Download Chemistry 4202: Enzyme Kinetics and Mechanisms - Chapter 6 Objectives and more Study notes Biochemistry in PDF only on Docsity! Dr. Susan F. Hornbuckle Clayton State University CHEM 4202 Chapter 6 Objectives 1. Be able to define: enzyme, cofactor, coenzyme, prosthetic group, apoenzyme, holoenzyme, active site, substrate. 2. Be able to classify the enzyme that catalyzes a given reaction as: oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase. 3. Be able to explain the difference between thermodynamics and kinetics. 4. Be able to explain how an enzyme catalyzes a reaction in terms of kinetics and thermodynamics. Does the enzyme affect the equilibrium and/or rate of the reaction? 5. Be able to draw a graph of “Reaction Process” versus “Free Energy” in order to support your answers to number four. 6. Be able to explain how enzymes use “binding energy” to lower the activation energy of a reaction. 7. Be able to explain the “Lock and Key Theory” and the “Induced Fit Mechanism” using words and diagrams. 8. Other than binding energy, explain three other ways in which and enzyme may function. 9. Be able to describe and recognize “General Acid-Base catalysis”, “Specific Acid- Base Catalysis”, “Covalent Catalysis” and “Metal Ion Catalysis”. 10. Be able to write and use the Michaelis-Menten equation. 11. Know what is meant by pre-steady state kinetics and steady-state kinetics. Which is used in determining V0? 12. Be able to locate and determine the values of Vmax and Km on a Michaelis-Menten graph. 13. Know the significance of the Michaelis-Menten constant. 14. Be able to solve for Km when V0 is equal to 1/2 Vmax using the Michaelis-Menten equation. 15. Be able to derive the Lineweaver-Burke equation (Double Reciprocal Equation) from the Michaelis-Menten equation. 16. Be able to locate and determine the values of Vmax and Km on a Lineweaver-Burke graph. 17. Be able to draw a Lineweaver-Burke plot given [S] and V0 data. 18. Be able to describe the significance of kcat, turnover number. 19. Given Km and kcat, be able to determine the catalytic efficiency of an enzyme and compare to the catalytic efficiency of other given enzymes. 20. Be able to describe the relationship between the enzyme’s affinity for the substrate and Km. What effect does this have on the enzymes catalytic efficiency? Why? 21. Be able to describe the three possible reaction pathways that might occur when an enzyme catalyzes a reaction involving two substrates. Write and name each pathway. How are these pathways studied? 22. Be able to identify (from reaction information or a Lineweaver Burke plot), describe, and write a reaction pathway for a competitive inhibitor, uncompetitive inhibitor, a mixed inhibitor, and a noncompetitive inhibitor. 23. Be able to define: reversible inhibitor, irreversible inhibitor, suicide inhibitors (inactivators), and mechanism-based inhibitors (inactivators).
