메뉴 건너뛰기




Volumn 58, Issue 9, 2014, Pages 5372-5378

Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMPICILLIN; BETA LACTAM ANTIBIOTIC; CARBAPENEM DERIVATIVE; CEFEPIME; CEPHALOSPORIN DERIVATIVE; ERTAPENEM; IMIPENEM; MEROPENEM; METALLO BETA LACTAMASE; ANTIINFECTIVE AGENT; BETA LACTAMASE; BETA-LACTAMASE NDM-1;

EID: 84906095863     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01977-13     Document Type: Article
Times cited : (41)

References (32)
  • 1
    • 77957770819 scopus 로고    scopus 로고
    • Alarming beta-lactamase-mediated resistance in multi-drug-resistant Enterobacteriaceae
    • Bush K. 2010. Alarming beta-lactamase-mediated resistance in multi-drug-resistant Enterobacteriaceae. Curr. Opin. Microbiol. 13:558-564. http://dx.doi.org/10.1016/j.mib.2010.09.006.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 558-564
    • Bush, K.1
  • 2
    • 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. http://dx.doi.org/10.1128/AAC.39.6.1211.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 3
    • 77149165713 scopus 로고    scopus 로고
    • Updated functional classification of beta-lactamases
    • Bush K, Jacoby GA. 2010. Updated functional classification of beta-lactamases. Antimicrob. Agents Chemother. 54:969-976. http://dx.doi.org/10. 1128/AAC.01009-09.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 969-976
    • Bush, K.1    Jacoby, G.A.2
  • 4
    • 80053247739 scopus 로고    scopus 로고
    • Epidemiological expansion, structural studies, and clinical challenges of new beta-lactamases from Gram-negative bacteria
    • Bush K, Fisher JF. 2011. Epidemiological expansion, structural studies, and clinical challenges of new beta-lactamases from Gram-negative bacteria. Annu. Rev. Microbiol. 65:455-478. http://dx.doi.org/10.1146/annurev-micro- 090110-102911.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 455-478
    • Bush, K.1    Fisher, J.F.2
  • 7
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • Drawz SM, Bonomo RA. 2010. Three decades of beta-lactamase inhibitors. Clin. Microbiol. Rev. 23:160-201. http://dx.doi.org/10.1128/CMR.00037-09.
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 8
    • 71249134038 scopus 로고    scopus 로고
    • NDM-1, and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India
    • NDM-1, and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India. Antimicrob. Agents Chemother. 53:5046-5054. http://dx.doi.org/10.1128/AAC.00774-09.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 5046-5054
    • Yong, D.1    Toleman, M.A.2    Giske, C.G.3    Cho, H.S.4    Sundman, K.5    Lee, K.6    Walsh, T.R.7
  • 10
    • 37349007671 scopus 로고    scopus 로고
    • The Three-Dimensional Structure of VIM-2, a Zn-beta-Lactamase from Pseudomonas aeruginosa in Its Reduced and Oxidised Form
    • DOI 10.1016/j.jmb.2007.11.012, PII S0022283607014726
    • Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O. 2008. The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J. Mol. Biol. 375:604-611. http://dx.doi.org/10.1016/j.jmb.2007.11.012. (Pubitemid 350297297)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.3 , pp. 604-611
    • Garcia-Saez, I.1    Docquier, J.-D.2    Rossolini, G.M.3    Dideberg, O.4
  • 11
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • DOI 10.1021/bi992569m
    • Concha NO, Janson CA, Rowling P, Pearson S, Cheever CA, Clarke BP, Lewis C, Galleni M, Frere JM, Payne DJ, Bateson JH, Abdel-Mequid SS. 2000. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39:4288-4298. http://dx.doi.org/10.1021/bi992569m. (Pubitemid 30212644)
    • (2000) Biochemistry , vol.39 , Issue.15 , 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    Lewis, C.7    Galleni, M.8    Frere, J.-M.9    Payne, D.J.10    Bateson, J.H.11    Abdel-Meguid, S.S.12
  • 12
    • 33644948482 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases
    • Murphy TA, Catto LE, Halford SE, Hadfield AT, Minor W, Walsh TR, Spencer J. 2006. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases. J. Mol. Biol. 357:890-903. http://dx.doi.org/10.1016/j.jmb.2006.01.003.
