TAILIEUCHUNG - Lecture Biochemistry (2/e): Chapter 14 - Reginald Garrett, Charles Grisham

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 Catalytic Power, Specificity, Regulation Introduction to Enzyme Kinetics Kinetics of Enzyme-Catalyzed Reactions Enzyme Inhibition Kinetics of Two-Substrate Reactions 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 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

• Sinh học
• Lecture Biochemistry
• Biological phenomena
• Living systems
• Structure of cells
• Catalytic power
• Enzyme kinetics
• Principles of biochemistry
• Lecture Principles of biochemistry
• Biological systems
• Biochemical compounds
• Biological macromolecules
• Chemical principles
• Properties of water
• Hydrogen bonding
• Amino acids
• Amino acid structure
• Protein purification
• Cell extract
• Protein classification
• Protein 3 Dimensional structure
• Protein folding
• Protein 3 D structure
• 3 D structure
• Oxygen binding curve
• Rate constants
• Classes of enzymes
• Inhibitor kinetics
• Enzyme regulation
• Allosteric regulation
• Enzyme action
• Mechanisms of enzyme action
• Ions Cofactors
• Metal ion
• Nguyên lý hóa sinh
• Biotin cofactor
• Conformation of monosaccharides
• Carbohydrate classifications
• Oligo carbohydrate
• Polysaccharides carbohydrate
• Lipid subclasses
• Acyl lipids
• Fluid mosaic model
• membrane transporters
• Metabolism proceed
• Anaeorbic process
• Triose Phosphate Isomerase
• Regulation of glycolysis
• Control points in glycolysis
• Citric acid cycle
• TCA cycle
• Additional pathways
• Carbohydrate metabolism
• Electron transport
• Chemosmotic theory