7-423-08EnzKinetRegStudent

7-423-08EnzKinetRegStudent - Enzymes: Kinetics and...

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Enzymes: Kinetics and inhibition Objectives -Be able to define and explain each of the terms and all the assumptions of the MM equation -Know and be able to use the MM equation -Know how to set up an experiment that will allow you to measure kinetic parameters -Be able to use, draw, interpret enzyme graphs -Be able to describe the alterations that occur in enzyme behavior when inhibitors are present -Be able to distinguish between competitive and mixed inhibition in terms of the affects on Km and Vmax; be able to do this from graphic representations of the kinetic data -Why are most irreversible inhibitors poisons? OUTLINE Intro to Enzymes I. Function A. Biological catalysts B. Functional properties Specificity Catalytic power Regulatable C. Process Bind substrate(s), catalyze a rxn to produce product(s) II. Active sites A. Function of active sites part 1: bind substrate B. Structure Catalytic residues 3-dimensional place Multiple weak interactions Fit C. Function part 2: release product, and enzyme is unchanged III. Energetics A. The difficulty 1
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B. Review of bioenergetics C. Enzymes accelerate reactions by lowering the activation energy because they stabilize the transition state IV. Environmental effects A. Temperature B. pH Enzyme Kinetics I. Why care about kinetics? II. Definitions of terms k1, k-1, k2, k-2 S E P ES Vo Vmax Km III. Michaelis menten kinetics A. Equation B. Assumptions C. Enzyme experiments and [S] vs Vo graphs D. Lineweaver-Burk plots E. Km, again Enzyme Inhibition I.Why care? II. Reversible Inhibition A. Competitive inhibition Mechanism Kinetic effects 2
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B. Mixed inhibition Mechanism Kinetic effects III. Irreversible inhibition REGULATION OF ENZYMES OBJECTIVES Be able to describe and distinguish between the various ways that enzymes are regulated in cells Understand the temporal limits of each type of regulation Review cooperativity Review the concept of allosterism. Understand the metabolic benefit that allosteric enzymes provide to an organism. Know the functional significance of the synthesis of proteins in inactive form. Recognize how phosphorylation/dephosphorylation of an enzyme can produce major changes in an enzyme's three-dimensional structure and its function. OUTLINE I. Alteration of enzyme activity A. Control by interaction with surrounding species 1. Substrate 2. Product --Feedback inhibition 3. Allosteric effector 3
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B. Control by covalent enzyme modification 1. Reversible -phosphorylation, adenylylation 2. Irreversible -Zymogens, proproteins II. Alteration of number of enzyme molecules Transcriptional, translational level, degradation III. Control by location
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7-423-08EnzKinetRegStudent - Enzymes: Kinetics and...

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