Page M. I., The aminolysis of penicillin derivatives. Rate constants for the formation and breakdown of the tetrahedral addition intermediate Journal of the Chemical Society, Perkin Transactions 2 1979 2 137 142
    • (1979) Journal of the Chemical Society, Perkin Transactions 2 , Issue.2 , pp. 137-142
    • Gensmantel, N.P.1    Page, M.I.2
  • 8
    • 0031765412 scopus 로고    scopus 로고
    • Chemical reactivity of penicillins and cephalosporins. Intramolecular involvement of the acyl-amido side chain
    • Llinás A., Vilanova B., Frau J., Muñoz F., Donoso J., Page M. I., Chemical reactivity of penicillins and cephalosporins. Intramolecular involvement of the acyl-amido side chain Journal of Organic Chemistry 1998 63 24 9052 9060
    • (1998) Journal of Organic Chemistry , vol.63 , Issue.24 , pp. 9052-9060
    • Llinás, A.1    Vilanova, B.2    Frau, J.3    Muñoz, F.4    Donoso, J.5    Page, M.I.6
  • 9
    • 0026433541 scopus 로고
    • The energetics of intramolecular reactions and enzyme catalysis
    • Page M. I., The energetics of intramolecular reactions and enzyme catalysis Philosophical Transactions of the Royal Society B 1991 332 1263 149 156
    • (1991) Philosophical Transactions of the Royal Society B , vol.332 , Issue.1263 , pp. 149-156
    • Page, M.I.1
  • 12
    • 4644301876 scopus 로고    scopus 로고
    • Resistance to β -lactam antibiotics
    • Poole K., Resistance to β -lactam antibiotics Cellular and Molecular Life Sciences 2004 61 17 2200 2223
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.17 , pp. 2200-2223
    • Poole, K.1
  • 13
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β -lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher J. F., Meroueh S. O., Mobashery S., Bacterial resistance to β -lactam antibiotics: compelling opportunism, compelling opportunity Chemical Reviews 2005 105 2 395 424
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 15
    • 0001817705 scopus 로고
    • β -lactamase: Mechanism of action
    • London, UK Blackie
    • Waley S. G., Page M. I., β -lactamase: mechanism of action The Chemistry of β-Lactams 1992 London, UK Blackie 198 228
    • (1992) The Chemistry of β-Lactams , pp. 198-228
    • Waley, S.G.1    Page, M.I.2
  • 16
    • 0029019031 scopus 로고
    • β -lactamases and bacterial resistance to antibiotics
    • Frère J.-M., β -lactamases and bacterial resistance to antibiotics Molecular Microbiology 1995 16 3 385 395
    • (1995) Molecular Microbiology , vol.16 , Issue.3 , pp. 385-395
    • Frère, J.-M.1
  • 17
    • 0027284501 scopus 로고
    • Metallo- β -lactamases-a new therapeutic challenge
    • Payne D. J., Metallo- β -lactamases-a new therapeutic challenge Journal of Medical Microbiology 1993 39 2 93 99
    • (1993) Journal of Medical Microbiology , vol.39 , Issue.2 , pp. 93-99
    • Payne, D.J.1
  • 20
    • 0027409878 scopus 로고
    • An overview of the kinetic parameters of class B β -lactamases
    • Felici A., Amicosante G., Oratore A., An overview of the kinetic parameters of class B β -lactamases Biochemical Journal 1993 291, part 1 151 155
    • (1993) Biochemical Journal , vol.2911 , pp. 151-155
    • Felici, A.1    Amicosante, G.2    Oratore, A.3
  • 22
    • 0028837277 scopus 로고
    • Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo- β - llactamases
    • Felici A., Amicosante G., Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo- β-lactamases Antimicrobial Agents and Chemotherapy 1995 39 1 192 199
    • (1995) Antimicrobial Agents and Chemotherapy , vol.39 , Issue.1 , pp. 192-199
    • Felici, A.1    Amicosante, G.2
  • 23
    • 0035077110 scopus 로고    scopus 로고
    • Biochemical characterization of the FEZ-1 metallo- β -lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli
    • Mercuri P. S., Bouillenne F., Boschi L., Biochemical characterization of the FEZ-1 metallo- β -lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli Antimicrobial Agents and Chemotherapy 2001 45 4 1254 1262
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.4 , pp. 1254-1262
    • Mercuri, P.S.1    Bouillenne, F.2    Boschi, L.3
  • 24
    • 0037025381 scopus 로고    scopus 로고
    • Characterization of monomeric L1 metallo- β -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis
