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Q14. The transition state is an important intermediate that can influence the rate of an exergonic reaction.
Which of the following statements about the transition state is correct?
A. At the transition state reacting molecules are the most stable.
B. The more molecules that can reach the transition state the faster the reaction will be.
C. The transition state increases in the presence of an enzyme.
D. If the transition state is high enough the reaction can move from being exergonic to being endergonic.
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- Q12. Suppose you conduct an experiment in the laboratory in which you add increasing amounts of substrate to a solution containing an enzyme and a pH buffer. You incubate the container at the optimal temperature for the enzyme. Each time you add more substrate, you measure the rate of the reaction. Also suppose that you graph the results such that the x axis shows the substrate concentration, and the y axis shows the resulting reaction rate. What will you find over time? A. The rate of the reaction will increase rapidly, taper off, and plateau. B. The resulting graph will be a perfect bell curve. C. The rate of the reaction will increase slowly, plateau, and then drop sharply back to zero. D. The rate of the reaction will proceed with a slope of 1 and continue in a linear fashion indefinitely or until you run out of reactants.Q14. The characterization of an enzyme by measuring the rate of its reaction includes determining the values for both Vmax and Km. Which of the following statements about these two parameters is correct? A. The presence of a competitive inhibitor will result in a lower Vmax. B. The Km increases as enzyme-substrate affinity increases. C. A reaction that has a high Vmax may have a low Km. D. An increase in enzyme concentration will only affect the Km not the Vmax.Q13: Pick 1 out of all the options for each blank. In reaction A, the stability of the substrate is (equal to, less than or greater than) the stability of the product. The free energy change, TRAINGLE G, of the reaction is (positive, zero or negative), so the reaction is considered (endergonic or exergonic) and (spontaneous, not spontaneous or at equilibrium). In reaction B, the stability of the substrate is (equal to, greater than or less than) the stability of the product. The free energy change, TRIANGLE G, of the reaction is (negative, positive or zero), so the reaction is considered (exergonic or endergonic) and (spontaneous, at equilibrium or not spontaneous).
- Q32: Which of the following is true about enzymes?O enzymes change the enerey in the productsO enzymes change activation energy required in a reactionO enzymes change the energy in the reactantsO enzymes change the amount of energy released in a reactionQ2. When discussing energy and enzymes our need to eat as human was discussed. With reference to the diagram below, which of the following statements explains why we need to eat? A. Food is required to ensure that reaction B stays high. B. Because reaction A is exergonic, it requires energy. C. Because reaction A results in increased entropy it needs a source of energy. D. Because reaction B will always occur, we need food energy for reaction A.Q10: What are the functions of the following enzymes in the MVA pathway? Give the full chemical equation for each step. a) AACT b) HMGS c) HMGR Q11: Explain the following reactions in the MVA pathway? Give the full chemical equation for each type. a) Claisen condensation b) Aldol type reaction c) Isomerization
- Introduction: (4 pts) (Answer questions in paragraph form - 300 words max) What are enzymes and what do they do? What are the optimal conditions for an enzyme? What factors affect enzyme activity and how? How is the structure of an enzyme related to its function? What is amylase? What reaction does it catalyze? Research the amylase enzyme you used (organism) and the optimal conditions of temperature, pH, or salt, it requires. Explain why DNS is used and why it is important for determining enzyme activity. Cite and reference your sources using APA style.Q28: In allosteric regulationO a molecule binds the active site of an enzyme blocking the substrateO a cofactor binds the active site of an enzyme blocking the substrateO a molecule binds a site other than the active site to regulate an enzymes actvlyO all of the aboveO a coenzyme binds the active site of an enzyme blocking the substrale9:34 AM You sent Help me with this one Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…
- 2a) explain the difference between the net free energy change of a reaction and the activation energy of the same reactionBIOC 384 Redox Reactions and Reduction Potentials Q10.1: Answer the following three-part question. a) Calculate the ΔEº’ for the citrate cycle reaction converting malate to oxaloacetate and describe how you calculated this value. b) What is the overall change in standard free energy (ΔGº') for this reaction and describe how you calculated it. c) Do you think the actual change in free energy (ΔG) for this reaction differs significantly from the standard free energy (ΔGº') for the reaction, and if so, why is it different?Q2: What is the maximum initial reaction rate for this enzyme at pH 7?
