EP CONNECT ONLINE ACCESS FOR BIOLOGY
20th Edition
ISBN: 9781260494655
Author: Raven
Publisher: MCG COURSE
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Chapter 6, Problem 6A
Summary Introduction
Introduction:
For the efficient operation of the biochemical pathway, the activity of the reactions in that pathway needs to be regulated and coordinated. In circumstances when the product of the reaction is plenty, in those situations synthesizing more products would be wastage of energy. One of these regulatory mechanisms is known as the feedback inhibition.
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Students have asked these similar questions
The mechanism in which the end product of a metabolic pathway inhibits an either step in the pathway is known as
A. Reversible inhibition
B. Metabolic inhibition
C. Feedback inhibition
D. Allosteric inhibition
E. Noncoopetative inhibition
Which of the following statements about allosteric enzyme regulation are true.
A. Allosteric regulation is always used to negatively regulate enzyme activity.
B. Allosteric regulators are often end products of a biochemical pathway.
C. Different allosteric regulators turn enzyme activity on or off by binding the same site.
D. Binding of allosteric regulators alters the conformation of an enzyme.
Which of the following statements about allosteric enzyme regulations are true.
A. Allosteric regulations is always used to negatively regulate enzyme activity.
B. Allosteric regulations are often end products of a biochemical pathway.
C. Diffrent allosteric regulators turn enzyme activity on or off by binding the same site.
D. Binding of allosteric regulators alters the conformation of an enzyme.
B only
B and C
B and D
D only
A and D
Chapter 6 Solutions
EP CONNECT ONLINE ACCESS FOR BIOLOGY
Ch. 6.1 - Prob. 1LOCh. 6.1 - Prob. 2LOCh. 6.1 - Describe the nature of redox reactions.Ch. 6.2 - Explain the laws of thermodynamics.Ch. 6.2 - Prob. 2LOCh. 6.2 - Contrast the course of a reaction with and without...Ch. 6.3 - Describe the role of ATP in short-term energy...Ch. 6.3 - Prob. 2LOCh. 6.4 - Discuss the specificity of enzymes.Ch. 6.4 - Explain how enzymes bind to their substrates.
Ch. 6.4 - Prob. 3LOCh. 6.5 - Prob. 1LOCh. 6.5 - Prob. 2LOCh. 6.5 - Prob. 3LOCh. 6 - Prob. 1DACh. 6 - A covalent bond between two atoms represents what...Ch. 6 - During a redox reaction the molecule that gains an...Ch. 6 - Prob. 3UCh. 6 - A spontaneous reaction is one in which a. the...Ch. 6 - Prob. 5UCh. 6 - Which of the following is NOT a properly of a...Ch. 6 - Where is the energy stored in a molecule of ATP?...Ch. 6 - Prob. 1ACh. 6 - Which of the following statements is NOT true...Ch. 6 - Prob. 3ACh. 6 - Prob. 4ACh. 6 - Enzymes have similar responses to both changes in...Ch. 6 - Prob. 6ACh. 6 - Examine the graph showing the rate of reaction...Ch. 6 - Phosphofructokinase functions to add a phosphate...
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- An allosteric inhibitor does which of the following? a. Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding. b. Binds to the active site and blocks it from binding substrate. c. Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate. d. Binds directly to the active site and mimics the substrate.arrow_forwardWhich of the following is a primary function of the active site of an enzyme? a. It binds allosteric regulators of the enzyme. b. It binds noncompetitive inhibitors of the enzyme. c. It catalyzes the reaction associated with the enzyme. d. It is activated by the presence of the end product of the metabolic pathway in which the enzyme is involved. Clear my choice Question 2 Not yet answered Points out of 2.00 Flag question Question text Which of the following statement about the mass spectrometry is true? a. Large amount of protein sample is needed for mass spectrum, and thus it is very expensive. b. It is a powerful method to determine the 3-dimensional structure of proteins. c. It can be sued for protein location in a living cell. d. It can be used to measure the molecular weight of proteins. e. It can be used to determine the stability of a protein structure in solution. Clear my choice…arrow_forwardIn drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mmarrow_forward
- The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.arrow_forwardAn enzyme has the ability to catalyze reactions of several unrelated compounds. The mechanism of how this enzyme operates is best explained by a. the lock-and-key theory b. the induced-fit theory c. the enzyme-substrate complex d. the efficiency of the enzymearrow_forwardIndicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.arrow_forward
- Which 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_forwardA noncompetitive inhibitor (Circle one). a. Binds at the active site of the enzyme. b. Alters the three-dimensional structure of the enzyme. c. Increases the rate of the enzyme-catalyzed reaction. d. Has a structure similar to the substrate. e. Has its effect reversed by adding more substrate.arrow_forwardWhich 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.arrow_forward
- A noncompetitive inhibition is best overcome (or reversed) by: A. Increasing [enzyme] B. Increasing [product] C. Increasing [Substrate] D. All of the abovearrow_forwardHow could you use the diversity of metabolic pathways that produce the same or similar products to critique this argument? Rank the steps from first to last. a. New enzymes cause modification of the pathway in an advantageous way. b. The biochemical pathway is gradually modified. c. A pathway exists and accomplishes some functions. d. An organism with cellular enzymes has mutations that allow new enzymes to arise.arrow_forwardIn competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.arrow_forward
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