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Volumn 5, Issue 11, 2013, Pages 1243-1263

Targeting metallo-β-lactamase enzymes in antibiotic resistance

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; BETA LACTAM ANTIBIOTIC; BIPHENYL DERIVATIVE; BIPHENYL TETRAZOLE; CEPHALOSPORIN DERIVATIVE; CYCLOBUTANONE DERIVATIVE; DICARBOXYLIC ACID DERIVATIVE; DNA; HETEROCYCLIC DICARBOXYLIC ACID; MERCAPTOACETIC ACID THIOESTER DERIVATIVE; METALLO BETA LACTAMASE; PENICILLIN DERIVATIVE; PEPTIDE INHIBITOR; PROTEIN INHIBITOR; PYRIDINE DERIVATIVE; PYRROLE DERIVATIVE; SUCCINIC ACID DERIVATIVE; TETRAZOLE DERIVATIVE; THIOGLYCOLIC ACID DERIVATIVE; THIOL DERIVATIVE; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; ZINC ION;

EID: 84893391938     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.55     Document Type: Review
Times cited : (55)

References (82)
  • 1
    • 84867040298 scopus 로고    scopus 로고
    • In Antibiotic Discovery and Development. Dougherty TJ, Pucci MJ (Eds). Springer, NY, USA
    • Page MGP. Beta-lactam antibiotics. In: Antibiotic Discovery and Development. Dougherty TJ, Pucci MJ (Eds). Springer, NY, USA, 79-117 (2012).
    • (2012) Beta-lactam Antibiotics , pp. 79-117
    • Page, M.G.P.1
  • 2
    • 0020972419 scopus 로고
    • Penicillin-binding proteins and the mechanism of action of b-lactam antibiotics
    • Waxman DJ, Strominger JL. Penicillin-binding proteins and the mechanism of action of b-lactam antibiotics. Annu. Rev. Biochem. 52, 825-869 (1983).
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 825-869
    • Waxman, D.J.1    Strominger, J.L.2
  • 3
    • 0000123301 scopus 로고
    • An enzyme from bacteria able to destroy penicillin
    • Abraham EP, Chain E. An enzyme from bacteria able to destroy penicillin. Nature 146, 837-837 (1940).
    • (1940) Nature , vol.146 , pp. 837-837
    • Abraham, E.P.1    Chain, E.2
  • 4
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-b-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone C. Metallo-b-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem. Pharmacol. 74(12), 1686-1701 (2007).
    • (2007) Biochem. Pharmacol. , vol.74 , Issue.12 , pp. 1686-1701
    • Bebrone, C.1
  • 5
    • 0013865825 scopus 로고
    • Zinc as a cofactor for cephalosporinase from Bacillus cereus 569
    • Sabath LD, Abraham EP. Zinc as a cofactor for cephalosporinase from Bacillus cereus 569. Biochem. J. 98(1), 11c-13c (1966).
    • (1966) Biochem. J. , vol.98 , Issue.1
    • Sabath, L.D.1    Abraham, E.P.2
  • 7
    • 0025041530 scopus 로고
    • Cloning and sequencing of the class B beta-lactamase gene (CcrA) from Bacteriodes fragilis TAL3636
    • Rasmussen BA, Gluzman Y, Tally FP. Cloning and sequencing of the class B beta-lactamase gene (CcrA) from Bacteriodes fragilis TAL3636. Antimicrob. Agents Chemother. 34, 1590-1592 (1990).
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 1590-1592
    • Rasmussen, B.A.1    Gluzman, Y.2    Tally, F.P.3
  • 8
    • 0025875773 scopus 로고
    • The Aeromonas hydrophila CphA gene: Molecular heterogeneity among class B metallo-beta-lactamases
    • Massidda O, Rossolini GM, Satta G. The Aeromonas hydrophila CphA gene: Molecular heterogeneity among class B metallo-beta-lactamases. J. Bacteriol. 173, 4611-4617 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 4611-4617
    • Massidda, O.1    Rossolini, G.M.2    Satta, G.3
  • 9
    • 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, Duée E, et al.: The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14(20), 4914-4921 (1995).
    • (1995) EMBO J. , vol.14 , Issue.20 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3
  • 11
    • 0022648089 scopus 로고
    • Aztreonam A review of its antibacterial activity, pharmacokinetic properties and therapeutic use
    • Brogden RN, Heel RC. Aztreonam. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs 31(2), 96-130 (1986).
    • (1986) Drugs , vol.31 , Issue.2 , pp. 96-130
    • Brogden, R.N.1    Heel, R.C.2
  • 13
    • 84855808713 scopus 로고    scopus 로고
    • Biapenem inactivation by B2 metallo b-lactamase: Energy landscape of the post-hydolysis reactions
    • doi:10.1371/journal.pone.0030079 Epub ahead of print
    • Gatti DL. Biapenem inactivation by B2 metallo b-lactamase: Energy landscape of the post-hydolysis reactions. PLoS ONE doi:10.1371/journal.pone. 0030079 (2012) (Epub ahead of print).
