生物化学原理教学（杨荣武）Chapter9 Enzyme kinetics.pptVIP

Chapter 9 Enzyme Kinetics Outline Definition of enzyme kinetics Factors affecting enzyme-catalyzed reactions Michaelis-Menten Kinetics Enzyme inhibition kinetics Allosteric enzyme kinetics Kinetics concerns with the rates of chemical reaction. Enzyme kinetics addresses the biological roles of enzyme and quantify the remarkable function of enzymes; Enzyme kinetics information can be exploited to control and manipulate the course of metabolic events. Pharmaceuticals or drugs are often special inhibitors targeted at a particular enzyme. The rate of unimolecular reaction is proportional to the concentration of the reactant. Thus rate is linearily dependent on [A]. But if this reaction is catalyzed by an enzyme, the rate shows saturation behavior. Why? You need to know how this is derived This is the complete chemical formula for an enzyme-catalyzed (E) reaction of substrate, S and product, P; Mechaelis-Menten equation describes the relationship between reaction rate and substrate concentration. It can explain the saturation behavior in catalyzed reactions as shown in the previous slide. Mechaelis-Menten equation is derived based on the following three conditions: State steady assumption; Initial velocity assumption; Rate law. In the beginning of the reaction, there is very little product, or [P] is small. So the amount of [ES] contributed by E+P is negligible. Thus, the MM equation concerns the reaction rate that is measured during early reaction period. In which case, the enzyme catalyzed reaction can be modified to: Rate law still applies in enzyme catalyzed reactions. The forward velocity, or rate, vf is, The reverse velocity or rate, or the rate of disappearance vd is, At steady state, there is no accumulation of [ES], thus: We need one more condition, that is, the total enzyme concentration, [Et] is the sum of that of enzyme-substrate complex, [ES], and that of free enzyme, [E]: At steady state, the forward rate should equal to the rev