U04_F08 - Unit 4 1 UNIT 4 PART A: ENZYME MECHANISMS PART B:...

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Unit 4 1 U NIT 4 P ART A: E NZYME M ECHANISMS P ART B: P ROTEIN E VOLUTION P ART C: C ONTROL OF E NZYMATIC A CTIVITY NOTE: The unit 4 and 5 tests are combined! Please be sure to prepare both units before you try to tackle the quiz! P ART A: E NZYME M ECHANISMS Assignment: Nelson & Cox, review pp. 188 - 192, pp. 192 - 194, 204 - 213. In Unit 3 we learned that enzymes form an ES complex when appropriate substrates make weak noncovalent interactions with amino acid side chains. This gives the complex its specificity. Once the ES complex has formed, weak noncovalent interactions are optimized to stabilize the transition state and allow the reaction to proceed. In this section we will learn how specific catalytic groups contribute to catalysis using three enzymes (chymotrypsin, hexokinase, and enolase) to illustrate the points.
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2 Objectives: 1. Binding energy contributes to reaction specificity and catalysis. a. Discuss the following forces that are involved in the binding of substrates to enzymes. For each, point out whether the interacting groups must be precisely aligned to get significant binding and whether the distance between interacting groups is critical for binding. 1) electrostatic interactions 2) hydrogen bonds (Fig. 2-5, p. 46) 3) van der Waals forces 4) hydrophobic interactions b. Discuss the importance of binding energy, Δ G B , in enzyme catalyzed reactions (pp. 188 - 192). c. Discuss each of the following in terms of binding energy (p. 192). 1) entropy reduction 2) desolvation 3) induced fit 2. Specific catalytic groups contribute to catalysis (pp. 192 - 194) a. Describe general acid-base catalysis. What is the general purpose of acid/base catalysis (pp. 192 - 193)? Use Fig. 6-9 (p. 193) to identify the amino acid side chains that can function as acid-base catalysts. b. Describe covalent catalysis. What is the purpose of covalent catalysis (p. 193)? c.
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U04_F08 - Unit 4 1 UNIT 4 PART A: ENZYME MECHANISMS PART B:...

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