    • Simm A. M., Higgins C. S., Carenbauer A. L., Characterization of monomeric L1 metallo- β -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis Journal of Biological Chemistry 2002 277 27 24744 24752
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24744-24752
    • Simm, A.M.1    Higgins, C.S.2    Carenbauer, A.L.3
  • 25
    • 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., Pares S., Duée E., The 3-D structure of a zinc metallo- β -lactamase from Bacillus cereus reveals a new type of protein fold The EMBO Journal 1995 14 20 4914 4921
    • (1995) The EMBO Journal , vol.14 , Issue.20 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3
  • 27
    • 0032510815 scopus 로고    scopus 로고
    • Unanticipated inhibition of the metallo- β -lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): A crystallographic study at 1.85 Å resolution
    • Fitzgerald P. M., Wu J. K., Toney J. H., Unanticipated inhibition of the metallo- β -lactamase from Bacteroides fragilis by 4- morpholineethanesulfonic acid (MES): a crystallographic study at 1.85 Å resolution Biochemistry 1998 37 19 6791 6800
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6791-6800
    • Fitzgerald, P.M.1    Wu, J.K.2    Toney, J.H.3
  • 28
    • 33644948482 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo- β -lactamases
    • Murphy T. A., Catto L. E., Halford S. E., Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo- β -lactamases Journal of Molecular Biology 2006 357 3 890 903
    • (2006) Journal of Molecular Biology , vol.357 , Issue.3 , pp. 890-903
    • Murphy, T.A.1    Catto, L.E.2    Halford, S.E.3
  • 30
    • 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
    • Fabiane S. M., Sohi M. K., Wan T., 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 1998 37 36 12404 12411
    • (1998) Biochemistry , vol.37 , Issue.36 , pp. 12404-12411
    • Fabiane, S.M.1    Sohi, M.K.2    Wan, T.3
  • 31
    • 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
    • Concha N. O., Janson C. A., Rowling P., 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 2000 39 15 4288 4298
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3
  • 32
    • 0031440226 scopus 로고    scopus 로고
    • Crystal structures of the cadmium- and mercury-substituted metallo- β -lactamase from Bacteroides fragilis
    • Concha N. O., Rasmussen B. A., Bush K., Herzberg O., Crystal structures of the cadmium- and mercury-substituted metallo- β -lactamase from Bacteroides fragilis Protein Science 1997 6 12 2671 2676
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2671-2676
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 34
    • 0035976958 scopus 로고    scopus 로고
    • Metal ion binding and coordination geometry for wild type and mutants of metallo- β -lactamase from Bacillus cereus 569/H/9 (BcII)
    • de Seny D., Heinz U., Wommer S., Metal ion binding and coordination geometry for wild type and mutants of metallo- β -lactamase from Bacillus cereus 569/H/9 (BcII) Journal of Biological Chemistry 2001 276 48 45065 45078
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.48 , pp. 45065-45078
    • De Seny, D.1    Heinz, U.2    Wommer, S.3
  • 35
    • 0037025301 scopus 로고    scopus 로고
    • Substrate-activated zinc binding of metallo- β -lactamases
    • Wommer S., Rival S., Heinz U., Substrate-activated zinc binding of metallo- β -lactamases Journal of Biological Chemistry 2002 277 27 24142 24147
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24142-24147
    • Wommer, S.1    Rival, S.2    Heinz, U.3
  • 36
    • 0029808391 scopus 로고    scopus 로고
    • Characterization of the metal-binding sites of the β -lactamase from Bacteroides fragilis
    • Crowder M. W., Wang Z., Franklin S. L., Zovinka E. P., Benkovic S. J., Characterization of the metal-binding sites of the β -lactamase from Bacteroides fragilis Biochemistry 1996 35 37 12126 12132
    • (1996) Biochemistry , vol.35 , Issue.37 , pp. 12126-12132
    • Crowder, M.W.1    Wang, Z.2    Franklin, S.L.3    Zovinka, E.P.4    Benkovic, S.J.5
  • 37
    • 0037065696 scopus 로고    scopus 로고
    • Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo- β -lactamase
    • Rasia R. M., Vila A. J., Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo- β -lactamase Biochemistry 2002 41 6 1853 1860
