Kinetics of coupled enzyme reactions.
A theory has been developed for the kinetics of coupled enzyme reactions. This theory does not assume that the first reaction is irreversible. The validity of this theory is confirmed by a model system consisting of enoyl-CoA hydratase (EC 4.2.1.17) and 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) with 2,4-decadienoyl coenzyme A (CoA) as a substrate. This theory, in contrast to the conventional theory, proves to be indispensible for dealing with coupled enzyme systems where the equilibrium constant of the first reaction is small and/or the concentration of the coupling enzyme is higher than that of the intermediate. Equations derived on the basis of this theory can be used to calculate steady-state velocities of coupled enzyme reactions and to predict the time course of coupled enzyme reactions during the pre steady state.
Yang
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SY
Department of Chemistry, City College of the City University of New York, New York 10031.
Schulz
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D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism*; D000214:Acyl Coenzyme A / Q000378:metabolism; D000818:Animals; D002417:Cattle; D004746:Enoyl-CoA Hydratase / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D006836:Hydro-Lyases / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008433:Mathematics; D008962:Models, Theoretical; D009206:Myocardium / Q000201:enzymology; D013552:Swine
D000214:Acyl Coenzyme A; D004798:Enzymes; C040351:2,4-decadienoyl-coenzyme A; D015094:3-Hydroxyacyl CoA Dehydrogenases; D006836:Hydro-Lyases; D004746:Enoyl-CoA Hydratase