A steady state mathematical model for stepwise "slow-binding" reversible enzyme inhibition.
The standard mathematical model for stepwise "slow-binding" enzyme inhibition (E+Iright harpoon over left harpoonEIright harpoon over left harpoonEI( *)) assumes that the initial enzyme-inhibitor complex EI is always at equilibrium with the free component species E and I. This assumption implies that the dissociation rate constant (EI-->E+I) is infinitely higher than the isomerization rate constant for EI-->EI( *). This paper presents a more general mathematical treatment, under the steady state approximation rather than the usual rapid-equilibrium approximation, whereby the two rate constants for the disappearance of EI are allowed to be comparable in magnitude. Experimentally relevant illustrative examples include discrimination between a single-step and a two-step mechanism for slow-binding inhibition kinetics.
Kuzmic
Petr
P
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D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D016018:Least-Squares Analysis; D016014:Linear Models; D008956:Models, Chemical; D011485:Protein Binding; D013997:Time Factors
D004791:Enzyme Inhibitors