2. Indicate whether each of the following statements describes a reversible competitive inhibitor,reversible noncompetitive inhibition, or an irreversible inhibitor.a. It bonds covalently to the active siteb. The inhibitor effect can be reversed by the addition of more substratec. Inhibitor structure resembles that of the substrated. The inhibitor and substrate cannot bind to the enzyme simultaneously.

Enzymes are usually protein molecules which catalyzes the biochemical reaction by decreasing its…

Answered: 2. Indicate whether each of the…

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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1. A substance that is able to interact with an enzyme, reducing its ability to process a substrate, is called an inhibitor. If the inhibitor acts by temporarily attaching to an area other than the binding site, causing a change in the shape of the enzyme's active site, it would be a(n) a. Irreversible inhibitor b. Competitive inhibitor c. Reversible inhibitor d. Noncompetitive inhibitor 2. Several factors can affect the rate of an enzyme-catalyzed reaction. The following four diagrams show how reaction rates are affected by pH, temperature, substrate concentration and the amount of enzyme. Which diagram best represents how changes in the substrate concentration affect the rate? a b C d. While there are several theories used to explain how enzymes function, one popular one is call the induced-fit theory. Which of the following is the basis of that theory? 3. а. Different cofactors can be used by the same apoenzyme, allowing it to interact with an entire class of substrates. b.…
8. Which of the following is characteristic of a competitive inhibitor of an enzyme-catalyzed reaction? 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.
1. As seen in the picture: - What kind of inhibition (competitive, uncompetitive, mixed) is involved? - Calculate Vmax and Kmax in the absence and presence of inhibitor A Show complete solution.
Indicate whether each of the following statements describes a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. More than one answer may apply.a. Both inhibitor and substrate bind at the active site on a random basis.b. The inhibitor effect cannot be reversed by the addition of more substrate.c. Inhibitor structure does not have to resemble substrate structure.d. The inhibitor and substrate can bind to the enzyme simultaneously
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…
4. Compare and contrast the mechanism used by competitive and noncompetitive enzyme inhibitors. Which type of inhibitor can be "out-competed" by adding extra substrate to a reaction?
1. Activatotrs are types of A. inhibitor B. cofactor C. enzyme D. substrate 2. Which of the following does NOT affect enzyme selectivity ? A. Electrostatic interactions B. Molecular shape C. hydrophillic Interactions D. None of these answers are correct
1. A competitive inhibitor for an enzyme a. b. C. d. e. changes the apparent Km but has no effect on Vmax. alters Vmax but has no effect on Km. is competitive with respect to substrate for binding to the enzyme active site. Answers a and care both correct. Answers b and care both correct.
3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…
1. A substrate is converted to product using an enzyme that follows the mechanism below when an inhibitor (1) and an activator (A) are both present in the reaction mixture. ES (2)→→ E + P E+S (1) E +1 < (3) → EI E+A← (4)→ EA {the inhibitor and activator do not bind simultaneously} EI + S EA+S (5) → EIS -(6)→ EI + P (7)→ EAS-(8)→ EA + P with reaction rate constants of k₁ and k.₁ (and so on) for each of the reactions: A. Although this mechanism does not match exactly any of the inhibitor mechanisms discussed in class, which type of inhibitor is this most like (competitive, uncompetitive or non-competitive)? B. Write the enzyme balance equation. C. Write the total rate of product, P, formation based on the kinetic rate constants and concentrations of intermediate species. D. Write each of the equations that result from applying the rapid equilibrium and quasi steady state assumptions. E. Knowing that I is an inhibitor and A is an activator, discuss the relative values of k₂, k6 and kg.
. Define the following terms:a. competitive inhibitorb. uncompetitive inhibitorc. noncompetitive inhibitord. reversible inhibitione. irreversible inhibition
A noncompetitive inhibition can be overcome/reverse by which of the following: a. Increasing [enzyme] b. Increasing [Substrate] c. Increasing [product] d. All of the above

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2. Indicate whether each of the following statements describes a reversible competitive inhibito reversible noncompetitive inhibition, or an irreversible inhibitor.