title: Design of on-target FAAH inhibitors.
abstract: In this issue of Chemistry & Biology, Alexander and Cravatt propose a model for the binding of carbamate inhibitors to fatty acid amide hydrolase (FAAH), the enzyme that breaks down signaling lipids. Using competitive activity-based protein profiling and click chemistry, they designed potent and selective FAAH inhibitors and characterized their off-target reactions.
authors.affiliation: Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, New York 11794, USA.
authors.forename: Dale G
authors.initials: DG
authors.lastname: Deutsch
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D002219:Carbamates / Q000737:chemistry / Q000378:metabolism; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D051379:Mice; D013379:Substrate Specificity; D000099252:Fatty Acid Amide Hydrolases
chemical_list: D000581:Amidohydrolases; D002219:Carbamates; D004791:Enzyme Inhibitors; D000099252:Fatty Acid Amide Hydrolases