title: Enzyme inhibition in open systems. Superiority of uncompetitive agents.
abstract: Investigations of the open system behavior of reversible dead-end inhibitors were carried out by means of computer simulations and experimental studies. The results from both approaches indicate that substrate-competitive inhibition may often be an inappropriate basis for design of potential therapeutic agents. The use of uncompetitive (also called anticompetitive) inhibitors in this role is likely to be far more effective. Chemical analogs of pathogen-specific enzymic reaction products rather than analogs of substrates provide a promising basis for the systematic design of such uncompetitive inhibitors.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.
authors.forename: A M
authors.initials: AM
authors.lastname: Westley
authors.forename: J
authors.initials: J
authors.lastname: Westley
mesh_terms: D001667:Binding, Competitive; D003198:Computer Simulation; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008962:Models, Theoretical; D013329:Structure-Activity Relationship
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes