4-1-Biochemistry-生物化学.pptVIP

Enzymes: Basic Concepts and Kinetics Enzymes Are Powerful and Highly Specific Catalysts The specificity of an enzyme is due to the precise interaction of the substrate with the enzyme. This precision is a result of the intricate three-dimensional structure of the enzyme protein. Many Enzymes Require Cofactors for Activity Enzymes May Transform Energy from One Form into Another Enzymes Are Classified on the Basis of the Types of Reactions That They Catalyze Free Energy Is a Useful Thermodynamic Function for Understanding Enzymes The Free-Energy Change Provides Information About the Spontaneity but Not the Rate of a Reaction The rate of a reaction depends on the free energy of activation (ΔG?) The Standard Free-Energy Change of a Reaction Is Related to the Equilibrium Constant Enzymes Accelerate Reactions by Facilitating the Formation of the Transition State The Formation of an Enzyme-Substrate Complex Is the First Step in Enzymatic Catalysis The Active Sites of Enzymes Have Some Common Features The Michaelis-Menten Model Accounts for the Kinetic Properties of Many Enzymes The Significance of KM and Vmax Values Kinetic Perfection in Enzymatic Catalysis: The kcat/KM Criterion Most Biochemical Reactions Include Multiple Substrates Allosteric Enzymes Do Not Obey Michaelis-Menten Kinetics Enzymes Can Be Inhibited by Specific Molecules Competitive and Noncompetitive Inhibition Are Kinetically Distinguishable Irreversible Inhibitors Can Be Used to Map the Active Site Transition-State Analogs Are Potent Inhibitors of Enzymes Catalytic Antibodies Demonstrate the Importance of Selective Binding of the Transition State to Enzymatic Activity Penicillin Irreversibly Inactivates a Key Enzyme in Bacterial Cell-Wall Synthesis Distinction between a Competitive and a Noncompetitive Inhibitor. (Top) enzyme-substrate complex; (middle) a competitive inhibitor binds at the active site and thus prevents the substrate from binding; (bottom) a noncompetitive inhibitor does not prevent the