title: Structure, inhibition, and regulation of essential lipid A enzymes.
abstract: The Raetz pathway of lipid A biosynthesis plays a vital role in the survival and fitness of Gram-negative bacteria. Research efforts in the past three decades have identified individual enzymes of the pathway and have provided a mechanistic understanding of the action and regulation of these enzymes at the molecular level. This article reviews the discovery, biochemical and structural characterization, and regulation of the essential lipid A enzymes, as well as continued efforts to develop novel antibiotics against Gram-negative pathogens by targeting lipid A biosynthesis. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.
authors.affiliation: Department of Biochemistry, Duke University Medical Center, Research Drive, DUMC 3711, Durham, NC 27710, USA. Electronic address: peizhou@biochem.duke.edu.
authors.forename: Pei
authors.initials: P
authors.lastname: Zhou
authors.affiliation: Department of Biochemistry, Duke University Medical Center, Research Drive, DUMC 3711, Durham, NC 27710, USA.
authors.forename: Jinshi
authors.initials: J
authors.lastname: Zhao
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D024881:Drug Resistance, Bacterial; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000187:drug effects / Q000201:enzymology*; D008050:Lipid A / Q000096:biosynthesis*; D050155:Lipogenesis / Q000187:drug effects; D008958:Models, Molecular; D058990:Molecular Targeted Therapy; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D004798:Enzymes; D008050:Lipid A