MBB 222 Lecture Notes - Lecture 13: Enzyme, Activation Energy

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browncricket987

20 Dec 2018

School

Simon Fraser University

Department

Molec Biol & Biochem

Course

MBB 222

Professor

Adam Barlev

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Enzymes enhance rates of reaction by lowering g , the activation energy for the transition state . For the conversion of sucrose (table sugar) and oxygen (s) to co2 and water (p), the reaction has a very high negative g, so is thermodynamically favorable (exergonic). At equilibrium the sucrose concentration is very low (keq>>1). Yet, sucrose is very stable in the presence of oxygen. This reaction proceeds at an infinitesimally slow rate because there is a very high energy barrier the activation energy, g . Enzymes in our body can accelerate this reaction by lowering g . The free energy released ( g) is used to do work in the cell (drive other reactions, transport, etc. ) Models to explain the exquisite specificity of enzyme active sites for their substrates. Lock-and-key model: the substrate forms a perfect fit with the enzyme active site.

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33-To stabilize the transition state complex, which of the following must be lowered? A) Initial energy state B) Activation energy C) Net energy change D) The Vmax B) Final energy state 34- Which of the following statements about allosteric enzymes is CORRECT? A The binding of substrate to any active site affects the other active sites B The plot of initial velocity vs. substrate concentration is a straight line C The Keq of the reaction is increased when allosteric activator is bound D The enzymes contains only one polypeptide chain E Allosteric activators bind to all active sites equally 35. Which statement about the two different models proposed to explain enzyme specificity is CORRECT. a. The substrate changes shape when enzyme binds in the Lock and Key Model. b. The enzyme undergoes a covalent modification when bound to substrate in the Lock and Key Model. c. The active site of the enzyme alternates in conformation between opened and closed in the Induced Fit Model. d. The enzyme changes conformation after binding the substrate in the Induced Fit Model. eÂ·The product structure is altered after it has bound to the enzyme in the Induced Fit Model. 36. An enzymatic reaction proceeds with maximal velocity (Vmax) when A. the substrate concentration is equal to that of a competitive inhibitor. B. allosteric effectors are present. C. the enzyme substrate complex is maximal. D. the substrate concentration exceeds that of a noncompetitive inhibitor. E. all of the substrate is bound to the enzyme. 37. Which of the statements below are incorrect? A With all other factors that modify the rate of the enzyme catalyzed reaction remaining constant as we raise the temperature of an enzyme catalyzed reaction there is an initial increase of velocity with temperature. B. The rate of reaction increases with temperature because there is an increasing number of molecules with sufficient energy to pass over the energy barrier which we call the energy of activation C. Reaction rate increases with temperature until a maximum is reached, when the rate of the reaction will suddenly suddenly fall to zero because the enzyme will be denatured and therefore inactive. D. The reaction rate initially increases as temperature rises owing to increased kinetic energy of the reacting molecules E. Enzymes in crease reaction rates due to their ability to lower the energy barriers for reactions F. None of the above 38- Which of the following is true for the induced fit theory of enzyme action? A. The conformation of the substrate changes before binding to the enzyme. B. The active site changes shape during binding of the substrate C. The substrate fits into a preformed active site through a lock-and-key mechanism. D. Enzymes alternate between conformations where the active site is either open or closed. E. The substrate causes a cleft to form in the enzyme where it subsequently binds

1. C6H12O6 + 6O2 Ã 6CO2 + 6H2O Glucose is being _____ to _____ and oxygen is being _____ to _____. a. oxidized; carbon dioxide; reduced; water b. oxidized; water; reduced; carbon dioxide Incorrect c. reduced; water; oxidized; carbon dioxide d. reduced; carbon dioxide; oxidized; water

2. Which of the following stages in the breakdown of the piece of toast you had for breakfast generates the most ATP? a. the citric acid cycle Incorrect b. glycolysis c. the digestion of starch to glucose d. oxidative phosphorylation

3. Which of the following is a catabolic pathway? a. gluconeogenesis b. production of starch Incorrect c. glycolysis d. production of glycogen

4. Per molecule, the oxidation of a fatty acid results in _____ energy storage than the oxidation of glucose. a. the same b. less Incorrect c. more d. None of the above; fatty acids cannot be oxidized.