    • (2006) J. Mol. Biol. , vol.357 , pp. 890-903
    • Murphy, T.A.1    Catto, L.E.2    Halford, S.E.3    Hadfield, A.T.4    Minor, W.5    Walsh, T.R.6    Spencer, J.7
  • 13
    • 0031833739 scopus 로고    scopus 로고
    • 1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus
    • Carfi A, Duee E, Galleni M, Frere JM, Dideberg O. 1998. 1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus. Acta Crystallogr. D Biol. Crystallogr. 54:313-323. http://dx.doi.org/10.1107/ S0907444997010627.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 313-323
    • Carfi, A.1    Duee, E.2    Galleni, M.3    Frere, J.M.4    Dideberg, O.5
  • 14
    • 79957618735 scopus 로고    scopus 로고
    • Crystal structure of NDM-1 reveals a common beta-lactam hydrolysis mechanism
    • Zhang H, Hao Q. 2011. Crystal structure of NDM-1 reveals a common beta-lactam hydrolysis mechanism. FASEB J. 25:2574-2582. http://dx.doi.org/10. 1096/fj.11-184036.
    • (2011) FASEB J. , vol.25 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 15
    • 0036566439 scopus 로고    scopus 로고
    • Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase
    • DOI 10.1042/0264-6021:3630687
    • de Seny D, Prosperi-Meys C, Bebrone C, Rossolini GM, Page MI, Noel P, Frere JM, Galleni M. 2002. Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase. Biochem. J. 363:687-696. http://dx.doi.org/10.1042/0264-6021:3630687. (Pubitemid 34526389)
    • (2002) Biochemical Journal , vol.363 , Issue.3 , pp. 687-696
    • De Seny, D.1    Prosperi-Meys, C.2    Bebrone, C.3    Rossolini, G.M.4    Page, M.I.5    Noel, P.6    Frere, J.-M.7    Galleni, M.8
  • 16
    • 0033520073 scopus 로고    scopus 로고
    • On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis
    • Wang Z, Fast W, Benkovic SJ. 1999. On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis. Biochemistry 38:10013-10023. http://dx.doi.org/10.1021/bi990356r.
    • (1999) Biochemistry , vol.38 , pp. 10013-10023
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 17
    • 84863976350 scopus 로고    scopus 로고
    • New Delhi metallo-beta-lactamase: Structural insights into beta-lactam recognition and inhibition
    • King DT, Worrall LJ, Gruninger R, Strynadka NC. 2012. New Delhi metallo-beta-lactamase: structural insights into beta-lactam recognition and inhibition. J. Am. Chem. Soc. 134:11362-11365. http://dx.doi.org/10.1021/ ja303579d.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11362-11365
    • King, D.T.1    Worrall, L.J.2    Gruninger, R.3    Strynadka, N.C.4
  • 18
    • 14144255746 scopus 로고    scopus 로고
    • Impact of remote mutations on metallo-beta-lactamase substrate specificity: Implications for the evolution of antibiotic resistance
    • DOI 10.1110/ps.041093405
    • Oelschlaeger P, Mayo SL, Pleiss J. 2005. Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci. 14:765-774. http://dx.doi.org/10.1110/ps. 041093405. (Pubitemid 40283915)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 765-774
    • Oelschlaeger, P.1    Mayo, S.L.2    Pleiss, J.3
  • 19
    • 0037399075 scopus 로고    scopus 로고
    • Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis
    • Moali C, Anne C, Lamotte-Brasseur J, Groslambert S, Devreese B, Van Beeumen J, Galleni M, Frere JM. 2003. Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis. Chem. Biol. 10: 319 -329. http://dx.doi.org/10.1016/S1074-5521(03)00070-X.
    • (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 Beeumen, J.6    Galleni, M.7    Frere, J.M.8
  • 20
    • 37349001297 scopus 로고    scopus 로고
    • Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor
    • DOI 10.1021/jm701031n
    • Yamaguchi Y, Jin W, Matsunaga K, Ikemizu S, Yamagata Y, Wachino J, Shibata N, Arakawa Y, Kurosaki H. 2007. Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor. J. Med. Chem. 50:6647-6653. http://dx.doi.org/10.1021/jm701031n. (Pubitemid 350309101)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.26 , pp. 6647-6653
    • Yamaguchi, Y.1    Jin, W.2    Matsunaga, K.3    Ikemizu, S.4    Yamagata, Y.5    Wachino, J.-I.6    Shibata, N.7    Arakawa, Y.8    Kurosaki, H.9
  • 23
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31:455-461. http://dx.doi.org/10.1002/jcc. 21334.