    • (2012) PLoS ONE
    • Gatti, D.L.1
  • 14
    • 0037014621 scopus 로고    scopus 로고
    • IMP-1 metallo-beta-lactamase: Effects of chelators and assessment of metal requirement by electrospray mass spectrometry
    • Siemann S, Brewer D, Clarke AJ, Dmitrienko GI, Lajoie G, Viswanatha T. IMP-1 metallo-beta-lactamase: Effects of chelators and assessment of metal requirement by electrospray mass spectrometry. Biochem. Biophys. Acta 1571(3), 190-200 (2002).
    • (2002) Biochem. Biophys. Acta , vol.1571 , Issue.3 , pp. 190-200
    • Siemann, S.1    Brewer, D.2    Clarke, A.J.3    Dmitrienko, G.I.4    Lajoie, G.5    Viswanatha, T.6
  • 15
    • 0029449149 scopus 로고
    • Therapeutic iron chelators and their potential side-effects
    • Singh S, Khodr H, Taylor MI, Hider RC. Therapeutic iron chelators and their potential side-effects. Biochem. Soc. Symp. 61, 127-138 (1995).
    • (1995) Biochem. Soc. Symp. , vol.61 , pp. 127-138
    • Singh, S.1    Khodr, H.2    Taylor, M.I.3    Hider, R.C.4
  • 18
    • 77955618651 scopus 로고    scopus 로고
    • Role of changes in the L3 loop of the active site in the evolution of enzymatic activity of VIM-Type metallo-b-lactamases
    • Merino M, Pérez-Llarena FJ, Kerff F, et al.: Role of changes in the L3 loop of the active site in the evolution of enzymatic activity of VIM-Type metallo-b-lactamases. J. Antimicrob. Chemother. 65(9), 1950-1954 (2010).
    • (2010) J. Antimicrob. Chemother. , vol.65 , Issue.9 , pp. 1950-1954
    • Merino, M.1    Pérez-Llarena, F.J.2    Kerff, F.3
  • 19
    • 84860389616 scopus 로고    scopus 로고
    • Crystal structure of New Delhi metallo-b-lactamase reveals molecular basis for antibiotic resistance
    • King D, Strynadka N. Crystal structure of New Delhi metallo-b-lactamase reveals molecular basis for antibiotic resistance. Protein Sci. 20(9), 1484-1491 (2011).
    • (2011) Protein Sci. , vol.20 , Issue.9 , pp. 1484-1491
    • King, D.1    Strynadka, N.2
  • 20
    • 37349007671 scopus 로고    scopus 로고
    • The three-dimensional structure of VIM-2, a Zn-b-lactamase from Pseudomonas aeruginosa in its reduced and oxidized form
    • Garcia-Saez I, Docquier J, Rossolini GM, Dideberg O. The three-dimensional structure of VIM-2, a Zn-b-lactamase from Pseudomonas aeruginosa in its reduced and oxidized form. J. Mol. Biol. 375, 604-611 (2008).
    • (2008) J. Mol. Biol. , vol.375 , pp. 604-611
    • Garcia-Saez, I.1    Docquier, J.2    Rossolini, G.M.3    Dideberg, O.4
  • 21
    • 0034681922 scopus 로고    scopus 로고
    • Crystal Structure of the IMP-1 metallo b-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • Concha NO, Janson CA, Rowling P, et al.: Crystal Structure of the IMP-1 metallo b-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39, 4288-4298 (2000).
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3
  • 22
    • 0037399075 scopus 로고    scopus 로고
    • Analysis of the importance of the metallo-b-lactamase active site loop in substrate binding and catalysis
    • Moali C, Anne C, Lamotte-Brasseur J, Groslambert S, Devreese B, Van Beeuman J. Analysis of the importance of the metallo-b-lactamase active site loop in substrate binding and catalysis. Chem. Biol. 10, 319-329 (2003).
    • (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
  • 23
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-b-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, Dideberg O. A metallo-b-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J. Mol. Biol. 345(4), 785-795 (2004).
    • (2004) J. Mol. Biol. , vol.345 , Issue.4 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frère, J.5    Dideberg, O.6
  • 24
    • 84866417151 scopus 로고    scopus 로고
    • Binuclear metallohydrolases: Complex mechanistic strategies for a simple chemical reaction
    • Schenk G, Mitic N, Gahan LR, Ollis DL, McGeary RP, Guddat LW. Binuclear metallohydrolases: Complex mechanistic strategies for a simple chemical reaction. Acc. Chem. Res. 45(9), 1593-1603 (2012).