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1853-1860
    • Rasia, R.M.1    Vila, A.J.2
  • 38
    • 0032582569 scopus 로고    scopus 로고
    • Mono- and binuclear Zn- β -lactamase from Bacteroides fragilis: Catalytic and structural roles of the zinc ions
    • Paul-Soto R., Hernadez-Valladares M., Galleni M., Mono- and binuclear Zn- β -lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions FEBS Letters 1998 438 1-2 137 140
    • (1998) FEBS Letters , vol.438 , Issue.1-2 , pp. 137-140
    • Paul-Soto, R.1    Hernadez-Valladares, M.2    Galleni, M.3
  • 39
    • 0035852802 scopus 로고    scopus 로고
    • Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo- β -lactamase from Bacteroides fragilis
    • Fast W., Wang Z., Benkovic S. J., Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo- β -lactamase from Bacteroides fragilis Biochemistry 2001 40 6 1640 1650
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1640-1650
    • Fast, W.1    Wang, Z.2    Benkovic, S.J.3
  • 40
    • 0030931732 scopus 로고    scopus 로고
    • Zn(II) dependence of the Aeromonas hydrophila AE036 metallo- β -lactamase activity and stability
    • Hernandez Valladares M., Felici A., Weber G., Zn(II) dependence of the Aeromonas hydrophila AE036 metallo- β -lactamase activity and stability Biochemistry 1997 36 38 11534 11541
    • (1997) Biochemistry , vol.36 , Issue.38 , pp. 11534-11541
    • Hernandez Valladares, M.1    Felici, A.2    Weber, G.3
  • 41
    • 0031978726 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the cloned metallo- β -lactamase L1 from Stenotrophomonas maltophilia
    • Crowder M. W., Walsh T. R., Banovic L., Pettit M., Spencer J., Overexpression, purification, and characterization of the cloned metallo- β -lactamase L1 from Stenotrophomonas maltophilia Antimicrobial Agents and Chemotherapy 1998 42 4 921 926
    • (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
  • 42
    • 21844455264 scopus 로고    scopus 로고
    • Mode of action of bi- and trinuclear zinc hydrolases and their synthetic analogues
    • Weston J., Mode of action of bi- and trinuclear zinc hydrolases and their synthetic analogues Chemical Reviews 2005 105 6 2151 2174
    • (2005) Chemical Reviews , vol.105 , Issue.6 , pp. 2151-2174
    • Weston, J.1
  • 43
    • 1542304635 scopus 로고    scopus 로고
    • Synthetic analogues relevant to the structure and function of zinc enzymes
    • Parkin G., Synthetic analogues relevant to the structure and function of zinc enzymes Chemical Reviews 2004 104 2 699 768
    • (2004) Chemical Reviews , vol.104 , Issue.2 , pp. 699-768
    • Parkin, G.1
  • 45
    • 0028590042 scopus 로고
    • Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
    • Kiefer L. L., Fierke C. A., Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites Biochemistry 1994 33 51 15233 15240
    • (1994) Biochemistry , vol.33 , Issue.51 , pp. 15233-15240
    • Kiefer, L.L.1    Fierke, C.A.2
  • 46
    • 0035976960 scopus 로고    scopus 로고
    • Thiomandelic acid, a broad spectrum inhibitor of zinc β -lactamases
    • Mollard C., Moali C., Papamicael C., Thiomandelic acid, a broad spectrum inhibitor of zinc β -lactamases Journal of Biological Chemistry 2001 276 48 45015 45023
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.48 , pp. 45015-45023
    • Mollard, C.1    Moali, C.2    Papamicael, C.3
  • 47
    • 20544440614 scopus 로고    scopus 로고
    • Inhibitors of metallo- β -lactamase generated from β -lactam antibiotics
    • Badarau A., Llinás A., Laws A. P., Damblon C., Page M. I., Inhibitors of metallo- β -lactamase generated from β -lactam antibiotics Biochemistry 2005 44 24 8578 8589
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8578-8589
    • Badarau, A.1    Llinás, A.2    Laws, A.P.3    Damblon, C.4    Page, M.I.5
  • 48
    • 0023726228 scopus 로고
    • Comparison of carboxypeptidase a and thermolysin: Inhibition by phosphonamidates
    • Christianson D. W., Lipscomb W. N., Comparison of carboxypeptidase A and thermolysin: inhibition by phosphonamidates Journal of the American Chemical Society 1988 110 16 5560 5565
    • (1988) Journal of the American Chemical Society , vol.110 , Issue.16 , pp. 5560-5565
