lineweaver-burk作图法将米氏方程改写成enzymeinhibition.pptVIP

How do enzymes work? Free energy tells us nothing about the rate at which the reaction occurs Understanding Km Km is a constant derived from rate constants Km is, under true Michaelis-Menten conditions, an estimate of the dissociation constant of E from S, because at equilibrium, Reversible reaction, dissociation constant is So small Km means tight substrate binding; high Km means weak substrate binding. Km equals to the substrate concentration at which v=1/2vmax Understanding Vmax The theoretical maximal velocity Vmax is a constant Vmax is the theoretical maximal rate of the reaction - but it is NEVER achieved in reality To reach Vmax would require that ALL enzyme molecules are tightly bound with substrate Vmax is asymptotically approached as substrate is increased 双倒数作图法（Lineweaver-Burk作图法）  Enzyme Inhibition Enzyme can be inhibited by inhibitors. Inhibitors are tools to scientists to understand enzymes. Inhibitors are also in many cases pharmaceutical reagents against diseases; Inhibitors inhibit enzyme function by binding with enzymes. The binding reaction can be either reversible or irreversible; Reversible inhibitors associate with enzymes through non-covalent interactions. Reversible inhibitors include three kinds: Competitive inhibitors; Non-competitive inhibitors; Un-competitive inhibitors Irreversible inhibitors associate with enzymes through covalent interactions. Thus the consequences of irreversible inhibitors is to decrease in the concentration of active enzymes. 可逆抑制作用(reversible inhibition)及其动力学 （1）竞争性抑制作用（competitive inhibition） 竞争性抑制作用动力学方程的讨论 A、与标准米氏方程比较 C、取方程的倒数，进行双倒数作图 Competitve Inhibitors Often “resemble” substrates or cofactors Bind to enzyme through similar complementary interactions Example: Dihydrofolate reductase Competitive Inhibitors Summary of Classes of Inhibitors Competitive inhibition - inhibitor (I) binds only to E, not to ES Noncompetitive inhibition - inhibitor (I) binds either to E and/or to