    • (2012) Acc. Chem. Res. , vol.45 , Issue.9 , pp. 1593-1603
    • Schenk, G.1    Mitic, N.2    Gahan, L.R.3    Ollis, D.L.4    McGeary, R.P.5    Guddat, L.W.6
  • 25
    • 45349100770 scopus 로고    scopus 로고
    • The mechanisms of catalysis by metallo b-lactamases
    • Page MI, Badarau A. The mechanisms of catalysis by metallo b-lactamases. Bioinorg. Chem. Appl. 2008, 576297 (2008).
    • (2008) Bioinorg. Chem. Appl. , vol.2008 , pp. 576297
    • Page, M.I.1    Badarau, A.2
  • 26
    • 0037462925 scopus 로고    scopus 로고
    • 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
    • Garcia-Saez I, Mercuri PS, Papamicael C, et al.: 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 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 651-660
    • Garcia-Saez, I.1    Mercuri, P.S.2    Papamicael, C.3
  • 27
    • 80052552771 scopus 로고    scopus 로고
    • Structure of Apo-And monometalated forms of NDM-1-A highly potent carbapenem-hydrolyzing metallo-b-lactamase
    • Kim Y, Tesar C, Jedrzejczak R, et al.: Structure of Apo-And monometalated forms of NDM-1-A highly potent carbapenem-hydrolyzing metallo-b-lactamase. PLoS ONE 6(9), e24621 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.9
    • Kim, Y.1    Tesar, C.2    Jedrzejczak, R.3
  • 28
    • 33947199145 scopus 로고    scopus 로고
    • Role of zinc content on the catalytic efficiency of B1 metallo b-lactamases
    • Peraro MD, Vila AJ, Carloni P, Klein ML. Role of zinc content on the catalytic efficiency of B1 metallo b-lactamases. J. Am. Chem. Soc. 129(10), 2808-2816 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.10 , pp. 2808-2816
    • Peraro, M.D.1    Vila, A.J.2    Carloni, P.3    Klein, M.L.4
  • 29
    • 7944238165 scopus 로고    scopus 로고
    • Analysis of the context dependent sequence requirements of active site residues in the metallo-b-lactamase IMP-1
    • Materon IC, Beharry Z, Huang W, Perez C, Palzkill T. Analysis of the context dependent sequence requirements of active site residues in the metallo-b-lactamase IMP-1. J. Mol. Biol. 344(3), 653-663 (2004).
    • (2004) J. Mol. Biol. , vol.344 , Issue.3 , pp. 653-663
    • Materon, I.C.1    Beharry, Z.2    Huang, W.3    Perez, C.4    Palzkill, T.5
  • 30
    • 79957618735 scopus 로고    scopus 로고
    • Crystal structure of NDM-1 reveals a common b-lactam hydrolysis mechanism
    • Zhang H, Hao Q. Crystal structure of NDM-1 reveals a common b-lactam hydrolysis mechanism. FASEB J. 25(8), 2574-2582 (2011).
    • (2011) FASEB J. , vol.25 , Issue.8 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 31
    • 84863976350 scopus 로고    scopus 로고
    • New Delhi metallo-b-lactamase: Structural insights into b-lactam recognition and inhibition
    • King DT, Worrall LJ, Gruninger R, Strynadka NCJ. New Delhi metallo-b-lactamase: Structural insights into b-lactam recognition and inhibition. J. Am. Chem Soc. 134(28), 11362-11365 (2012).
    • (2012) J. Am. Chem Soc. , vol.134 , Issue.28 , pp. 11362-11365
    • King, D.T.1    Worrall, L.J.2    Gruninger, R.3    Strynadka, N.C.J.4
  • 32
    • 33646855255 scopus 로고    scopus 로고
    • Catalytic mechanism of class B2 metallo-b-lactamase
    • Xu D, Xie D, Guo H. Catalytic mechanism of class B2 metallo-b-lactamase. J. Biol. Chem. 281(13), 8740-8747 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.13 , pp. 8740-8747
    • Xu, D.1    Xie, D.2    Guo, H.3
  • 33
    • 80051672898 scopus 로고    scopus 로고
    • Crystal structure of Serratia fonticola Sfh-I: Activation of the nucleophile in mono-zinc metallo-b-lactamases
    • Fonseca F, Bromley EH, Saavedra MJ, Correia A, Spencer J. Crystal structure of Serratia fonticola Sfh-I: Activation of the nucleophile in mono-zinc metallo-b-lactamases. J. Mol. Biol. 411, 951-959 (2011).
