메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

Kinetic Features of L,D-Transpeptidase Inactivation Critical for β-Lactam Antibacterial Activity

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; CEFTRIAXONE; ERTAPENEM; GAMMA GLUTAMYLTRANSFERASE; IMIPENEM;

EID: 84879815727     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067831     Document Type: Article
Times cited : (53)

References (26)
  • 1
    • 39149104344 scopus 로고    scopus 로고
    • Penicillin-binding proteins and beta-lactam resistance
    • Zapun A, Contreras-Martel C, Vernet T, (2008) Penicillin-binding proteins and beta-lactam resistance. FEMS Microbiol Rev 32: 361-385.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 361-385
    • Zapun, A.1    Contreras-Martel, C.2    Vernet, T.3
  • 2
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
    • Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P, (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32: 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 3
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper DJ, Strominger JL, (1965) Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci U S A 54: 1133-1141.
    • (1965) Proc Natl Acad Sci U S A , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 4
    • 39149095622 scopus 로고    scopus 로고
    • Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria
    • Mainardi JL, Villet R, Bugg TD, Mayer C, Arthur M, (2008) Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria. FEMS Microbiol Rev 32: 386-408.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 386-408
    • Mainardi, J.L.1    Villet, R.2    Bugg, T.D.3    Mayer, C.4    Arthur, M.5
  • 5
    • 0034595991 scopus 로고    scopus 로고
    • Novel mechanism of beta-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium
    • Mainardi JL, Legrand R, Arthur M, Schoot B, van Heijenoort J, et al. (2000) Novel mechanism of beta-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium. J Biol Chem 275: 16490-16496.
    • (2000) J Biol Chem , vol.275 , pp. 16490-16496
    • Mainardi, J.L.1    Legrand, R.2    Arthur, M.3    Schoot, B.4    van Heijenoort, J.5
  • 6
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation
    • Lavollay M, Arthur M, Fourgeaud M, Dubost L, Marie A, et al. (2008) The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation. J Bacteriol 190: 4360-4366.
    • (2008) J Bacteriol , vol.190 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5
  • 7
    • 78751490966 scopus 로고    scopus 로고
    • The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidases
    • Lavollay M, Fourgeaud M, Herrmann JL, Dubost L, Marie A, et al. (2011) The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidases. J Bacteriol 193: 778-782.
    • (2011) J Bacteriol , vol.193 , pp. 778-782
    • Lavollay, M.1    Fourgeaud, M.2    Herrmann, J.L.3    Dubost, L.4    Marie, A.5
  • 8
    • 80051695335 scopus 로고    scopus 로고
    • Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links
    • Peltier J, Courtin P, El Meouche I, Lemee L, Chapot-Chartier MP, et al. (2011) Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links. J Biol Chem 286: 29053-29062.
    • (2011) J Biol Chem , vol.286 , pp. 29053-29062
    • Peltier, J.1    Courtin, P.2    El Meouche, I.3    Lemee, L.4    Chapot-Chartier, M.P.5
  • 9
    • 33644689807 scopus 로고    scopus 로고
    • A novel peptidoglycan cross-linking enzyme for a beta-lactam-resistant transpeptidation pathway
    • Mainardi JL, Fourgeaud M, Hugonnet JE, Dubost L, Brouard JP, et al. (2005) A novel peptidoglycan cross-linking enzyme for a beta-lactam-resistant transpeptidation pathway. J Biol Chem 280: 38146-38152.
    • (2005) J Biol Chem , vol.280 , pp. 38146-38152
    • Mainardi, J.L.1    Fourgeaud, M.2    Hugonnet, J.E.3    Dubost, L.4    Brouard, J.P.5
  • 10
    • 35648983979 scopus 로고    scopus 로고
    • Unexpected inhibition of peptidoglycan LD-transpeptidase from Enterococcus faecium by the beta-lactam imipénème
    • Mainardi JL, Hugonnet JE, Rusconi F, Fourgeaud M, Dubost L, et al. (2007) Unexpected inhibition of peptidoglycan LD-transpeptidase from Enterococcus faecium by the beta-lactam imipénème. J Biol Chem 282: 30414-30422.
    • (2007) J Biol Chem , vol.282 , pp. 30414-30422
    • Mainardi, J.L.1    Hugonnet, J.E.2    Rusconi, F.3    Fourgeaud, M.4    Dubost, L.5
  • 11
  • 12
    • 79959539774 scopus 로고    scopus 로고
    • Inactivation kinetics of a new target of beta-lactam antibiotics
    • Triboulet S, Arthur M, Mainardi JL, Veckerle C, Dubee V, et al. (2011) Inactivation kinetics of a new target of beta-lactam antibiotics. J Biol Chem 286: 22777-22784.
    • (2011) J Biol Chem , vol.286 , pp. 22777-22784
    • Triboulet, S.1    Arthur, M.2    Mainardi, J.L.3    Veckerle, C.4    Dubee, V.5
  • 13
  • 14
    • 0037184056 scopus 로고    scopus 로고
    • Balance between two transpeptidation mechanisms determines the expression of beta-lactam resistance in Enterococcus faecium
    • Mainardi JL, Morel V, Fourgeaud M, Cremniter J, Blanot D, et al. (2002) Balance between two transpeptidation mechanisms determines the expression of beta-lactam resistance in Enterococcus faecium. J Biol Chem 277: 35801-35807.
