메뉴 건너뛰기




Volumn 59, Issue 1, 2016, Pages 474-479

Exploring the Mechanism of β-Lactam Ring Protonation in the Class A β-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CEFOTAXIME; ENZYME; GLUTAMIC ACID; LIGAND; LYSINE; PROTEIN; SERINE; ANTIINFECTIVE AGENT; BETA LACTAM; ENZYME INHIBITOR;

EID: 84955112630     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b01215     Document Type: Article
Times cited : (43)

References (36)
  • 2
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M β-lactamases: Extended spectrum activities from increased mobility and decreased stability
    • Chen, Y.; Delmas, J.; Sirot, J.; Shoichet, B.; Bonnet, R. Atomic resolution structures of CTX-M β-lactamases: Extended spectrum activities from increased mobility and decreased stability J. Mol. Biol. 2005, 348, 349-362 10.1016/j.jmb.2005.02.010
    • (2005) J. Mol. Biol. , vol.348 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, J.3    Shoichet, B.4    Bonnet, R.5
  • 3
    • 0033082703 scopus 로고    scopus 로고
    • The β-lactamase cycle: A tale of selective pressure and bacterial ingenuity
    • Matagne, A.; Dubus, A.; Galleni, M.; Frere, J. M. The β-lactamase cycle: a tale of selective pressure and bacterial ingenuity Nat. Prod. Rep. 1999, 16, 1-19 10.1039/a705983c
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 1-19
    • Matagne, A.1    Dubus, A.2    Galleni, M.3    Frere, J.M.4
  • 4
    • 0028821830 scopus 로고
    • Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure
    • Knox, J. R. Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: mutations, specificity, and three-dimensional structure Antimicrob. Agents Chemother. 1995, 39, 2593-2601 10.1128/AAC.39.12.2593
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2593-2601
    • Knox, J.R.1
  • 5
    • 0347362476 scopus 로고    scopus 로고
    • Growing group of extended-spectrum β-lactamases: The CTX-M enzymes
    • Bonnet, R. Growing group of extended-spectrum β-lactamases: The CTX-M enzymes Antimicrob. Agents Chemother. 2004, 48, 1-14 10.1128/AAC.48.1.1-14.2004
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1-14
    • Bonnet, R.1
  • 6
    • 0032032930 scopus 로고    scopus 로고
    • Catalytic properties of class A β-lactamases: Efficiency and diversity
    • Matagne, A.; Lamotte-Brasseur, J.; Frere, J. M. Catalytic properties of class A β-lactamases: efficiency and diversity Biochem. J. 1998, 330, 581-598 10.1042/bj3300581
    • (1998) Biochem. J. , vol.330 , pp. 581-598
    • Matagne, A.1    Lamotte-Brasseur, J.2    Frere, J.M.3
  • 7
    • 0034056878 scopus 로고    scopus 로고
    • CTX-M-type β-lactamases: An emerging group of extended-spectrum enzymes
    • Tzouvelekis, L. S.; Tzelepi, E.; Tassios, P. T.; Legakis, N. J. CTX-M-type β-lactamases: an emerging group of extended-spectrum enzymes Int. J. Antimicrob. Agents 2000, 14, 137-142 10.1016/S0924-8579(99)00165-X
    • (2000) Int. J. Antimicrob. Agents , vol.14 , pp. 137-142
    • Tzouvelekis, L.S.1    Tzelepi, E.2    Tassios, P.T.3    Legakis, N.J.4
  • 8
    • 0028986292 scopus 로고
    • TEM-derived and SHV-derived extended-spectrum β-lactamases - Relationship between selection, structure and function
    • Dubois, S. K.; Marriott, M. S.; Amyes, S. G. B. TEM-derived and SHV-derived extended-spectrum β-lactamases-relationship between selection, structure and function J. Antimicrob. Chemother. 1995, 35, 7-22 10.1093/jac/35.1.7
    • (1995) J. Antimicrob. Chemother. , vol.35 , pp. 7-22
    • Dubois, S.K.1    Marriott, M.S.2    Amyes, S.G.B.3
  • 10
    • 0029121020 scopus 로고
    • Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A β-lactamase isolated from Escherichia coli
    • Ishii, Y.; Ohno, A.; Taguchi, H.; Imajo, S.; Ishiguro, M.; Matsuzawa, H. Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A β-lactamase isolated from Escherichia coli Antimicrob. Agents Chemother. 1995, 39, 2269-2275 10.1128/AAC.39.10.2269
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2269-2275
    • Ishii, Y.1    Ohno, A.2    Taguchi, H.3    Imajo, S.4    Ishiguro, M.5    Matsuzawa, H.6
