5 31. What are the advantages of metabolic channeling? Describe two mechanisms of metabolic channeling?32. The regulatory and catalytic sites on a quaternary structured enzyme could be on different subunits.True or False?33. The most common allosteric enzyme inhibitors act competitively. True or False?34. By raising the substrate concentration sufficiently high, all modes of allosteric inhibition can be overcome.True or False?35. All irreversible enzyme inhibitors are synthetic.True or False?

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Description: 5 31. What are the advantages of metabolic channeling? Describe two mechanisms of metabolic channeling?32. The regulatory and catalytic sites on a quaternary structured enzyme could be on different subunits.True or False?33. The most common allosteri

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What are the advantages of metabolic channeling? Describe two mechanisms of metabolic channelirg

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 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

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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.
1. What do some enzymes require for catalytic activity? What is a catalytically active complete enzyme called, along with its cofactor?2. Classify the enzymes. What class of enzymes are lactate dehydrogenase and alpha-amylase?3. What is the function of an enzyme as a catalyst? Where does an enzyme-catalyzed reaction occur?4. What is the most used enzyme activity unit? What is understood when one unit of enzyme activity is mentioned?5. What are the factors affecting the rate of an enzymatic reaction?6. What are the reasons why the rate of a reaction catalyzed by an enzyme decreases over time?7.Describe the relationship between ACE2 (Angiotensin converting enzyme 2) and the COVID-19 outbreak using bioinformatics tools.
Item 35 Organic cofactors are referred to as _________. Fill in the blank 36 Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e.substrate, and its effectiveness depends on product concentration.
Item 35 Organic cofactors are referred to as _________. Fill in the blank Item36 Item Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e. substrate, and its effectiveness depends on product concentration. Item37 Item 37 A substance that binds to the active site of an enzyme and turns it off is called a _________ inhibitor. Fill in the blank Item 38 Lactase is an enzyme that digests lactose. True or False Item 39 Exergonic reactions do not require activation energy. True or False
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
1. Can you describe how electrostatic and steric considerations may lead to preferential stabilization of the transition state at an enzyme active site? 2. What factors are involved in “transition-state complementarity”?
1. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 2. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
47. Which of the following is true under the following conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 mM. (1 nM = 10-9 M, 1 μM=10-6 M, 1 mM = 10-3 M) Group of answer choices Between 0% and 50% of active sites have substrate bound 0% of active sites have substrate bound 50% of active sites have substrate bound 100% of active sites have substrate bound Between 50% and 100% of active sites have substrate bound
an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
1a-Which of the following is/are true for all exergonic reactions? Select all that apply Select one or more: a. The products have more total free energy than the reactants. b. The reaction proceeds with a net release of free energy c. The reaction requires energy from a coupled endergonic reaction d. A net input of energy from the surroundings is required for the reactions to proceed 1b-Which of the following can change the activity of a single enzyme? Select all that apply Select one or more: a. An inhibiting molecule noncovalently binding to the active site. b. A regulatory molecule noncovalently binding to a location other then the active site (an allosteric site). c. Another enzyme phosphorylating the enzyme of interest. d-Removal of a small section of the enzyme.
7. What is the activation site of an enzyme? 8. What does it mean to denature an enzyme? 9. List at least 2 ways an enzyme may be denatured. 10. Explain the difference between endergonic and exergonic reactions.
1.The class of enzyme that catalyzes addition of a group to a double bond is? oxidoreductases lyases ligases isomerases hydrolases transferases 2. Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme? the active site of the enzyme must be rigid the active site of the enzyme must be flexible only one substrate could be converted to product by the enzyme the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures the entire enzyme must be rigid 3. Which of the following enzymes is found in blood serum and is diagnostic of prostate cancer if enzyme levels are elevated? alanine aminotransferase phosphohexose isomerase lactate dehydrogenase acid phosphatase alkaline phosphatase 4. A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of…