    • (2011) J. Mol. Biol. , vol.411 , pp. 951-959
    • Fonseca, F.1    Bromley, E.H.2    Saavedra, M.J.3    Correia, A.4    Spencer, J.5
  • 34
    • 26844434108 scopus 로고    scopus 로고
    • Antibiotic recognition by binuclear metallo-beta-lactamases revealed by x-ray crystallography
    • Spencer J, Read J, Sessions RB, Howell S, Blackburn GM, Gamblin SJ. Antibiotic recognition by binuclear metallo-beta-lactamases revealed by x-ray crystallography. J. Am. Chem. Soc. 127, 14439-14444 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14439-14444
    • Spencer, J.1    Read, J.2    Sessions, R.B.3    Howell, S.4    Blackburn, G.M.5    Gamblin, S.J.6
  • 35
    • 56349139534 scopus 로고    scopus 로고
    • The porin and the permeating antibiotic: A selective barrier in Gram-negative bacteria
    • Pagès J-M, James CE, Winterhalter M. The porin and the permeating antibiotic: A selective barrier in Gram-negative bacteria. Nat. Rev. Microbiol. 6(12), 893-903 (2008).
    • (2008) Nat. Rev. Microbiol. , vol.6 , Issue.12 , pp. 893-903
    • Pagès, J.-M.1    James, C.E.2    Winterhalter, M.3
  • 36
    • 0024605207 scopus 로고
    • A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus Evidence for the direct interaction between the essential metal ion and substrate
    • Murphy, Brian P, Pratt RF. A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for the direct interaction between the essential metal ion and substrate. Biochem. J. 258, 765-768 (1989).
    • (1989) Biochem. J. , vol.258 , pp. 765-768
    • Murphy Brian, P.1    Pratt, R.F.2
  • 38
    • 20544440614 scopus 로고    scopus 로고
    • Inhibitors of metallo-b-lactamase generated from b-lactam antibiotics
    • Badarau A, Llinás A, Laws AP, et al.: Inhibitors of metallo-b-lactamase generated from b-lactam antibiotics. Biochemistry. 44, 8578-8589 (2005).
    • (2005) Biochemistry. , vol.44 , pp. 8578-8589
    • Badarau, A.1    Llinás, A.2    Laws, A.P.3
  • 39
    • 0034819514 scopus 로고    scopus 로고
    • Inactivation of Aeromonas hydrophila metallo-b-lactamase by cephamycins and moxalactam
    • Zervosen A, Valladares MH, Devreese B, et al.: Inactivation of Aeromonas hydrophila metallo-b-lactamase by cephamycins and moxalactam. Eur. J. Biochem. 268, 3840-3850 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3840-3850
    • Zervosen, A.1    Valladares, M.H.2    Devreese, B.3
  • 40
    • 1242316384 scopus 로고    scopus 로고
    • 2004 Penicillin-derived inhibitors that simultaneously target both metallo-And serine-beta-lactamases
    • Buynak JD, Chen H, Vogeti L, et al.: 2004. Penicillin-derived inhibitors that simultaneously target both metallo-And serine-beta-lactamases. Bioorg. Med. Chem. Lett. 14(5), 1299-1304 (2004).
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , Issue.5 , pp. 1299-1304
    • Buynak, J.D.1    Chen, H.2    Vogeti, L.3
  • 41
    • 0037399075 scopus 로고    scopus 로고
    • Analysis of the importance of the metallo-b-lactamase active site loop in substrate binding and catalysis
    • Moali C, Anne C, Lamotte-Brasseur J, et al.: Analysis of the importance of the metallo-b-lactamase active site loop in substrate binding and catalysis. Chem. Biol. 10(4), 319-329 (2003).
    • (2003) Chem. Biol. , vol.10 , Issue.4 , pp. 319-329
    • Moali, C.1    Anne, C.2    Lamotte-Brasseur, J.3
  • 42
    • 0033517787 scopus 로고    scopus 로고
    • NMR characterization of the metallo-b-lactamase from Bacteriodes fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop
    • Scrofani SDB, Chung J, Huntley JJA, Benkovic SJ, Wright PE, Dyson HJ. NMR characterization of the metallo-b-lactamase from Bacteriodes fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop. Biochemistry. 38, 14507-14514 (1999).
    • (1999) Biochemistry. , vol.38 , pp. 14507-14514
    • Scrofani, S.D.B.1    Chung, J.2    Huntley, J.J.A.3    Benkovic, S.J.4    Wright, P.E.5    Dyson, H.J.6
  • 43
    • 0032879868 scopus 로고    scopus 로고
    • Carbapenem derivatives as potential inhibitors of various b-lactamases, including class B metallo-b-lactamases
    • Nagano R, Adachi Y, Imamura H, Yamada K, Hashizume T, Morishima H. Carbapenem derivatives as potential inhibitors of various b-lactamases, including class B metallo-b-lactamases. Antimicrob. Agents Chemother. 43(10), 2497-2503 (1999).