  • 11
    • 34247857459 scopus 로고    scopus 로고
    • The acylation mechanism of CTX-M β-lactamase at 0.88 angstrom resolution
    • Chen, Y.; Bonnet, R.; Shoichet, B. K. The acylation mechanism of CTX-M β-lactamase at 0.88 angstrom resolution J. Am. Chem. Soc. 2007, 129, 5378-5380 10.1021/ja0712064
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5378-5380
    • Chen, Y.1    Bonnet, R.2    Shoichet, B.K.3
  • 12
    • 0037094114 scopus 로고    scopus 로고
    • An ultrahigh resolution structure of TEM-1 β-lactamase suggests a role for Glu166 as the general base in acylation
    • Minasov, G.; Wang, X. J.; Shoichet, B. K. An ultrahigh resolution structure of TEM-1 β-lactamase suggests a role for Glu166 as the general base in acylation J. Am. Chem. Soc. 2002, 124, 5333-5340 10.1021/ja0259640
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5333-5340
    • Minasov, G.1    Wang, X.J.2    Shoichet, B.K.3
  • 13
    • 0028237904 scopus 로고
    • Site-directed mutagenesis of glutamate-166 in β-lactamase leads to a branched path mechanism
    • Escobar, W. A.; Tan, A. K.; Lewis, E. R.; Fink, A. L. Site-directed mutagenesis of glutamate-166 in β-lactamase leads to a branched path mechanism Biochemistry 1994, 33, 7619-7626 10.1021/bi00190a015
    • (1994) Biochemistry , vol.33 , pp. 7619-7626
    • Escobar, W.A.1    Tan, A.K.2    Lewis, E.R.3    Fink, A.L.4
  • 14
    • 0023204095 scopus 로고
    • Bacterial resistance to beta-lactam antibiotics: Crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution
    • Herzberg, O.; Moult, J. Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution Science 1987, 236, 694-701 10.1126/science.3107125
    • (1987) Science , vol.236 , pp. 694-701
    • Herzberg, O.1    Moult, J.2
  • 15
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution
    • Strynadka, N. C.; Adachi, H.; Jensen, S. E.; Johns, K.; Sielecki, A.; Betzel, C.; Sutoh, K.; James, M. N. Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution Nature 1992, 359, 700-5 10.1038/359700a0
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.1    Adachi, H.2    Jensen, S.E.3    Johns, K.4    Sielecki, A.5    Betzel, C.6    Sutoh, K.7    James, M.N.8
  • 16
    • 27644522933 scopus 로고    scopus 로고
    • Ab initio QM/MM study of class A β-lactamase acylation: Dual participation of Glu166 and Lys73 in a concerted base promotion of Ser70
    • Meroueh, S. O.; Fisher, J. F.; Schlegel, H. B.; Mobashery, S. Ab initio QM/MM study of class A β-lactamase acylation: Dual participation of Glu166 and Lys73 in a concerted base promotion of Ser70 J. Am. Chem. Soc. 2005, 127, 15397-15407 10.1021/ja051592u
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15397-15407
    • Meroueh, S.O.1    Fisher, J.F.2    Schlegel, H.B.3    Mobashery, S.4
  • 17
    • 0031041590 scopus 로고    scopus 로고
    • Site-directed mutagenesis of glutamate 166 in two beta-lactamases - Kinetic and molecular modeling studies
    • Guillaume, G.; Vanhove, M.; LamotteBrasseur, J.; Ledent, P.; Jamin, M.; Joris, B.; Frere, J. M. Site-directed mutagenesis of glutamate 166 in two beta-lactamases-Kinetic and molecular modeling studies J. Biol. Chem. 1997, 272, 5438-5444 10.1074/jbc.272.9.5438
    • (1997) J. Biol. Chem. , vol.272 , pp. 5438-5444
    • Guillaume, G.1    Vanhove, M.2    LamotteBrasseur, J.3    Ledent, P.4    Jamin, M.5    Joris, B.6    Frere, J.M.7
  • 18
    • 0027461951 scopus 로고
    • A Catalytically-Impaired Class-A Beta-Lactamase - 2 Angstrom Crystal-Structure and Kinetics of the Bacillus-Licheniformis E166a Mutant
    • Knox, J. R.; Moews, P. C.; Escobar, W. A.; Fink, A. L. A Catalytically-Impaired Class-a Beta-Lactamase-2 Angstrom Crystal-Structure and Kinetics of the Bacillus-Licheniformis E166a Mutant Protein Eng., Des. Sel. 1993, 6, 11-18 10.1093/protein/6.1.11
    • (1993) Protein Eng., Des. Sel. , vol.6 , pp. 11-18
    • Knox, J.R.1    Moews, P.C.2    Escobar, W.A.3    Fink, A.L.4
  • 19
    • 4544384195 scopus 로고    scopus 로고
