I would appreciate the typed answer to all of the questions. Ch8 - Enzyme Mechan
ID: 198392 • Letter: I
Question
I would appreciate the typed answer to all of the questions.
Ch8 - Enzyme Mechanisms and Inhibitors 1. Define an allosteric enzyme/ protein 2. How do the following reversible inhibitors alter Michaelis Menten kinetics: competitive inhibitor, noncompetitive inhibitor, & uncompetitive inhibitor? Be familiar with the Lineweaver-Burk plot of each inhibitor. How are irreversible inhibitors different from reversible ones? What are the 4 types of irreversible inhibitors? List and define the 4 different strategies (catalytic mechanisms) enzymes use to catalyze reactions. What mechanism of action does chymotrypsin use? Sketch the catalytic triad of chymotrypsin. What role do the AA's in the catalytic triad play in the catalytic 3. 4. 5. 6. activity of chymotrypsin? 7. The reaction catalyzed by chymotrypsin takes place in 2 stages; be familiar with what this description means. 8. What are the roles of the S1 pocket and oxyanion hole? Ch9 Hemoglobin, An Allosteric Protein 1. Compare and contrast O2 binding by hemoglobin & myoglobin. Which protein is allosteric? 2. What factors affect the ability of hemoglobin to bind O2? Myoglobin to 02? 3. Define cooperativity. 4. Understand the mechanism of cooperativity of O2 binding by Hb and the structural changes Hb undergoes when it binds O2 (T & R forms).Explanation / Answer
Answer.
1. An allosteric enzyme is an enzyme that contains a region to which small, regulatory molecules ("effects") may bind in addition to and separate from the substrate binding site and therby affect the catalytic activity.