    • (1999) Antimicrob. Agents Chemother. , vol.43 , Issue.10 , pp. 2497-2503
    • Nagano, R.1    Adachi, Y.2    Imamura, H.3    Yamada, K.4    Hashizume, T.5    Morishima, H.6
  • 44
    • 0034051621 scopus 로고    scopus 로고
    • In vitro antibacterial activity and mechanism of action of J-111 ,225, a novel 1b-methylcarbapenem, against transferable IMP-1 metallo-b-lactamase producers
    • Nagano R, Adachi Y, Hashizume T, Morishima H. In vitro antibacterial activity and mechanism of action of J-111,225, a novel 1b-methylcarbapenem, against transferable IMP-1 metallo-b-lactamase producers. J. Antimicrob. Chemother. 45, 271-276 (2000).
    • (2000) J. Antimicrob. Chemother. , vol.45 , pp. 271-276
    • Nagano, R.1    Adachi, Y.2    Hashizume, T.3    Morishima, H.4
  • 45
    • 33746748748 scopus 로고    scopus 로고
    • Structure-Activity relationship of 6-methylidene penems bearing 6,5 bicyclic heterocycles as broad-spectrum b-lactamase inhibitors: Evidence for 1,4-Thiazopine intermediates with C7 R stereochemistry by computational methods
    • Venkatesan AM, Agarwal A, Abe T, et al.: Structure-Activity relationship of 6-methylidene penems bearing 6,5 bicyclic heterocycles as broad-spectrum b-lactamase inhibitors: Evidence for 1,4-Thiazopine intermediates with C7 R stereochemistry by computational methods. J. Med. Chem. 49. 4623-4637 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 4623-4637
    • Venkatesan, A.M.1    Agarwal, A.2    Abe, T.3
  • 46
    • 52449105960 scopus 로고    scopus 로고
    • Cyclobutanone mimics of penicillins: Effects of substitution on conformation and hemiketal stability
    • Johnson JW, Evanoff DP, Savard ME, et al.: Cyclobutanone mimics of penicillins: Effects of substitution on conformation and hemiketal stability. J. Org. Chem. 73, 6970-6982 (2008).
    • (2008) J. Org. Chem. , vol.73 , pp. 6970-6982
    • Johnson, J.W.1    Evanoff, D.P.2    Savard, M.E.3
  • 47
    • 77950411087 scopus 로고    scopus 로고
    • Cyclobutanone analogues of b-lactams revisited: Insights into conformational requirements for inhibition of serine-And Metallo-b-lactamases
    • Johnson JW, Gretes M, Goodfellow VJ, et al.: Cyclobutanone analogues of b-lactams revisited: Insights into conformational requirements for inhibition of serine-And Metallo-b-lactamases. J. Am. Chem. Soc. 132, 2558-2560 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2558-2560
    • Johnson, J.W.1    Gretes, M.2    Goodfellow, V.J.3
  • 48
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: A critical biological partnership
    • Maret W. Zinc and sulfur: A critical biological partnership. Biochemistry. 43(12), 3301-3309 (2004).
    • (2004) Biochemistry. , vol.43 , Issue.12 , pp. 3301-3309
    • Maret, W.1
  • 49
    • 0038419647 scopus 로고    scopus 로고
    • Coordination geometries of metal ions in d-or l-captopril-inhibited metallo-b-lactamases
    • Heinz U, Bauer R, Wommer S, et al.: Coordination geometries of metal ions in d-or l-captopril-inhibited metallo-b-lactamases. J. Biol. Chem. 278(23), 20659-20666 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.23 , pp. 20659-20666
    • Heinz, U.1    Bauer, R.2    Wommer, S.3
  • 50
    • 0037592222 scopus 로고    scopus 로고
    • The 1.5Å structure of chryseobacterium meningosepticum zinc b-lactamase in complex with the inhibitor, d-captopril
    • García-Sáez I, Hopkins J, Papamicael C, et al.: The 1.5Å Structure of Chryseobacterium meningosepticum zinc b-lactamase in complex with the inhibitor, d-captopril. J. Biol. Chem. 278, 23868-23873 (2004).
    • (2004) J. Biol. Chem. , vol.278 , pp. 23868-23873
    • García-Sáez, I.1    Hopkins, J.2    Papamicael, C.3
  • 51
    • 36448989329 scopus 로고    scopus 로고
    • Structural insights into the design of inhibitors for the L1 metallo-b-lactamase from Stenotrophomonas maltophilia
    • Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O. Structural insights into the design of inhibitors for the L1 metallo-b-lactamase from Stenotrophomonas maltophilia. J. Mol. Biol. 375, 257-269 (2008).