    • The importance of a critical protonation state and the fate of the catalytic steps in class A β-lactamases and penicillin-binding proteins
    • Golemi-Kotra, D.; Meroueh, S. O.; Kim, C.; Vakulenko, S. B.; Bulychev, A.; Stemmler, A. J.; Stemmler, T. L.; Mobashery, S. The importance of a critical protonation state and the fate of the catalytic steps in class A β-lactamases and penicillin-binding proteins J. Biol. Chem. 2004, 279, 34665-34673 10.1074/jbc.M313143200
    • (2004) J. Biol. Chem. , vol.279 , pp. 34665-34673
    • Golemi-Kotra, D.1    Meroueh, S.O.2    Kim, C.3    Vakulenko, S.B.4    Bulychev, A.5    Stemmler, A.J.6    Stemmler, T.L.7    Mobashery, S.8
  • 20
    • 0032562183 scopus 로고    scopus 로고
    • Crystal structure of an acylation transition-state analog of the TEM-1 β-lactamase. Mechanistic implications for class A β-lactamases
    • Maveyraud, L.; Pratt, R. F.; Samama, J. P. Crystal structure of an acylation transition-state analog of the TEM-1 β-lactamase. Mechanistic implications for class A β-lactamases Biochemistry 1998, 37, 2622-2628 10.1021/bi972501b
    • (1998) Biochemistry , vol.37 , pp. 2622-2628
    • Maveyraud, L.1    Pratt, R.F.2    Samama, J.P.3
  • 22
    • 76849096440 scopus 로고    scopus 로고
    • The catalytic efficiency (k(cat)/K-m) of the class A β-lactamase Toho-1 correlates with the thermal stability of its catalytic intermediate analog
    • Nitanai, Y.; Shimamura, T.; Uchiyama, T.; Ishii, Y.; Takehira, M.; Yutani, K.; Matsuzawa, H.; Miyano, M. The catalytic efficiency (k(cat)/K-m) of the class A β-lactamase Toho-1 correlates with the thermal stability of its catalytic intermediate analog Biochim. Biophys. Acta, Proteins Proteomics 2010, 1804, 684-691 10.1016/j.bbapap.2009.10.023
    • (2010) Biochim. Biophys. Acta, Proteins Proteomics , vol.1804 , pp. 684-691
    • Nitanai, Y.1    Shimamura, T.2    Uchiyama, T.3    Ishii, Y.4    Takehira, M.5    Yutani, K.6    Matsuzawa, H.7    Miyano, M.8
  • 23
    • 70449585313 scopus 로고    scopus 로고
    • Neutron macromolecular crystallography
    • Blakeley, M. P. Neutron macromolecular crystallography Crystallogr. Rev. 2009, 15, 157-218 10.1080/08893110902965003
    • (2009) Crystallogr. Rev. , vol.15 , pp. 157-218
    • Blakeley, M.P.1
  • 24
    • 70350787183 scopus 로고    scopus 로고
    • Deuterium labeling for neutron structure-function-dynamics analysis
    • Meilleur, F.; Weiss, K. L.; Myles, D. A. A. Deuterium labeling for neutron structure-function-dynamics analysis Methods Mol. Biol. (N. Y., NY, U. S.) 2009, 544, 281-92 10.1007/978-1-59745-483-418
    • (2009) Methods Mol. Biol. (N. Y., NY, U. S.) , vol.544 , pp. 281-292
    • Meilleur, F.1    Weiss, K.L.2    Myles, D.A.A.3
  • 25
    • 77952471388 scopus 로고    scopus 로고
    • The macromolecular neutron diffractometer (MaNDi) at the Spallation Neutron Source, Oak Ridge: Enhanced optics design, high-resolution neutron detectors and simulated diffraction
    • Coates, L.; Stoica, A. D.; Hoffmann, C.; Richards, J.; Cooper, R. The macromolecular neutron diffractometer (MaNDi) at the Spallation Neutron Source, Oak Ridge: enhanced optics design, high-resolution neutron detectors and simulated diffraction J. Appl. Crystallogr. 2010, 43, 570-577 10.1107/S0021889810008587
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 570-577
    • Coates, L.1    Stoica, A.D.2    Hoffmann, C.3    Richards, J.4    Cooper, R.5
  • 26
    • 34247857459 scopus 로고    scopus 로고
    • The acylation mechanism of CTX-M β-lactamase at 0.88 angstrom resolution
    • Chen, Y.; Bonnet, R.; Shoichet, B. K. The acylation mechanism of CTX-M β-lactamase at 0.88 angstrom resolution J. Am. Chem. Soc. 2007, 129, 5378-5380 10.1021/ja0712064
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5378-5380
    • Chen, Y.1    Bonnet, R.2    Shoichet, B.K.3
  • 29
    • 78651374505 scopus 로고    scopus 로고
    • The active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation
