Kinetic effects due to nonspecific substrate-inhibitor interactions in enzymatic reactions.
Nonspecific protein binding is a commonly encountered problem with synthetic molecules designed as enzyme inhibitors. When the substrate for the enzymatic reaction is itself a protein, such nonspecific protein binding can also occur. Here, we demonstrate that this phenomenon can have a dramatic effect on the steady-state kinetic evaluation of such inhibitors.
Department of Chemical Enzymology, The DuPont Merck Research Laboratories, Wilmington, DE 19880-0400, USA. Copelara@lldmpc.dnet.dupont.com
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Copeland
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Horiuchi
D002384:Catalysis; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D011485:Protein Binding
D004791:Enzyme Inhibitors; D004798:Enzymes