Which of the following is incorrect about the enzyme chymotrypsin? a. It catalyzes the addition of water across a double bond O b. It is known as a serine protease O c. Artificial substrates are used to monitor the reaction catalyzed by the enzyme Od. It is classified as a hydrolase
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- Which statements are true of an inhibitor that binds the active site of an enzyme? Select all that apply, there may be one correct answer or several. a These inhibitors are a kind of allosteric regulator that decreases enzyme activity. b Adding more substrate can reduce the effect of these inhibitors. c These inhibitors compete with the substrate for the active site of the enzyme. d These inhibitors increase the rate of enzyme activity. e These inhibitors function by changing the shape of the enzyme, stopping if from binding to substrate.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.Cells carry out anabolic as well as catabolic pathways, with some enzymes functioning in both types of pathways. (a) Explain why these enzymes catalyze near-equilibrium reactions. (b) Explain why opposing anabolic and catabolic pathways must have different enzymes for at least one of the steps.
- Which of the following accurately describes how an enzyme functions? a. reduces the energy content of the products b. allows for the exothermic reaction of materials that are usually endothermic c. changes the reaction mechanism effectively reducing the activation energy d. shifts the equilibrium for the reactionAn enzyme-substrate solution has been "poisoned" with a noncompetitive inhibitor. It is expected that the addition of more substrate to the solution will _____ the activity of the enzyme. a. increase b. decrease c. have no effect onthe type of enzyme inhibition in which covalent bulky adduct prevents catalysis is ? a) uncompetitive b) reversible c) noncompetitive d) competitive e) Irreversible
- In the metabolic pathway, A->B->C->D->E what effect would molecule E likely have on the enzyme that catalyzes A->B? (The answer is A. Could you justify the reason why the answer is A?) a) Allosteric inhibitor b)Allosteric activator c) Competitive inhibitor d) feedback activator e) coenzymeCharacterization of enzyme activity does not allow us to: a. determine how different variables affect the enzyme's ability to function b. determine the molecular composition of the enzyme c. determine the optimal environment for an enzyme to function d. determine the effect of inhibitors on the enzymeWhich of the following statements concerning enzymes is TRUE? a. Enzymes can increase the equilibrium constant of a reaction by 1000-fold. b. The activity of many enzymes can be regulated. c. Many enzymes are consumed in the reactions they catalyze. d. The rate of enzymatic catalysis is independent of pH.
- Which of the following would best explain how an enzyme catalyzes two different reactions? A) The enzyme contains a-helices and B-pleated sheets. B) The enzyme is subject to cooperativity C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures D) The enzyme is subject to competitive inhibition and allosteric regulation E) The enzyme is composed of at least two subunitsWhich of the following is TRUE about the enzymatic catalysis of a chemical reaction? A. It increases the energy of the transition state B. It decreases the free energy ∆G so that a reaction can proceed spontaneously C. It decreases the energy of the transition state D. It increases the forward and reverse ratesEnzymes have similar responses to both changes in temperature and pH. The effect of both is on the a. rate of movement of the substrate molecules. b. strength of the chemical bonds within the substrate. c. three-dimensional shape of the enzyme. d. rate of movement of the enzyme.