Pseudomonas aeruginosa MurE amide ligase: enzyme kinetics and peptide inhibitor.

@article{ParadisBleau2009PseudomonasAM,
  title={Pseudomonas aeruginosa MurE amide ligase: enzyme kinetics and peptide inhibitor.},
  author={Catherine Paradis-Bleau and Adrian Lloyd and François Sanschagrin and Halim Maaroufi and Tom A. Clarke and Anne M Blewett and Chris Dowson and David I Roper and T. Bugg and Roger C. L{\'e}vesque},
  journal={The Biochemical journal},
  year={2009},
  volume={421 2},
  pages={263-72}
}
The enzyme kinetics of the amide ligase MurE, a cell wall biosynthesis enzyme, from Pseudomonas aeruginosa were determined using the synthesized nucleotide substrate UDP-MurNAc-Ala-Glu (uridine 5'-diphosphoryl N-acetylmuramoyl-L-alanyl-D-glutamate). When coupled to a competitive bio-panning technique using a M13 phage display library encoding approximately 2.7 x 10(9) random peptide permutations and the specific substrates meso-A2pm (meso-diaminopimelic acid) and ATP, a peptide inhibitor of… CONTINUE READING