Enzymes are potent catalysts because they: A) are consumed in the reactions they catalyze. B) are...
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Enzymes are potent catalysts because they: A) are consumed in the reactions they catalyze. B) are very specific and can prevent the conversion of products back to substrates. C) drive reactions to completion while other catalysts drive reactions to equilibrium. D) increase the equilibrium constants for the reactions they catalyze. E) lower the activation energy for the reactions they catalyze. 2. How enzymes work Which one of the following statements is true of enzyme catalysts? A) Their catalytic activity is independent of pH. B) They are generally equally active on D and L isomers of a given substrate. C) They can increase the equilibrium constant for a given reaction by a thousand fold or more. D) They can increase the reaction rate for a given reaction by a thousand-fold or more. E) To be effective, they must be present at the same concentration as their substrate. 3. How enzymes work Which of the following statements is false? A) A reaction may not occur at a detectable rate even though it has a favorable equilibrium. B) After a reaction, the enzyme involved becomes available to catalyze the reaction again. C) For S→P, a catalyst shifts the reaction equilibrium to the right. D) Lowering the temperature of a reaction will lower the reaction rate. E) Substrate binds to an enzyme's active site. 4. How enzymes work Which of the following is true of the binding energy derived from enzyme-substrate interactions? A) It cannot provide enough energy to explain the large rate accelerations brought about by enzymes. B) It is sometimes used to hold two substrates in the optimal orientation for reaction. C) It is the result of covalent bonds formed between enzyme and substrate. D) Most of it is derived from covalent bonds between enzyme and substrate. E) Most of it is used up simply binding the substrate to the enzyme. 5. Enzyme kinetics as an approach to understanding mechanism The concept of "induced fit" refers to the fact that: A) enzyme specificity is induced by enzyme-substrate binding. B) enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. C) enzyme-substrate binding induces movement along the reaction coordinate to the transition state. D) substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. E) when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate. Enzymes are potent catalysts because they: A) are consumed in the reactions they catalyze. B) are very specific and can prevent the conversion of products back to substrates. C) drive reactions to completion while other catalysts drive reactions to equilibrium. D) increase the equilibrium constants for the reactions they catalyze. E) lower the activation energy for the reactions they catalyze. 2. How enzymes work Which one of the following statements is true of enzyme catalysts? A) Their catalytic activity is independent of pH. B) They are generally equally active on D and L isomers of a given substrate. C) They can increase the equilibrium constant for a given reaction by a thousand fold or more. D) They can increase the reaction rate for a given reaction by a thousand-fold or more. E) To be effective, they must be present at the same concentration as their substrate. 3. How enzymes work Which of the following statements is false? A) A reaction may not occur at a detectable rate even though it has a favorable equilibrium. B) After a reaction, the enzyme involved becomes available to catalyze the reaction again. C) For S→P, a catalyst shifts the reaction equilibrium to the right. D) Lowering the temperature of a reaction will lower the reaction rate. E) Substrate binds to an enzyme's active site. 4. How enzymes work Which of the following is true of the binding energy derived from enzyme-substrate interactions? A) It cannot provide enough energy to explain the large rate accelerations brought about by enzymes. B) It is sometimes used to hold two substrates in the optimal orientation for reaction. C) It is the result of covalent bonds formed between enzyme and substrate. D) Most of it is derived from covalent bonds between enzyme and substrate. E) Most of it is used up simply binding the substrate to the enzyme. 5. Enzyme kinetics as an approach to understanding mechanism The concept of "induced fit" refers to the fact that: A) enzyme specificity is induced by enzyme-substrate binding. B) enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. C) enzyme-substrate binding induces movement along the reaction coordinate to the transition state. D) substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. E) when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.
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