    • (2008) J. Mol. Biol. , vol.375 , pp. 257-269
    • Nauton, L.1    Kahn, R.2    Garau, G.3    Hernandez, J.F.4    Dideberg, O.5
  • 52
    • 45449088355 scopus 로고    scopus 로고
    • Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols
    • Liénard BM, Garau L, Horsfall L, et al.: Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols. Org. Biomol. Chem. 6(13), 2282-2294 (2008).
    • (2008) Org. Biomol. Chem. , vol.6 , Issue.13 , pp. 2282-2294
    • Liénard, B.M.1    Garau, L.2    Horsfall, L.3
  • 53
    • 33747348451 scopus 로고    scopus 로고
    • Homo-cysteinyl peptide inhibitors of the L1 metallo-b-lactamase, and SAR as determined by combinatorial library synthesis
    • Sun Q, Law A, Crowder MW, Geysen HM. Homo-cysteinyl peptide inhibitors of the L1 metallo-b-lactamase, and SAR as determined by combinatorial library synthesis. Bioorg. Med. Chem. Lett. 16(19), 6169-5175 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , Issue.19 , pp. 6169-5175
    • Sun, Q.1    Law, A.2    Crowder, M.W.3    Geysen, H.M.4
  • 54
    • 0035078014 scopus 로고    scopus 로고
    • Cyseinyl peptide inhibitors of Bacillus cereus zinc b-lactamase
    • Bounaga S, Galleni M, Laws AP, Page MI. Cyseinyl peptide inhibitors of Bacillus cereus zinc b-lactamase. Bioorg. Med. Chem. 9, 503-510 (2001).
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 503-510
    • Bounaga, S.1    Galleni, M.2    Laws, A.P.3    Page, M.I.4
  • 55
    • 37349001297 scopus 로고    scopus 로고
    • Crystallographic investigation of the inhibition mode of a VIM-2 metallo-b-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor
    • Yamaguchi Y, Jin W, Matsunaga K, et al.: Crystallographic investigation of the inhibition mode of a VIM-2 metallo-b-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor. J. Med. Chem. 50, 6647-6653 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 6647-6653
    • Yamaguchi, Y.1    Jin, W.2    Matsunaga, K.3
  • 56
    • 0031391773 scopus 로고    scopus 로고
    • Inhibition of the metallo-b-lactamase produced from Serratia marcescens by thiol compounds
    • Goto M, Takahashi T, Yamashita F, et al.: Inhibition of the metallo-b-lactamase produced from Serratia marcescens by thiol compounds. Biol. Pharm. Bull. 20(11), 1136-1140 (1997).
    • (1997) Biol. Pharm. Bull. , vol.20 , Issue.11 , pp. 1136-1140
    • Goto, M.1    Takahashi, T.2    Yamashita, F.3
  • 57
    • 0035976960 scopus 로고    scopus 로고
    • Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: Kinetic and spectroscopic studies
    • Mollard C, Moali C, Papamicael C, et al.: Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: Kinetic and spectroscopic studies. J. Biol. Chem. 276(48), 45015-45023 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.48 , pp. 45015-45023
    • Mollard, C.1    Moali, C.2    Papamicael, C.3
  • 58
    • 0042707576 scopus 로고    scopus 로고
    • The inhibitor thiomandelic acid binds to both metal ions in metallo-b-lactamase and induces positive cooperativity in metal binding
    • Damblon C, Jensen M, Ababou A, et al.: The inhibitor thiomandelic acid binds to both metal ions in metallo-b-lactamase and induces positive cooperativity in metal binding. J. Biol. Chem. 278(31), 29240-29251 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.31 , pp. 29240-29251
    • Damblon, C.1    Jensen, M.2    Ababou, A.3
  • 59
    • 33749030701 scopus 로고    scopus 로고
    • Probing, inhibition, and crystallographic characterization of metallo-b-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups
    • Kurosaki H, Yamaguchi Y, Yasuzawa H, Jin W, Yamagata Y, Arakawa Y. Probing, inhibition, and crystallographic characterization of metallo-b-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups. Chem Med Chem 1, 969-972 (2006).
    • (2006) Chem Med Chem , vol.1 , pp. 969-972
    • Kurosaki, H.1    Yamaguchi, Y.2    Yasuzawa, H.3    Jin, W.4    Yamagata, Y.5    Arakawa, Y.6
  • 60
    • 21244446747 scopus 로고    scopus 로고
    • Irreversible inhibition of metallo-b-lactamase (IMP-1) by 3-(3-mercaptopropionylsulfanyl)-propionic acid pentafluorophenyl ester
    • Kurosaki H, Yamaguchi Y, Higashi T, et al.: Irreversible inhibition of metallo-b-lactamase (IMP-1) by 3-(3-mercaptopropionylsulfanyl)-propionic acid pentafluorophenyl ester. Angew. Chem. Int. Ed. Engl. 44, 3861-3864 (2005).
