Abstract
The rapid increase of health-threatening infections by Gram-negative pathogens along with the emergence of multidrugresistant bacterial strains demands the development of novel antibiotics directed against the previously unexploited targets. One of the promising targets in Gram-negative bacteria is the zinc-dependent metalloamidase, UDP-3-O-(R-3-hydroxymyristoyl)-Nacetylglucosamine deacetylase (LpxC). LpxC catalyzes the first committed, second overall step in the biosynthetic pathway of lipid A. Thus, research on LpxC inhibitors as antibacterial agents has become an attractive field in the development of the novel antibiotic therapy of Gram-negative bacteria. In this review, we will summarize the recent progress in the studies on the structure, catalytic mechanism and regulation of LpxC and the current development of LpxC inhibitors.
Keywords: Gram-negative bacteria, MDR, lipid A, biosynthesis, LpxC, Structure, FtsH, LpxC Inhibitors
Current Medicinal Chemistry
Title:UDP-3-O-(R-3-hydroxymyristoyl)-N-Acetylglucosamine Deacetylase (LpxC) Inhibitors: A New Class of Antibacterial Agents
Volume: 19 Issue: 13
Author(s): J. Zhang, L. Zhang, X. Li and W. Xu
Affiliation:
Keywords: Gram-negative bacteria, MDR, lipid A, biosynthesis, LpxC, Structure, FtsH, LpxC Inhibitors
Abstract: The rapid increase of health-threatening infections by Gram-negative pathogens along with the emergence of multidrugresistant bacterial strains demands the development of novel antibiotics directed against the previously unexploited targets. One of the promising targets in Gram-negative bacteria is the zinc-dependent metalloamidase, UDP-3-O-(R-3-hydroxymyristoyl)-Nacetylglucosamine deacetylase (LpxC). LpxC catalyzes the first committed, second overall step in the biosynthetic pathway of lipid A. Thus, research on LpxC inhibitors as antibacterial agents has become an attractive field in the development of the novel antibiotic therapy of Gram-negative bacteria. In this review, we will summarize the recent progress in the studies on the structure, catalytic mechanism and regulation of LpxC and the current development of LpxC inhibitors.
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Cite this article as:
Zhang J., Zhang L., Li X. and Xu W., UDP-3-O-(R-3-hydroxymyristoyl)-N-Acetylglucosamine Deacetylase (LpxC) Inhibitors: A New Class of Antibacterial Agents, Current Medicinal Chemistry 2012; 19 (13) . https://dx.doi.org/10.2174/092986712800167374
DOI https://dx.doi.org/10.2174/092986712800167374 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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