Chemical shift perturbations induced by the acylation of Enterococcus faecium L,D-transpeptidase catalytic cysteine with ertapenem.

@article{Lecoq2014ChemicalSP,
  title={Chemical shift perturbations induced by the acylation of Enterococcus faecium L,D-transpeptidase catalytic cysteine with ertapenem.},
  author={Lauriane Lecoq and Catherine Bougault and S{\'e}bastien Triboulet and Vincent Dub{\'e}e and Jean-Emmanuel Hugonnet and Michel Arthur and Jean-Pierre Simorre},
  journal={Biomolecular NMR assignments},
  year={2014},
  volume={8 2},
  pages={339-43}
}
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… CONTINUE READING
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