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 3861-3864
    • Kurosaki, H.1    Yamaguchi, Y.2    Higashi, T.3
  • 61
    • 0035943678 scopus 로고    scopus 로고
    • Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-b-lactamase
    • Toney JH, Hammond GG, Fitzgerald PMD, et al.: Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-b-lactamase. J. Biol. Chem. 276(34), 31913-31918 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 31913-31918
    • Toney, J.H.1    Hammond, G.G.2    Fitzgerald, P.M.D.3
  • 62
    • 12844264250 scopus 로고    scopus 로고
    • Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1
    • Moloughney JG, Thomas J, Toney JH. Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1. FEMS Microbiol. Lett. 243(1), 65-71 (2005).
    • (2005) FEMS Microbiol. Lett. , vol.243 , Issue.1 , pp. 65-71
    • Moloughney, J.G.1    Thomas, J.2    Toney, J.H.3
  • 63
    • 77956116298 scopus 로고    scopus 로고
    • In vitro potentiation of carbapenems with ME1071, a novel metallo-b-lactamase producing Pseudomonas aeruginosa clinical isolates
    • Ishii Y, Eto M, Mano Y, Tateda K, Yamaguchi K. In vitro potentiation of carbapenems with ME1071, a novel metallo-b-lactamase producing Pseudomonas aeruginosa clinical isolates. Antimicrob. Agents Chemother. 54(9), 3625-3629 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.9 , pp. 3625-3629
    • Ishii, Y.1    Eto, M.2    Mano, Y.3    Tateda, K.4    Yamaguchi, K.5
  • 64
    • 68349152498 scopus 로고    scopus 로고
    • Metallo-b-lactamase inhibitory activity of phthalic acid derivatives
    • Hiraiwa Y, Morinaka A, Fukushima T, et al.: Metallo-b-lactamase inhibitory activity of phthalic acid derivatives. Bioorg. Med. Chem. Lett. 19, 5162-5165 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5162-5165
    • Hiraiwa, Y.1    Morinaka, A.2    Fukushima, T.3
  • 65
    • 0031020833 scopus 로고    scopus 로고
    • Inhibition of metallo-b-lactamases by a series of mercaptoacetic acid thiol derivatives
    • Payne DJ, Bateson JH, Gasson BC, et al.: Inhibition of metallo-b-lactamases by a series of mercaptoacetic acid thiol derivatives. Antimicrob. Agents Chemother. 41(1), 135-140 (1997).
    • (1997) Antimicrob. Agents Chemother. , vol.41 , Issue.1 , pp. 135-140
    • Payne, D.J.1    Bateson, J.H.2    Gasson, B.C.3
  • 66
    • 0031416125 scopus 로고    scopus 로고
    • Inhibition of metallo-b-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid
    • Payne DJ, Bateson JH, Gasson BC, et al.: Inhibition of metallo-b-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid. FEMS Microbiol. Lett. 157, 171-175 (1997).
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 171-175
    • Payne, D.J.1    Bateson, J.H.2    Gasson, B.C.3
  • 67
    • 0032842513 scopus 로고    scopus 로고
    • Inhibition of IMP-1 metallo-b-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives
    • Hammond GG, Huber JL, Greenlee ML, et al.: Inhibition of IMP-1 metallo-b-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives. FEMS Microbiol. Lett. 459, 289-296 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.459 , pp. 289-296
    • Hammond, G.G.1    Huber, J.L.2    Greenlee, M.L.3
  • 68
    • 0033530093 scopus 로고    scopus 로고
    • Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-b-lactamase
    • Greenlee ML, Laub JB, Balkovec JM, et al.: Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-b-lactamase. Bioorg. Med. Chem. Lett. 9, 2549-2554 (1999).
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2549-2554
    • Greenlee, M.L.1    Laub, J.B.2    Balkovec, J.M.3
  • 69
    • 84866631880 scopus 로고    scopus 로고
    • Synthesis and kinetic testing of tetrahydropyrimidine-2-Thione and pyrrole derivatives as inhibitors of the metallo-b-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
    • Hussein WM, Fatahala SS, Mohamed ZM, et al.: Synthesis and kinetic testing of tetrahydropyrimidine-2-Thione and pyrrole derivatives as inhibitors of the metallo-b-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Chem. Biol. Drug Des. 80(4), 500-515 (2012).
    • (2012) Chem. Biol. Drug Des. , vol.80 , Issue.4 , pp. 500-515
    • Hussein, W.M.1    Fatahala, S.S.2    Mohamed, Z.M.3
  • 70
    • 80955151611 scopus 로고    scopus 로고
    • Synthesis and kinetic testing of new inhibitors for a metallo-b-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
    • Mohamed MS, Hussein WM, McGeary RP, Vella P, Schenk G, Abd El-Hameed RH. Synthesis and kinetic testing of new inhibitors for a metallo-b-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Eur. J. Med. Chem. 46(12), 6075-6082 (2011).