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 25
    • 81255195336 scopus 로고    scopus 로고
    • Characterization of purified New Delhi metallo-beta-lactamase-1
    • Thomas PW, Zheng M, Wu S, Guo H, Liu D, Xu D, Fast W. 2011. Characterization of purified New Delhi metallo-beta-lactamase-1. Biochemistry 50:10102-10113. http://dx.doi.org/10.1021/bi201449r.
    • (2011) Biochemistry , vol.50 , pp. 10102-10113
    • Thomas, P.W.1    Zheng, M.2    Wu, S.3    Guo, H.4    Liu, D.5    Xu, D.6    Fast, W.7
  • 26
    • 80052552771 scopus 로고    scopus 로고
    • Structure of apo- and monometalated forms of NDM-1 - A highly potent carbapenem-hydrolyzing metallo-beta-lactamase
    • Kim Y, Tesar C, Mire J, Jedrzejczak R, Binkowski A, Babnigg G, Sacchettini J, Joachimiak A. 2011. Structure of apo- and monometalated forms of NDM-1 - a highly potent carbapenem-hydrolyzing metallo-beta-lactamase. PLoS One 6:e24621. http://dx.doi.org/10.1371/journal.pone.0024621.
    • (2011) PLoS One , vol.6
    • Kim, Y.1    Tesar, C.2    Mire, J.3    Jedrzejczak, R.4    Binkowski, A.5    Babnigg, G.6    Sacchettini, J.7    Joachimiak, A.8
  • 27
    • 0038648570 scopus 로고    scopus 로고
    • Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase
    • DOI 10.1110/ps.0305303
    • Huntley JJ, Fast W, Benkovic SJ, Wright PE, Dyson HJ. 2003. Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase. Protein Sci. 12:1368-1375. http://dx.doi.org/10.1110/ps.0305303. (Pubitemid 36759341)
    • (2003) Protein Science , vol.12 , Issue.7 , pp. 1368-1375
    • Huntley, J.J.A.1    Fast, W.2    Benkovic, S.J.3    Wright, P.E.4    Dyson, H.J.5
  • 28
    • 81555201969 scopus 로고    scopus 로고
    • Analysis of the functional contributions of Asn233 in metallo-betalactamase IMP-1
    • Brown NG, Horton LB, Huang W, Vongpunsawad S, Palzkill T. 2011. Analysis of the functional contributions of Asn233 in metallo-betalactamase IMP-1. Antimicrob. Agents Chemother. 55:5696-5702. http://dx.doi.org/10.1128/AAC.00340- 11.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 5696-5702
    • Brown, N.G.1    Horton, L.B.2    Huang, W.3    Vongpunsawad, S.4    Palzkill, T.5
  • 29
    • 33748274756 scopus 로고    scopus 로고
    • II-containing metallo-beta-lactamase ImiS from Aeromonas sobria
    • DOI 10.1021/bi060893t
    • Sharma NP, Hajdin C, Chandrasekar S, Bennett B, Yang KW, Crowder MW. 2006. Mechanistic studies on the mononuclear ZnII-containing metallo-beta-lactamase ImiS from Aeromonas sobria. Biochemistry 45:10729-10738. http://dx.doi.org/10.1021/bi060893t. (Pubitemid 44320488)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10729-10738
    • Sharma, N.P.1    Hajdin, C.2    Chandrasekar, S.3    Bennett, B.4    Yang, K.-W.5    Crowder, M.W.6
  • 30
    • 0035190707 scopus 로고    scopus 로고
    • Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection
    • DOI 10.1110/ps.ps.40884
    • Materon IC, Palzkill T. 2001. Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection. Protein Sci. 10:2556-2565. http://dx.doi.org/10.1110/ps.ps.40884. (Pubitemid 33091580)
    • (2001) Protein Science , vol.10 , Issue.12 , pp. 2556-2565
    • Materon, I.C.1    Palzkill, T.2
  • 32
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-beta-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. http://dx.doi.org/10.1016/j.jmb.2004.10.070. (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.