    • Christianson, D.W.1    Lipscomb, W.N.2
  • 49
    • 0032080039 scopus 로고    scopus 로고
    • The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β -lactamase
    • Bounaga S., Laws A. P., Galleni M., Page M. I., The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β -lactamase Biochemical Journal 1998 331, part 3 703 711
    • (1998) Biochemical Journal , vol.3313 , pp. 703-711
    • Bounaga, S.1    Laws, A.P.2    Galleni, M.3    Page, M.I.4
  • 50
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β -lactamase from Bacteroides fragilis
    • Concha N. O., Rasmussen B. A., Bush K., Herzberg O., Crystal structure of the wide-spectrum binuclear zinc β -lactamase from Bacteroides fragilis Structure 1996 4 7 823 836
    • (1996) Structure , vol.4 , Issue.7 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 51
    • 0032556222 scopus 로고    scopus 로고
    • Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo- β -lactamase from Bacteroides fragilis
    • Wang Z., Fast W., Benkovic S. J., Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo- β -lactamase from Bacteroides fragilis Journal of the American Chemical Society 1998 120 41 10788 10789
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.41 , pp. 10788-10789
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 52
    • 0033520073 scopus 로고    scopus 로고
    • On the mechanism of the metallo- β -lactamase from Bacteroides fragilis
    • Wang Z., Fast W., Benkovic S. J., On the mechanism of the metallo- β -lactamase from Bacteroides fragilis Biochemistry 1999 38 31 10013 10023
    • (1999) Biochemistry , vol.38 , Issue.31 , pp. 10013-10023
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 53
    • 0033514290 scopus 로고    scopus 로고
    • Kinetic mechanism of metallo- β -lactamase L1 from Stenotrophomonas maltophilia
    • McManus-Munoz S., Crowder M. W., Kinetic mechanism of metallo- β -lactamase L1 from Stenotrophomonas maltophilia Biochemistry 1999 38 5 1547 1553
    • (1999) Biochemistry , vol.38 , Issue.5 , pp. 1547-1553
    • McManus-Munoz, S.1    Crowder, M.W.2
  • 54
    • 0035823527 scopus 로고    scopus 로고
    • Novel mechanism of hydrolysis of therapeutic β -lactams by Stenotrophomonas maltophilia L1 metallo- β -lactamase
    • Spencer J., Clarke A. R., Walsh T. R., Novel mechanism of hydrolysis of therapeutic β -lactams by Stenotrophomonas maltophilia L1 metallo- β -lactamase Journal of Biological Chemistry 2001 276 36 33638 33644
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.36 , pp. 33638-33644
    • Spencer, J.1    Clarke, A.R.2    Walsh, T.R.3
  • 55
    • 2942750568 scopus 로고    scopus 로고
    • Mechanistic study of the hydrolysis of nitrocefin mediated by B.cereus metallo- β -lactamase
    • Rasia R. M., Vila A. J., Mechanistic study of the hydrolysis of nitrocefin mediated by B.cereus metallo- β -lactamase ARKIVOC 2003 2003 10 507 516
    • (2003) ARKIVOC , vol.2003 , Issue.10 , pp. 507-516
    • Rasia, R.M.1    Vila, A.J.2
  • 56
    • 0022373155 scopus 로고
    • Cryoenzymology of Bacillus cereus β -lactamase II
    • Bicknell R., Waley S. G., Cryoenzymology of Bacillus cereus β -lactamase II Biochemistry 1985 24 24 6876 6887
    • (1985) Biochemistry , vol.24 , Issue.24 , pp. 6876-6887
    • Bicknell, R.1    Waley, S.G.2
  • 57
    • 10044225894 scopus 로고    scopus 로고
    • A metallo- β -lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • Garau G., Bebrone C., Anne C., Galleni M., Frère J.-M., Dideberg O., A metallo- β -lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem Journal of Molecular Biology 2005 345 4 785 795
    • (2005) Journal of Molecular Biology , vol.345 , Issue.4 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frère, J.-M.5    Dideberg, O.6
  • 58
    • 0036566439 scopus 로고    scopus 로고
    • Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo- β -lactamase
    • de Seny D., Prosperi-Meys C., Bebrone C., Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo- β -lactamase Biochemical Journal 2002 363 687 696
    • (2002) Biochemical Journal , vol.363 , pp. 687-696
    • De Seny, D.1    Prosperi-Meys, C.2    Bebrone, C.3
  • 59
    • 0033056949 scopus 로고    scopus 로고
    • Kinetic properties and metal content of the metallo- β -lactamase CcrA harboring selective amino acid substitutions