    • (2011) Eur. J. Med. Chem. , vol.46 , Issue.12 , pp. 6075-6082
    • Mohamed, M.S.1    Hussein, W.M.2    McGeary, R.P.3    Vella, P.4    Schenk, G.5    Abd El-Hameed, R.H.6
  • 71
    • 34250214527 scopus 로고    scopus 로고
    • Competitive inhibitors of the CphA metallo-b-lactamase from Aeromonas hydrophila
    • Horsfall LE, Garau G, Liénard BMR, et al.: Competitive inhibitors of the CphA metallo-b-lactamase from Aeromonas hydrophila. Antimicrob. Agents Chemother. 51(6), 2136-2142 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.6 , pp. 2136-2142
    • Horsfall, L.E.1    Garau, G.2    Liénard, B.M.R.3
  • 73
    • 77955915532 scopus 로고    scopus 로고
    • NH-1 ,2,3-Triazole inhibitors of the VIM-2 metallo-b-lactamase
    • Weide T, Saldanha SA, Minond D, et al.: NH-1,2,3-Triazole inhibitors of the VIM-2 metallo-b-lactamase. ACS Med. Chem. Lett. 1(4), 150-154 (2010).
    • (2010) ACS Med. Chem. Lett. , vol.1 , Issue.4 , pp. 150-154
    • Weide, T.1    Saldanha, S.A.2    Minond, D.3
  • 75
    • 14744282967 scopus 로고    scopus 로고
    • A specific peptide inhibitor of the class B metallo-b-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display
    • Sanschagrin F, Levesque RC. A specific peptide inhibitor of the class B metallo-b-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display. J. Antimicrob. Chemother. 55, 252-255 (2005).
    • (2005) J. Antimicrob. Chemother. , vol.55 , pp. 252-255
    • Sanschagrin, F.1    Levesque, R.C.2
  • 76
    • 0036096423 scopus 로고    scopus 로고
    • Identification of a series of tricylic natural products as potent broad-spectrum inhibitors of metallo-b-lactamase
    • Payne DJ, Hueso-Rodríguez JA, Boyd H, et al.: Identification of a series of tricylic natural products as potent broad-spectrum inhibitors of metallo-b-lactamase. Antimicrob. Agents Chemother. 46, 1880-1886 (2002).
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1880-1886
    • Payne, D.J.1    Hueso-Rodríguez, J.A.2    Boyd, H.3
  • 79
    • 78049300941 scopus 로고    scopus 로고
    • Efficacy of calcium-EDTA as an inhibitor for metallo-b-lactamase in a mouse model of Pseudomonas aeruginosa pneumonia
    • Aoki N, Ishii Y, Tateda K, et al.: Efficacy of calcium-EDTA as an inhibitor for metallo-b-lactamase in a mouse model of Pseudomonas aeruginosa pneumonia. Antimicrob. Agents Chemother. 54(11), 4582-4588 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.11 , pp. 4582-4588
    • Aoki, N.1    Ishii, Y.2    Tateda, K.3
  • 80
    • 13144295022 scopus 로고    scopus 로고
    • Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-b-lactamase
    • Toney JH, Fitzgerald PMD, Grover-Sharma N, et al.: Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-b-lactamase. Chem. Biol. 5, 185-196 (1998).
    • (1998) Chem. Biol. , vol.5 , pp. 185-196
    • Toney, J.H.1    Fitzgerald, P.M.D.2    Grover-Sharma, N.3
  • 81
    • 0033588861 scopus 로고    scopus 로고
    • Structure-Activity relationships of biphenyl tetrazoles as metallo-b-lactamase Inhibitors
    • Toney JH, Cleary KA, Hammond GG, et al.: Structure-Activity relationships of biphenyl tetrazoles as metallo-b-lactamase Inhibitors. Bioorg. Med. Chem Lett. 9, 2741-2746 (1999).
    • (1999) Bioorg. Med. Chem Lett. , vol.9 , pp. 2741-2746
    • Toney, J.H.1    Cleary, K.A.2    Hammond, G.G.3
  • 82
    • 84864417937 scopus 로고    scopus 로고
    • N-Heterocyclic dicarboxylic acids: Broad-spectrum inhibitors of metallo-b-lactamases with co-Antibacterial effect against antibiotic-resistant bacteria
    • Feng L, Yang K-W, Zhou L-S, et al.: N-Heterocyclic dicarboxylic acids: Broad-spectrum inhibitors of metallo-b-lactamases with co-Antibacterial effect against antibiotic-resistant bacteria. Bioorg. Med. Chem. Lett. 22, 5185-5189 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 5185-5189
    • Feng, L.1    Yang, K.-W.2    Zhou, L.-S.3


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