    • Tomanicek, S. J.; Wang, K. K.; Weiss, K. L.; Blakeley, M. P.; Cooper, J.; Chen, Y.; Coates, L. The active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation FEBS Lett. 2011, 585, 364-368 10.1016/j.febslet.2010.12.017
    • (2011) FEBS Lett. , vol.585 , pp. 364-368
    • Tomanicek, S.J.1    Wang, K.K.2    Weiss, K.L.3    Blakeley, M.P.4    Cooper, J.5    Chen, Y.6    Coates, L.7
  • 30
    • 2242480185 scopus 로고    scopus 로고
    • Acyl-intermediate structures of the extended-spectrum class A β-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin
    • Shimamura, T.; Ibuka, A.; Fushinobu, S.; Wakagi, T.; Ishiguro, M.; Ishii, Y.; Matsuzawa, H. Acyl-intermediate structures of the extended-spectrum class A β-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin J. Biol. Chem. 2002, 277, 46601-46608 10.1074/jbc.M207884200
    • (2002) J. Biol. Chem. , vol.277 , pp. 46601-46608
    • Shimamura, T.1    Ibuka, A.2    Fushinobu, S.3    Wakagi, T.4    Ishiguro, M.5    Ishii, Y.6    Matsuzawa, H.7
  • 31
    • 17644390560 scopus 로고    scopus 로고
    • Structure, function, and inhibition along the reaction coordinate of CTX-M β-lactamases
    • Chen, Y.; Shoichet, B.; Bonnet, R. Structure, function, and inhibition along the reaction coordinate of CTX-M β-lactamases J. Am. Chem. Soc. 2005, 127, 5423-5434 10.1021/ja042850a
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5423-5434
    • Chen, Y.1    Shoichet, B.2    Bonnet, R.3
  • 32
    • 0041818050 scopus 로고    scopus 로고
    • Crystal structure of extended-spectrum β-lactamase Toho-1: Insights into the molecular mechanism for catalytic reaction and substrate specificity expansion
    • Ibuka, A. S.; Ishii, Y.; Galleni, M.; Ishiguro, M.; Yamaguchi, K.; Frere, J. M.; Matsuzawa, H.; Sakai, H. Crystal structure of extended-spectrum β-lactamase Toho-1: Insights into the molecular mechanism for catalytic reaction and substrate specificity expansion Biochemistry 2003, 42, 10634-10643 10.1021/bi0342822
    • (2003) Biochemistry , vol.42 , pp. 10634-10643
    • Ibuka, A.S.1    Ishii, Y.2    Galleni, M.3    Ishiguro, M.4    Yamaguchi, K.5    Frere, J.M.6    Matsuzawa, H.7    Sakai, H.8
  • 33
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
    • Strynadka, N. C. J.; Adachi, H.; Jensen, S. E.; Johns, K.; Sielecki, A.; Betzel, C.; Sutoh, K.; James, M. N. G. Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution Nature 1992, 359, 700-705 10.1038/359700a0
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.J.1    Adachi, H.2    Jensen, S.E.3    Johns, K.4    Sielecki, A.5    Betzel, C.6    Sutoh, K.7    James, M.N.G.8
  • 34
    • 0025768209 scopus 로고
    • Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G
    • Lamotte-Brasseur, J.; Dive, G.; Dideberg, O.; Charlier, P.; Frere, J. M.; Ghuysen, J. M. Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G Biochem. J. 1991, 279, 213-221 10.1042/bj2790213
    • (1991) Biochem. J. , vol.279 , pp. 213-221
    • Lamotte-Brasseur, J.1    Dive, G.2    Dideberg, O.3    Charlier, P.4    Frere, J.M.5    Ghuysen, J.M.6
  • 35
    • 0034724334 scopus 로고    scopus 로고
    • Protonation of the β-lactam nitrogen is the trigger event in the catalytic action of class A β-lactamases
    • Atanasov, B. P.; Mustafi, D.; Makinen, M. W. Protonation of the β-lactam nitrogen is the trigger event in the catalytic action of class A β-lactamases Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 3160-3165 10.1073/pnas.97.7.3160
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3160-3165
    • Atanasov, B.P.1    Mustafi, D.2    Makinen, M.W.3
  • 36
    • 21644480798 scopus 로고    scopus 로고
    • Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM-lactamase
    • Thomas, V. L.; Golemi-Kotra, D.; Kim, C.; Vakulenko, S. B.; Mobashery, S.; Shoichet, B. K. Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM-lactamase Biochemistry 2005, 44, 9330-9338 10.1021/bi0502700
    • (2005) Biochemistry , vol.44 , pp. 9330-9338
    • Thomas, V.L.1    Golemi-Kotra, D.2    Kim, C.3    Vakulenko, S.B.4    Mobashery, S.5    Shoichet, B.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.