Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase.

@article{Kotnik2007StructuralAF,
  title={Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase.},
  author={Miha Kotnik and Jan Humljan and Carlos Contreras-Martel and Marko Oblak and Katja Kristan and Mireille Herv{\'e} and Didier Blanot and Uro{\vs} Urleb and Stanislav Gobec and Andr{\'e}a Dessen and Tom {\vS}olmajer},
  journal={Journal of molecular biology},
  year={2007},
  volume={370 1},
  pages={107-15}
}
Mur ligases play an essential role in the intracellular biosynthesis of bacterial peptidoglycan, the main component of the bacterial cell wall, and represent attractive targets for the design of novel antibacterials. UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) catalyses the addition of D-glutamic acid to the cytoplasmic intermediate UDP-N-acetylmuramoyl-L-alanine (UMA) and is the second in the series of Mur ligases. MurD ligase is highly stereospecific for its substrate, D-glutamic… CONTINUE READING