5. Of the eight reactions in the citric acid cycle, how many are oxidation-reduction reactions? a. one b. two c. three d. four e. five

6. The process of glycolysis transfers the energy in sugar molecules into the stored energy of activated carriers such as ATP and NADH. Which statement is true about glycolysis? a. Only eukaryotic organisms do glycolysis. b. The ten reactions of glycolysis are identical in all eukaryotic cells, but are different in prokaryotic cells due to their diverse metabolic strategies. Incorrect c. The ten reactions of glycolysis are identical in almost all living organisms on the planet. d. There are many ways to oxidize glucose and transfer energy into activated carriers; the diversity of organisms on the planet is reflected in the diversity of their mechanisms of glycolysis.

7. Referring to the sentence completed in #13 above, the purpose of the latter reaction (in active muscle cells) is to _____. a. accumulate lactic acid in the cell, which provides additional energy for the production of ATP Incorrect b. slow down glycolysis until oxygen becomes available again c. accelerate the Krebs cycle, which will restore the oxygen supply d. regenerate NAD+ so that glycolysis can continue in the absence of oxygen

8. What are the products of the citric acid cycle? a. carbon dioxide, NADH, FADH2 and GTP b. carbon dioxide, NAD+, FAD and GTP c. NADH, FADH2, and acetyl CoA Incorrect d. carbon dioxide and water

9. Which statement is true about enzymes? a. Enzymes catalyze chemical reactions because they make inherently endergonic reactions exergonic. b. Each enzyme in a cell can catalyze many different chemical reactions involving chemically different substrates. Incorrect c. Enzymes can only catalyze reactions in one direction. d. After catalyzing a reaction, an enzyme is permanently altered and can no longer bind substrate. e. None of the above is true. 1

10. âG measures the change in free energy in a system as it converts reactant (Y) into product (X). When [X] = [Y], âG is equal to _____. a. RT b. ÎGÂ° + RT c. ÎGÂ° d. ln [X]/[Y]

11. The âGÂ° for the hydrolysis of ATP is -7.3 kcal/mol. What conditions in the cell would lead to a âG for ATP hydrolysis of -11 kcal/mol? a. An increase in the ATP/ADP ratio b. An increase in anabolic activity in the cell c. Transport of ATP out of the compartment where the reaction is occurring Incorrect d. A decrease in the ATP/ADP ratio

12. In the first reaction of glycolysis, a phosphate transferred from ATP to a glucose molecule to produce glucose-6-phosphate and ADP. Under conditions existing in the cell, the free energy change for this reaction is -8.0 kcal/mole. Which of the following statements is true? Recall that the âGÂ° for the hydrolysis of ATP is -7.3 kcal/mol. a. Glucose concentrations in the cell are always low, making this reaction more favorable than would be expected. b. This reaction is less favorable than would be expected, given the âGÂ° of ATP hydrolysis. c. Glucose-6-P concentrations in the cell are very low relative to glucose concentrations, making the reaction more favorable than would be expected. d. The âGÂ° for the addition of a phosphate to glucose must be -0.7 kcal/mole.

13. Protein E can bind to two different proteins, S and I. The binding reactions are described by the following equations and values: E + S --> ES Keq for ES = 10 E + I> EI Keq for EI = 2 Given the equilibrium constant values, which one of the following statements is true? a. When S is present in excess, no I molecules will bind to E. b. E binds I more tightly than S. c. The binding energy of the ES interaction is greater than that of the EI interaction. d. Changing an amino acid on the binding surface of I from a basic amino acid to an acidic one will probably make the free energy of association with E more negative.

MBB 222 Lecture Notes - Lecture 13: Enzyme, Activation Energy

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