Answered: 4. What is the effect of changing the…

4. What is the effect of changing the concentration of the catalase? 5. What is the effect of temperature on catalase? 6. Differentiate INDUCED FIT MODEL from LOCK AND KEY model of the enzyme.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 5TYK: In the following graph: A represents the product. B represents the energy of activation when enzymes...

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Please answer the three given questions. Thank you.

4. What is the effect of changing the concentration of the catalase?
5. What is the effect of temperature on catalase?
6. Differentiate INDUCED FIT MODEL from LOCK AND KEY model of the enzyme.

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In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
3. How does changes in enzymatic factors affect the native conformation of enzymes? What happens to the enzyme’s native conformation once it is denatured? What structural organization are destroyed by this process? Answer thoroughly.
1. What are the differences classification of enzymes? List 5 classification of enzymes and cite their functions.
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
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1. How do pH and temperature affect enzyme activity? 2. What do the graphs suggest about the activity of the enzyme?
5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?
1. Which of the following options is a viable way to increase the Vmax of an enzymatic reaction? Increase the amount of substrate present. Increase the amount of enzyme present. Decrease the temperature of the reaction. Decrease the Km of the enzyme.