Rate equations and simulation curves for enzymatic reactions which utilize lipids as substrates. II. Effect of adsorption of the substrate or enzyme on the steady-state kinetics.
Theoretical aspects of the kinetics of interaction of enzymes with lipid substrates are presented. Rate equations were written and used to simulate v versus S curves for the following cases: (a) The substrate is adsorbed onto non-catalytic sites of the enzyme or to other proteins accompanying the enzyme. (b) The enzyme is adsorbed, via non-catalytic sites to aggregated forms of the substrate. (c) The substrate is adsorbed onto an externally added protein such as albumin. Although all rate equations are based on the Michaelis-Menten kinetic theory, most of the simulated v vs. S curves were not hyperbolic and some of the v vs. E curves not linear.
D000327:Adsorption; D001665:Binding Sites; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008055:Lipids; D008433:Mathematics; D008823:Micelles; D008954:Models, Biological; D008970:Molecular Weight; D011485:Protein Binding
D004798:Enzymes; D008055:Lipids; D008823:Micelles