Molecular validation of LpxC as an antibacterial drug target in Pseudomonas aeruginosa.

@article{Mdluli2006MolecularVO,
  title={Molecular validation of LpxC as an antibacterial drug target in Pseudomonas aeruginosa.},
  author={Khisimuzi E Mdluli and Pamela R Witte and Toni Kline and Adam W Barb and Alice L Erwin and Bryce E. Mansfield and Amanda L. McClerren and Michael C. Pirrung and L. Nathan Tumey and Paul Warrener and Christian R. H. Raetz and C Kendall Stover},
  journal={Antimicrobial agents and chemotherapy},
  year={2006},
  volume={50 6},
  pages={2178-84}
}
LpxC [UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase] is a metalloamidase that catalyzes the first committed step in the biosynthesis of the lipid A component of lipopolysaccharide. A previous study (H. R. Onishi, B. A. Pelak, L. S. Gerckens, L. L. Silver, F. M. Kahan, M. H. Chen, A. A. Patchett, S. M. Galloway, S. A. Hyland, M. S. Anderson, and C. R. H. Raetz, Science 274:980-982, 1996) identified a series of synthetic LpxC-inhibitory molecules that were bactericidal for Escherichia coli… CONTINUE READING

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