Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 6, Problem 8TY
Summary Introduction
Introduction: Vmax is the maximum value of velocity which is attained by the enzyme and after this value, the enzyme activity decreases. Km.is the maximum value of substrate concentration corresponding to the half of the value of Vmax
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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.
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
An enzyme-substrate solution has been "poisoned" with a noncompetitive inhibitor. It is expected that the addition of more substrate to the solution will _____ the activity of the enzyme.
a. increase
b. decrease
c. have no effect on
Chapter 6 Solutions
Biology
Ch. 6.1 - Which do you think has more entropy, a NaCl...Ch. 6.1 - Prob. 2CCCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 1CSCh. 6.2 - Prob. 1EQCh. 6.2 - Prob. 2EQCh. 6.2 - Prob. 3EQCh. 6.3 - Prob. 1CSCh. 6.3 - Prob. 2CS
Ch. 6.4 - What are advantages of protein degradation?Ch. 6 - Reactions that release free energy are a....Ch. 6 - Enzymes speed up reactions by a. providing...Ch. 6 - Prob. 3TYCh. 6 - Researchers analyzed a cell extracta mixture of...Ch. 6 - In biological systems, ATP functions by a....Ch. 6 - In a chemical reaction, NADH is converted to NAD+...Ch. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Autophagy provides a way for cells to a. degrade...Ch. 6 - Prob. 1CQCh. 6 - Prob. 2CQCh. 6 - Prob. 3CQCh. 6 - Prob. 1COQCh. 6 - Prob. 2COQ
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- A new drug has been discovered which inhibits the reaction catalyzed by enzyme A. The information on this drug is shown in the graph below. Based on this information, which one of the following is most correct about this drug? 1/No 2- inhibitor (0.1 uM] no inhibitor 11 1/[S), uM OA. competitive inhibitor binding to the substrate O B. competitive inhibitor binding to free enzyme A OC. uncompetitive inhibitor binding to [ES] O D. uncompetitive inhibitor binding to the Michaelis complex O E. allosteric enzymearrow_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_forwardWhat is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substratearrow_forward
- An inhibitor that reversibly binds to a site other than the enzyme's active site is called a(n) a. noncompetitive inhibitor b. competitive inhibitor c. antagonisitc inhibitor d. antibioticarrow_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 folowing types of inhibitors binds to the active site of an enzyme? Select one: a. Competitive b. All of them C. Uncompetitive O d. Noncompetitivearrow_forward
- If a competitive inhibitor of an enzyme is added to the mixture of the enzyme and its substrate, the inhibitor will: O a. decrease the value of Vmax for the chemical reaction catalyzed by this enzyme O b. decrease the value of KM for the chemical reaction catalyzed by this enzyme O c. increase the value of KM for the chemical reaction catalyzed by this enzyme O d. increase the value of Vmax for the chemical reaction catalyzed by this enzymearrow_forwardWhich of the following is incorrect about enzyme inhibitors? a. They can be reversible or irreversible b. The irreversible inhibitors form a covalent bond with the enzyme C. Some irreversible inhibitors are called suicide inhibitors d. Aspirin is an example of a reversible inhibitorarrow_forwardWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.arrow_forward
- Molecule X is expected to be a non-competitive inhibitor of an enzyme. If the inhibitor was tested at a saturating level of substrate the following would be observed: a. The inhibitor would decrease the Vmax b. The inhibitor would increase the Km c. The inhibitor would decrease the Km d. The inhibitor would increase the Vmax e. The inhibitor would not change the Vmaxarrow_forwardThe 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_forwardThere is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitivearrow_forward
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