Exploring the UDP pocket of LpxC through amino acid analogs
…, A Kutschke, M Johnstone, B Prince, J Thresher…
Index: Hale, Michael R.; Hill, Pamela; Lahiri, Sushmita; Miller, Matthew D.; Ross, Philip; Alm, Richard; Gao, Ning; Kutschke, Amy; Johnstone, Michele; Prince, Bryan; Thresher, Jason; Yang, Wei Bioorganic and Medicinal Chemistry Letters, 2013 , vol. 23, # 8 p. 2362 - 2367
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Citation Number: 7
Abstract
Lipopolysaccharide (LPS) biosynthesis is an attractive antibacterial target as it is both conserved and essential for the survival of key pathogenic bacteria. Lipid A is the hydrophobic anchor for LPS and a key structural component of the outer membrane of Gram- negative bacteria. Lipid A biosynthesis is performed in part by a unique zinc dependent metalloamidase, LpxC (UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine ...
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Exploring the UDP pocket of LpxC through amino acid analogs
[Bioorganic and Medicinal Chemistry Letters, , vol. 23, # 8 p. 2362 - 2367]