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According to the law of mass action, which of these conditions will drive the reaction
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Human Physiology
- The important amino acid residues in the active site of enzyme X were found to be aspartic acid and lysine. In an experiment, the pH of the buffer solution in which enzyme X was dissolved was changed from pH 7 to pH 5. What would be the expected effect of this change on the enzyme’s catalytic activity? A. decrease B. increase C. unchanged D. cannot be determinedarrow_forwardWhich ONE of the following would be most effective as a feedback mechanism for anenzymatic reaction? A. Reduced concentration of the product B. A change in pH C. Increased concentration of substrate D. Temporary binding of a non-substrate molecule in the active binding sitearrow_forwardYou have a reaction that takes 8 hours to reach completion at 20 degrees celcius. What is the likely result of changing the temperature to 30 degrees celcius? a. the reaction should take less times b. reaction time would be unaffected c. the reaction should take more time Which would be the correct answer to this question?arrow_forward
- Assuming an excess of substrate, if the enzyme concentration is doubled in a reaction vessel, the number of substrate molecules converted to product per minute will: a. be 1/2 as much as originally b. remain the same as originally c. be twice as much as originally d. only be able to be determined experimentally e. no correct response is givenarrow_forwardWhat is the reason why the transition state of a catalyzed reaction is lower has lower energy compared to an uncatalyzed reaction? A. because enzymes only work at low temperatures B. because of favorable interactions with the substrate C. because of enthalpic interactions between the enzyme and the transition state D. A and Barrow_forwardWhich of the following is NOT true about enzymes A. they do not alter reaction equilibria B. they accelerate the forward rate of a reaction C. they decrease ∆G’0 of a reaction D. they accelerate the reverse rate of a reaction E. they stabilize transition statesarrow_forward
- Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that applyarrow_forwardWhich of the following statements is TRUE in describing the activity of the lactaseenzyme? A. Lactase is converted to glucoseB. One lactase enzyme can catalyze many reactions C. The shape of lactase does not change during the reaction D. Lactase can function effectively at many different pH levelsarrow_forwardPotassium 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. Нydrolasearrow_forward
- Choose in the options what do enzymes do for the activation of energy of the reaction -Ea, given the theory of collision? a. enzymes will bind the reactants b. enzyme will raise temperature to incease the level of energy level. c. enzyme will provide an alternative reaction pathwayarrow_forwardSome enzymes function to breakdown harmful compounds that if allowed to accumulate could cause death. Below is a plot of the velocity of enzyme catalysis as a function of substrate concentration. Which one of the curves shown here is most likely for an enzyme that catalyses the breakdown of a toxic compound? A. A B. B C. C D. Darrow_forwardHow does a non-competitive inhibitor decrease the rate of an enzyme reaction? O A. by binding at the active site of the enzyme B. by changing the shape of the active site on the enzyme, without binding to active site O C. by changing the free energy change of the reaction D. by acting as a coenzyme for the reactionarrow_forward
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