This preview shows pages 1–4. Sign up to view the full content.
This preview has intentionally blurred sections. Sign up to view the full version.
View Full DocumentThis preview has intentionally blurred sections. Sign up to view the full version.
View Full Document
Unformatted text preview: Lecture 6: Lecture 6: Enzyme Catalysis Enzyme Catalysis BIOCHEMISTRY 100 Winter 2009 M. Ziegler Learning Objectives Learning Objectives 1. Terminology (explain/defne; understand use oF terms): catalyst, Free energy diagram, activation energy, transition state, rate enhancement, Free energy change, enzyme assay, hyperbola, allosteric (enzyme), steady state, Michaelis constant, turnover number, reversible inhibitor, irreversible inhibitor, competitive inhibitor, pure noncompetitive inhibitor 2. What parameter on the Free energy profle oF a reaction is altered by a catalyst such as an enzyme? 3. Calculate the rate enhancement due to the enzyme For a reaction whose uncatalyzed rate is 250 M•sec –1 and enzyme catalyzed rate is 5 x 10 15 M•sec –1 . 4. Write a rate equation to express the Forward velocity oF a reaction such as A + B C , with a Forward rate constant oF k 1 . What is the order oF the reaction with respect to A? With respect to B? What is the overall order oF the Forward reaction? 5. Explain in terms oF a Free energy diagram why it is important that the enzyme bind the transition state tightly, and not bind the subsrate too tightly. Learning Objectives, continued Learning Objectives, continued 6. What general types of reactions are catalyzed by chymotrypsin? 7. What is the shape of a plot of V vs. [S] for a chymotrypsin catalyzed reaction? 8. What is the shape of a plot of V vs. [S] for an allosterically regulated enzyme like ATCase? 9. Write the kinetic mechanism for an enzyme that follows a simple MichaelisMenten model. 10. Write the equation describing the “steady state” condition for an enzymecatalyzed reaction, i.e., the equation relating rate of formation of the ES complex to rate of breakdown of the ES complex. 11. Write the MichaelisMenten equation in its hyperbolic form. 12. Explain the parts of the hyperbolic plot of V vs. [S] for an enzyme  how does V relate to [S] when [S] = K M ? When [S] << K M ? When S >> K M ? 13. Learning Objectives, continued Learning Objectives, continued 6. What general types of reactions are catalyzed by chymotrypsin? 7. What is the shape of a plot of V vs. [S] for a chymotrypsin catalyzed reaction? 8. What is the shape of a plot of V vs. [S] for an allosterically regulated enzyme like ATCase? 9. Write the kinetic mechanism for an enzyme that follows a simple MichaelisMenten model. 10. Write the equation describing the “steady state” condition for an enzymecatalyzed reaction, i.e., the equation relating rate of formation of the ES complex to rate of breakdown of the ES complex. 11. Write the MichaelisMenten equation in its hyperbolic form. 12. Explain the parts of the hyperbolic plot of V vs. [S] for an enzyme  how does V relate to [S] when [S] = K M ?...
View
Full
Document
This note was uploaded on 02/25/2009 for the course BCH 100 taught by Professor Staff during the Spring '08 term at UC Riverside.
 Spring '08
 Staff
 Biochemistry

Click to edit the document details