title: Toward cocaine esterase therapeutics.
abstract: Cocaine is among the most reinforcing of all drugs of abuse, yet no effective pharmacotherapy is available. Herein, we report the development and characterization of phage-displayed cocaine esterases with pharmacologically relevant kinetic parameters (kcat/Km approximately 104 M-1 s-1).
authors: The Skaggs Institute for Chemical Biology and Departments of Chemistry and Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
authors: Claude J
authors: CJ
authors: Rogers
authors: Jenny M
authors: JM
authors: Mee
authors: Gunnar F
authors: GF
authors: Kaufmann
authors: Tobin J
authors: TJ
authors: Dickerson
authors: Kim D
authors: KD
authors: Janda
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D001435:Bacteriophages / Q000737:chemistry* / Q000201:enzymology* / Q000235:genetics; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D003042:Cocaine / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D006868:Hydrolysis; D007700:Kinetics
chemical_list: D001426:Bacterial Proteins; D002265:Carboxylic Ester Hydrolases; C019921:cocaine esterase; D003042:Cocaine