What would be the expected effect of this change on the enzyme’s catalytic activity?
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- Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pHWhich of the following analogies best describes the induced-fit model of enzyme-substrate binding? a. a hug between two people b. a key fitting into a lock c. a square peg fitting through the square hole and a round peg fitting through the round hole of a children’s toy d. the fitting together of two jigsaw puzzle piecesWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.
- You are performing an enzyme kinetics experiment testing the effect of pH on reaction rate. You accidentally one of the tubes to react two minutes longer than the other samples. How would this affect the interpretation of the data you obtain for that one tube? A. No change in the interpretation of your data B. Your data would represent an underestimate of the enzyme's activity at that one pH. Your data would represent an overestimate of your enzyme's activity at that one pH. D. All of the data would be invalid.A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction? A. forms a covalent bond with the substrate B. reduces the entropy of the substrate C. stabilizes a charged intermediate D. acts as a proton donor Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active? A. aspartate is protonated; lysine is deprotonated B. both residues are deprotonated C. aspartate is deprotonated; lysine is protonated D. both residues are protonatedWhat type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown in the graph below where the solid Ine represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhíbítion B. Noncompetitive inhíbition C. Competitive inhíbition D. Uncompetitive inhibition Potassium cyanide ia a polson which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? A. Irreveraible inhibition c. Competitive inhibition D. Uncompetitive inhibition B. Noncompetitive inhibition _10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase в. Нуdrolase c. Isomerase D. Ligase Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase…
- Which of the following is NOT true? a. For many enzymes, Vmax is essentially equal to k3. b. Km is the reaction rate at 1/2 Vmax. c. At steady state the formation of ES is equal to the breakdown of ES. d. A Lineweaver-Burke plot generates a straight line. e. An Eadie-Hofstee plot generates a straight line.Which of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.What are allosteric modulators? A. These are inhibitors that bind at sites other than the active site of enzymes resulting in the reduction of enzyme activities B. These are activators that bind at sites other than the active sites of enzymes resulting in enhanced enzyme activities. C. These are either inhibitors or activators that bind at the active site of enzymes. D. These are either inhibitors or activators that bind at sites other than the active sites of enzymes reducing or enhancing the latter's activities. E. These are small molecules that bind to an ES complex only.
- Select all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formWhich 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.Potassium cyanide is a poison which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? c. Competitive inhibition D. Uncompetitive inhibition A. Irreversible inhibition B. Noncompetitive inhibition 10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase В. Нydrolase C. Isomerase D. Ligase 11. Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? C. Isomerase D. Ligase A. Kinase В. Нydrolase
