Kinetics of irreversible enzyme inhibition by an unstable inhibitor.
A mathematical treatment for the general case of enzyme inactivation by an inhibitor that breaks down in solution in a first-order reaction is presented. Cathepsin D was inactivated by fluorescein isothiocyanate with a K(i) of 4.47mum. Kinetic constants were also determined for the inactivation of cathepsin D by 1,1-bis(diazoacetyl)-2-phenylethane, and the inactivation of pepsin C by diazoacetyl-dl-norleucine methyl ester.
D002403:Cathepsins / Q000037:antagonists & inhibitors; D004791:Enzyme Inhibitors; D005452:Fluoresceins; D007700:Kinetics; D008433:Mathematics; D009646:Norleucine / Q000031:analogs & derivatives; D010434:Pepsin A / Q000037:antagonists & inhibitors; D013861:Thiocyanates
D004791:Enzyme Inhibitors; D005452:Fluoresceins; D013861:Thiocyanates; D009646:Norleucine; D002403:Cathepsins; D010434:Pepsin A