title: UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) inhibitors: a new class of antibacterial agents.
abstract: The rapid increase of health-threatening infections by Gram-negative pathogens along with the emergence of multidrug-resistant 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)-N-acetylglucosamine 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.
authors.affiliation: Department of Medicinal Chemistry, School of Pharmaceutical Sciences, ShanDong University, Ji'nan, China.
authors.forename: J
authors.initials: J
authors.lastname: Zhang
authors.forename: L
authors.initials: L
authors.lastname: Zhang
authors.forename: X
authors.initials: X
authors.lastname: Li
authors.forename: W
authors.initials: W
authors.lastname: Xu
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology*; D055808:Drug Discovery; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D004791:Enzyme Inhibitors; D000581:Amidohydrolases; C097307:UDP-3-O-acyl-N-acetylglucosamine deacetylase