Chemical shift perturbations induced by the acylation of Enterococcus faecium l,d-transpeptidase catalytic cysteine with ertapenem

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• 作者：Lauriane Lecoq ; Catherine Bougault ; Sébastien Triboulet…
• 关键词：l ; d ; Transpeptidase ; Carbapenem ; β ; Lactam ; Peptidoglycan ; NMR resonance assignment
• 刊名：Biomolecular NMR Assignments
• 出版年：2014
• 出版时间：October 2014
• 年：2014
• 卷：8
• 期：2
• 页码：339-343
• 全文大小：2,784 KB
• 参考文献：1. Biarrotte-Sorin S, Hugonnet JE, Delfosse V, Mainardi JL, Gutmann L, Arthur M, Mayer C (2006) Crystal structure of a novel β-lactam-insensitive peptidoglycan transpeptidase. J Mol Biol 359:533-38 CrossRef
  2. Bielnicki J, Devedjiev Y, Derewenda U, Dauter Z, Joachimiak A, Derewenda ZS (2005) / B. subtilis YkuD protein at 2.0 ? resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins: Struct Funct Genet 62:144-51 CrossRef
  3. Dubée V, Arthur M, Fief H, Triboulet S, Mainardi JL, Gutmann L, Sollogoub M, Rice LB, Ethève-Quelquejeu M, Hugonnet JE (2012) Kinetic analysis of / Enterococcus faecium l,d -transpeptidase inactivation by carbapenems. Antimicrob Agents Chemother 56:3409-412 CrossRef
  4. Erdemli SB, Gupta R, Bishai WR, Lamichhane G, Amzel LM, Bianchet MA (2012) Targeting the cell wall of / Mycobacterium tuberculosis: structure and mechanism of l,d -transpeptidase 2. Structure?20:1-3 CrossRef
  5. Lavollay M, Fourgeaud M, Herrmann JL, Dubost L, Marie A, Gutmann L, Arthur M, Mainardi JL (2011) The peptidoglycan of / Mycobacterium abscessus is predominantly cross-linked by l,d -transpeptidases. J Bacteriol 193:778-82 CrossRef
  6. Lecoq L, Bougault C, Hugonnet JE, Veckerlé C, Pessey O, Arthur M, Simorre JP (2012) Dynamics induced by β-lactam antibiotics in the active site of / Bacillus subtilis l,d -transpeptidase. Structure?20:850-61 CrossRef
  7. Mainardi JL, Legrand R, Arthur M, Schoot B, van Heijenoort J, Gutmann L (2000) Novel mechanism of β-lactam resistance due to bypass of D, d -transpeptidation in / Enterococcus faecium. J Biol Chem 275:16490-6496 CrossRef
  8. Mainardi JL, Fourgeaud M, Hugonnet JE, Dubost L, Brouard JP, Ouazzani J, Rice LB, Gutmann L, Arthur M (2005) A novel peptidoglycan cross-linking enzyme for a β-lactam-resistant transpeptidation pathway. J Biol Chem 280:38146-8152 CrossRef
  9. Mainardi JL, Hugonnet JE, Rusconie F, Fourgeaud M, Dubost L, Moumi AN, Delfosse V, Mayer C, Gutmann L, Rice LB, Arthur M (2007) Unexpected inhibition of peptidoglycan l,d -transpeptidase from / Enterococcus faecium by the β-lactam imipenem. J Biol Chem 282:30414-0422 CrossRef
  10. Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32:234-58 CrossRef
  
• 作者单位：Lauriane Lecoq (1) (2) (3)
  Catherine Bougault (1) (2) (3)
  Sébastien Triboulet (4) (5) (6)
  Vincent Dubée (4) (5) (6)
  Jean-Emmanuel Hugonnet (4) (5) (6)
  Michel Arthur (4) (5) (6)
  Jean-Pierre Simorre (1) (2) (3)
  
  1. Institut de Biologie Structurale Jean-Pierre Ebel, CEA, 41 rue Jules Horowitz, 38027, Grenoble, France
  2. Institut de Biologie Structurale Jean-Pierre Ebel, CNRS, 41 rue Jules Horowitz, 38027, Grenoble, France
  3. Institut de Biologie Structurale Jean-Pierre Ebel, Université Joseph Fourier—Grenoble 1, 41 rue Jules Horowitz, 38027, Grenoble, France
  4. Centre de Recherche des Cordeliers, LRMA, Université Pierre et Marie Curie—Paris 6, UMR S 872, Paris, France
  5. Université Paris Descartes, UMR S 872, Paris, France
  6. INSERM, U872, Paris, France
  
• ISSN：1874-270X

文摘

Penicillin-binding proteins were long considered as the only peptidoglycan cross-linking enzymes and one of the main targets of β-lactam antibiotics. A new class of transpeptidases, the l,d-transpeptidases, has emerged in the last decade. In most Gram-negative and Gram-positive bacteria, these enzymes generally have nonessential roles in peptidoglycan synthesis. In some clostridiae and mycobacteria, such as Mycobacterium tuberculosis, they are nevertheless responsible for the major peptidoglycan cross-linking pathway. l,d-Transpeptidases are thus considered as appealing new targets for the development of innovative therapeutic approaches. Carbapenems are currently investigated in this perspective as they are active on extensively drug-resistant M. tuberculosis and represent the only β-lactam class inhibiting l,d-transpeptidases. The molecular basis of the enzyme selectivity for carbapenems nevertheless remains an open question. Here we present the backbone and side-chain 1H, 13C, 15N NMR assignments of the catalytic domain of Enterococcus faecium l,d-transpeptidase before and after acylation with the carbapenem ertapenem, as a prerequisite for further structural and functional studies.