8. Which of the following is characteristic of a competitive inhibitor of an enzyme-catalyzedreaction?A. The inhibitor binds covalently to the enzyme.B. The inhibitor increases the substrate binding affinity to the enzyme.C. In the presence of the inhibitor, the reaction exhibits an apparent increase in Km.D. In the presence of the inhibitor, the reaction exhibits an apparent decrease in Vmax-E. Increasing the substrate concentration fails to overcome the effects of the inhibitor.

Enzymes are biological catalysts which play important role catalysis of biochemical reactions.…

Answered: 8. Which of the following is…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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32. Which of the following is true? A. An exergonic reaction, energy is released and the delta G is positive B. An exergonic reaction, energy is stored and the delta G is negative C. An exergonic reaction, energy is released and the delta G is negative D. An exergonic reaction, energy is stored and the delta G is positive
Which of the following is incorrect about the competitive inhibitors? a. They increase the affinity of the enzyme for the substrate b. They increase KM c. They are structurally similar to the substrate d. They do not affect Vm max
A mixed inhibitor (sometimes called a mixed non-competitive inhibitor) of an enzyme: a decreases both Km and V-max. b increases Km and decreases V-max. c increases Km without altering V-max. d decreases Km without altering V-max.
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.
please make sure the answer you provide is correct i submitted this question differnt times and everytime i got a differnt answer
Which of the following is incorrect? a. The ratio "catalyzed rate/uncatalyzed rate" is known as catalytic power b. Most enzymes exhibit a higher degree of specificity than non-biologic catalysts O c. Most enzymes are proteins; but a few are RNA molecules Od. Most enzymes exhibit a higher catalytic power than non-biologic catalysts
Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
1.With the data shown below, please answer the following: A. Which of the two inhibitors is more efficient at high substrate concentrations? At low substrate concentrations? Explain you reasoning
15. When an atom or molecule loses one or more electrons, it is said to be: A. energized. B. oxidized. C. polarized. D. reduced. 16. A drug binds to the active site of an enzyme. If it is bound to the active site of the enzyme, it prevents substrate binding. This drug would be considered a(n) A. noncompetitive inhibitor. B. allosteric inhibitor. C. allosteric activator. D. competitive inhibitor. 17. If the AG of a reaction was +31.45 kJoules, which of the following is NOT true regarding this reaction? A. the products have more free energy than the reactants B. the reaction requires an energy input of 31.45 kJoules to proceed. C. The reaction is exergonic D. The reaction is endergonic 18. The large number of alveoli in lungs improve gas exchange by A. decreasing the distance for diffusion B. increasing the surface area for diffusion C. increasing the concentration difference D. changing the diffusion constant 19. Exchange of gases and metabolites between the blood and tissues occurs in…
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…

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