    • Yang Y., Keeney D., Tang X., Canfield N., Rasmussen B. A., Kinetic properties and metal content of the metallo- β -lactamase CcrA harboring selective amino acid substitutions Journal of Biological Chemistry 1999 274 22 15706 15711
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.22 , pp. 15706-15711
    • Yang, Y.1    Keeney, D.2    Tang, X.3    Canfield, N.4    Rasmussen, B.A.5
  • 60
    • 0033840714 scopus 로고    scopus 로고
    • Functional analysis of the active site of a metallo- β -lactamase proliferating in Japan
    • Haruta S., Yamaguchi H., Yamamoto E. T., Functional analysis of the active site of a metallo- β -lactamase proliferating in Japan Antimicrobial Agents and Chemotherapy 2000 44 9 2304 2309
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.9 , pp. 2304-2309
    • Haruta, S.1    Yamaguchi, H.2    Yamamoto, E.T.3
  • 61
    • 0347093408 scopus 로고    scopus 로고
    • Metal binding Asp-120 in metallo- β -lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis
    • Garrity J. D., Carenbauer A. L., Herron L. R., Crowder M. W., Metal binding Asp-120 in metallo- β -lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis Journal of Biological Chemistry 2004 279 2 920 927
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 920-927
    • Garrity, J.D.1    Carenbauer, A.L.2    Herron, L.R.3    Crowder, M.W.4
  • 62
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo- β -lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution
    • Ullah J. H., Walsh T. R., Taylor I. A., The crystal structure of the L1 metallo- β -lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution Journal of Molecular Biology 1998 284 1 125 136
    • (1998) Journal of Molecular Biology , vol.284 , Issue.1 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3
  • 63
    • 0345256373 scopus 로고    scopus 로고
    • Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo- β -lactamase
    • Vanhove M., Zakhem M., Devreese B., Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo- β -lactamase Cellular and Molecular Life Sciences 2003 60 11 2501 2509
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.11 , pp. 2501-2509
    • Vanhove, M.1    Zakhem, M.2    Devreese, B.3
  • 64
    • 0035944474 scopus 로고    scopus 로고
    • Dynamics of mononuclear cadmium β -lactamase revealed by the combination of NMR and PAC spectroscopy
    • Hemmingsen L., Damblon C., Antony J., Dynamics of mononuclear cadmium β -lactamase revealed by the combination of NMR and PAC spectroscopy Journal of the American Chemical Society 2001 123 42 10329 10335
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.42 , pp. 10329-10335
    • Hemmingsen, L.1    Damblon, C.2    Antony, J.3
  • 65
    • 0042707576 scopus 로고    scopus 로고
    • The inhibitor thiomandelic acid binds to both metal ions in metallo- β -lactamase and induces positive cooperativity in metal binding
    • Damblon C., Jensen M., Ababou A., The inhibitor thiomandelic acid binds to both metal ions in metallo- β -lactamase and induces positive cooperativity in metal binding Journal of Biological Chemistry 2003 278 31 29240 29251
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 29240-29251
    • Damblon, C.1    Jensen, M.2    Ababou, A.3
  • 66
    • 0032575621 scopus 로고    scopus 로고
    • Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo- β -lactamase that provides multiple antibiotic resistance
    • Wang Z., Benkovic S. J., Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo- β -lactamase that provides multiple antibiotic resistance Journal of Biological Chemistry 1998 273 35 22402 22408
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.35 , pp. 22402-22408
    • Wang, Z.1    Benkovic, S.J.2
  • 67
    • 0032516439 scopus 로고    scopus 로고
    • Spectroscopic characterization of a binuclear metal site in Bacillus cereus β -lactamase II
    • Orellano E. G., Girardini J. E., Cricco J. A., Ceccarelli E. A., Vila A. J., Spectroscopic characterization of a binuclear metal site in Bacillus cereus β -lactamase II Biochemistry 1998 37 28 10173 10180
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10173-10180
    • Orellano, E.G.1    Girardini, J.E.2    Cricco, J.A.3    Ceccarelli, E.A.4    Vila, A.J.5