    • (2002) J Biol Chem , vol.277 , pp. 35801-35807
    • Mainardi, J.L.1    Morel, V.2    Fourgeaud, M.3    Cremniter, J.4    Blanot, D.5
  • 15
    • 84870500858 scopus 로고    scopus 로고
    • Targeting the cell wall of Mycobacterium tuberculosis: structure and mechanism of L,D-transpeptidase 2
    • Erdemli SB, Gupta R, Bishai WR, Lamichhane G, Amzel LM, et al. (2012) Targeting the cell wall of Mycobacterium tuberculosis: structure and mechanism of L,D-transpeptidase 2. Structure 20: 2103-2115.
    • (2012) Structure , vol.20 , pp. 2103-2115
    • Erdemli, S.B.1    Gupta, R.2    Bishai, W.R.3    Lamichhane, G.4    Amzel, L.M.5
  • 16
    • 0017284891 scopus 로고
    • Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61
    • Frere J, Ghuysen J, Vanderhaeghe H, Adriaens P, Degelaen J, et al. (1976) Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Nature 260: 451-454.
    • (1976) Nature , vol.260 , pp. 451-454
    • Frere, J.1    Ghuysen, J.2    Vanderhaeghe, H.3    Adriaens, P.4    Degelaen, J.5
  • 17
    • 0018408703 scopus 로고
    • Effects of nucleophiles on the breakdown of the benzylpenicilloyl-enzyme complex EI formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptiase of Streptomyces strain R61
    • Marquet A, Frere JM, Ghuysen JM, Loffet A, (1979) Effects of nucleophiles on the breakdown of the benzylpenicilloyl-enzyme complex EI formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptiase of Streptomyces strain R61. Biochem J 177: 909-916.
    • (1979) Biochem J , vol.177 , pp. 909-916
    • Marquet, A.1    Frere, J.M.2    Ghuysen, J.M.3    Loffet, A.4
  • 18
    • 35649007240 scopus 로고    scopus 로고
    • Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate
    • Hugonnet JE, Blanchard JS, (2007) Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate. Biochemistry 46: 11998-12004.
    • (2007) Biochemistry , vol.46 , pp. 11998-12004
    • Hugonnet, J.E.1    Blanchard, J.S.2
  • 19
    • 61349183785 scopus 로고    scopus 로고
    • Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis
    • Hugonnet JE, Tremblay LW, Boshoff HI, Barry CE IIIrd, Blanchard JS, (2009) Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis. Science 323: 1215-1218.
    • (2009) Science , vol.323 , pp. 1215-1218
    • Hugonnet, J.E.1    Tremblay, L.W.2    Boshoff, H.I.3    Barry IIIrd, C.E.4    Blanchard, J.S.5
  • 20
    • 81255143436 scopus 로고    scopus 로고
    • Fighting resistant tuberculosis with old compounds: the carbapenem paradigm
    • Mainardi JL, Hugonnet JE, Gutmann L, Arthur M, (2011) Fighting resistant tuberculosis with old compounds: the carbapenem paradigm. Clin Microbiol Infect 17: 1755-1756.
    • (2011) Clin Microbiol Infect , vol.17 , pp. 1755-1756
    • Mainardi, J.L.1    Hugonnet, J.E.2    Gutmann, L.3    Arthur, M.4
  • 21
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein Ldt(Mt2) is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • Gupta R, Lavollay M, Mainardi JL, Arthur M, Bishai WR, et al. (2010) The Mycobacterium tuberculosis protein Ldt(Mt2) is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med 16: 466-469.
    • (2010) Nat Med , vol.16 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5
  • 23
    • 84861049632 scopus 로고    scopus 로고
    • Dynamics induced by beta-lactam antibiotics in the active site of Bacillus subtilis L,D-transpeptidase
    • Lecoq L, Bougault C, Hugonnet JE, Veckerle C, Pessey O, et al. (2012) Dynamics induced by beta-lactam antibiotics in the active site of Bacillus subtilis L,D-transpeptidase. Structure 20: 850-861.
    • (2012) Structure , vol.20 , pp. 850-861
    • Lecoq, L.1    Bougault, C.2    Hugonnet, J.E.3    Veckerle, C.4    Pessey, O.5
  • 24
    • 84879750898 scopus 로고    scopus 로고
    • Structure of Enterococcus faecium L,D-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism
    • In press (DOI: 10.1021/cb4001603)
    • Lecoq L, Dubee V, Triboulet S, Bougault C, Hugonnet JE, et al. (2013) Structure of Enterococcus faecium L,D-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism. ACS Chem Biol. In press (DOI: 10.1021/cb4001603).
    • (2013) ACS Chem Biol.
    • Lecoq, L.1    Dubee, V.2    Triboulet, S.3    Bougault, C.4    Hugonnet, J.E.5
  • 25
    • 84875454006 scopus 로고    scopus 로고
    • Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains
    • Kim HS, Kim J, Im HN, Yoon JY, An DR, et al. (2013) Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains. Acta Crystallogr D Biol Crystallogr 69: 420-431.
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 420-431
    • Kim, H.S.1    Kim, J.2    Im, H.N.3    Yoon, J.Y.4    An, D.R.5
  • 26
    • 84877116129 scopus 로고    scopus 로고
    • Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis
    • Li WJ, Li DF, Hu YL, Zhang XE, Bi LJ, et al. (2013) Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis. Cell Res 23: 728-731.
    • (2013) Cell Res , vol.23 , pp. 728-731
    • Li, W.J.1    Li, D.F.2    Hu, Y.L.3    Zhang, X.E.4    Bi, L.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.