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In this chapter, you will learn to: Catalytic power, specificity, regulation; introduction to enzyme kinetics; kinetics of enzyme-catalyzed reactions; enzyme inhibition; kinetics of two-substrate reactions; ribozymes and abzymes. | Chapter 14 Enzyme Kinetics to accompany Biochemistry, 2/e by Reginald Garrett and Charles Grisham All rights reserved. Requests for permission to make copies of any part of the work should be mailed to: Permissions Department, Harcourt Brace & Company, 6277 Sea Harbor Drive, Orlando, Florida 32887-6777 Outline 14.1 Catalytic Power, Specificity, Regulation 14.2 Introduction to Enzyme Kinetics 14.3 Kinetics of Enzyme-Catalyzed Reactions 14.4 Enzyme Inhibition 14.5 Kinetics of Two-Substrate Reactions 14.6 Ribozymes and Abzymes Enzymes Enzymes endow cells with the remarkable capacity to exert kinetic control over thermodynamic potentiality Enzymes are the agents of metabolic function Catalytic Power Enzymes can accelerate reactions as much as 1016 over uncatalyzed rates! Urease is a good example: Catalyzed rate: 3x104/sec Uncatalyzed rate: 3x10 -10/sec Ratio is 1x1014 ! Specificity Enzymes selectively recognize proper substrates over other molecules Enzymes produce products in very high yields - often much greater than 95% Specificity is controlled by structure - the unique fit of substrate with enzyme controls the selectivity for substrate and the product yield Other Aspects of Enzymes Regulation - to be covered in Chapter 15 Mechanisms - to be covered in Chapter 16 Coenzymes - to be covered in Chapter 18 14.2 Enzyme Kinetics Several terms to know! rate or velocity rate constant rate law order of a reaction molecularity of a reaction The Transition State Understand the difference between G and G‡ The overall free energy change for a reaction is related to the equilibrium constant The free energy of activation for a reaction is related to the rate constant It is extremely important to appreciate this distinction! What Enzymes Do Enzymes accelerate reactions by lowering the free energy of activation Enzymes do this by binding the transition state of the reaction better than the substrate Much more of this in Chapter 16! The Michaelis-Menten Equation You should be | Chapter 14 Enzyme Kinetics to accompany Biochemistry, 2/e by Reginald Garrett and Charles Grisham All rights reserved. Requests for permission to make copies of any part of the work should be mailed to: Permissions Department, Harcourt Brace & Company, 6277 Sea Harbor Drive, Orlando, Florida 32887-6777 Outline 14.1 Catalytic Power, Specificity, Regulation 14.2 Introduction to Enzyme Kinetics 14.3 Kinetics of Enzyme-Catalyzed Reactions 14.4 Enzyme Inhibition 14.5 Kinetics of Two-Substrate Reactions 14.6 Ribozymes and Abzymes Enzymes Enzymes endow cells with the remarkable capacity to exert kinetic control over thermodynamic potentiality Enzymes are the agents of metabolic function Catalytic Power Enzymes can accelerate reactions as much as 1016 over uncatalyzed rates! Urease is a good example: Catalyzed rate: 3x104/sec Uncatalyzed rate: 3x10 -10/sec Ratio is 1x1014 ! Specificity Enzymes selectively recognize proper substrates over other molecules Enzymes produce products in very high .