  • 68
    • 0024514249 scopus 로고
    • Production, purification and spectral properties of metal-dependent β -lactamases of Bacillus cereus
    • Myers J. L., Shaw R. W., Production, purification and spectral properties of metal-dependent β -lactamases of Bacillus cereus Biochimica et Biophysica Acta 1989 995 264 272
    • (1989) Biochimica et Biophysica Acta , vol.995 , pp. 264-272
    • Myers, J.L.1    Shaw, R.W.2
  • 69
    • 0001411337 scopus 로고
    • Cobalt(II) as a probe of the structure and function of carbonic anhydrase
    • Bertini L., Luchinat C., Cobalt(II) as a probe of the structure and function of carbonic anhydrase Accounts of Chemical Research 1983 16 8 272 279
    • (1983) Accounts of Chemical Research , vol.16 , Issue.8 , pp. 272-279
    • Bertini, L.1    Luchinat, C.2
  • 70
    • 35648968634 scopus 로고    scopus 로고
    • Evidence for a dinuclear active site in the metallo- β -lactamase BcII with substoichiometric Co(II)
    • Llarrull L. I., Tioni M. F., Kowalski J., Bennett B., Vila A. J., Evidence for a dinuclear active site in the metallo- β -lactamase BcII with substoichiometric Co(II) Journal of Biological Chemistry 2007 282 42 30586 30595
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30586-30595
    • Llarrull, L.I.1    Tioni, M.F.2    Kowalski, J.3    Bennett, B.4    Vila, A.J.5
  • 71
    • 16444387315 scopus 로고    scopus 로고
    • Spectroscopic studies on cobalt(II)-substituted metallo- β -lactamase ImiS from Aeromonas veronii bv. sobria
    • Crawford P. A., Yang K.-W., Sharma N., Bennett B., Crowder M. W., Spectroscopic studies on cobalt(II)-substituted metallo- β -lactamase ImiS from Aeromonas veronii bv. sobria Biochemistry 2005 44 13 5168 5176
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5168-5176
    • Crawford, P.A.1    Yang, K.-W.2    Sharma, N.3    Bennett, B.4    Crowder, M.W.5
  • 72
    • 3142673911 scopus 로고    scopus 로고
    • Over-expression, purification, and characterization of metallo- β -lactamase ImiS from Aeromonas veronii bv. sobria
    • Crawford P. A., Sharma N., Chandrasekar S., Over-expression, purification, and characterization of metallo- β -lactamase ImiS from Aeromonas veronii bv. sobria Protein Expression and Purification 2004 36 2 272 279
    • (2004) Protein Expression and Purification , vol.36 , Issue.2 , pp. 272-279
    • Crawford, P.A.1    Sharma, N.2    Chandrasekar, S.3
  • 73
    • 12344323483 scopus 로고    scopus 로고
    • Direct evidence that the reaction intermediate of metallo- β -lactamase L1 Is metal bound
    • Garrity J. D., Bennet B., Crowder M. W., Direct evidence that the reaction intermediate of metallo- β -lactamase L1 Is metal bound Biochemistry 2005 44 3 1078 1087
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 1078-1087
    • Garrity, J.D.1    Bennet, B.2    Crowder, M.W.3
  • 74
    • 33748253736 scopus 로고    scopus 로고
    • The variation of catalytic efficiency of Bacillus cereus metallo- β -lactamase with different active site metal ions
    • Badarau A., Page M. I., The variation of catalytic efficiency of Bacillus cereus metallo- β -lactamase with different active site metal ions Biochemistry 2006 45 35 10654 10666
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10654-10666
    • Badarau, A.1    Page, M.I.2
  • 75
    • 33748480347 scopus 로고    scopus 로고
    • Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt- β -lactamase catalyzed hydrolysis of β -lactams
    • Badarau A., Page M. I., Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt- β -lactamase catalyzed hydrolysis of β -lactams Biochemistry 2006 45 36 11012 11020
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 11012-11020
    • Badarau, A.1    Page, M.I.2
  • 76
    • 33846318199 scopus 로고    scopus 로고
    • The activity of the dinuclear cobalt- β -lactamase from Bacillus cereus in catalysing the hydrolysis of β -lactams
    • Badarau A., Damblon C., Page M. I., The activity of the dinuclear cobalt- β -lactamase from Bacillus cereus in catalysing the hydrolysis of β -lactams Biochemical Journal 2007 401, part 1 197 203
    • (2007) Biochemical Journal , vol.4011 , pp. 197-203
    • Badarau, A.1    Damblon, C.2    Page, M.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.