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Molecular Validation Of Lpxc As An Antibacterial Drug Target In Pseudomonas Aeruginosa, Adam Barb, Khisimuzi E. Mdluli, Pamela R. Witte, Toni Kline, Alice L. Erwin, Bryce E. Mansfield, Amanda L. Mcclerren, Michael C. Pirrung, L. Nathan Tumey, Paul Warrener, Christian R. H. Raetz, C. Kenall Stover
Molecular Validation Of Lpxc As An Antibacterial Drug Target In Pseudomonas Aeruginosa, Adam Barb, Khisimuzi E. Mdluli, Pamela R. Witte, Toni Kline, Alice L. Erwin, Bryce E. Mansfield, Amanda L. Mcclerren, Michael C. Pirrung, L. Nathan Tumey, Paul Warrener, Christian R. H. Raetz, C. Kenall Stover
Adam Barb
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. These molecules did not inhibit the growth of Pseudomonas aeruginosa and were therefore not developed further as antibacterial drugs. The inactivity of the LpxC …