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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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Question

Which of the following statements
concerning uncompetitive inhibitors is NOT
true?
a. They decrease the Km
b.
c.
Od.
O e.
They bind to both ES and Enzyme
They decrease the Vmax
They bind to ES only
No product is formed after their binding

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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
Indicate how the observed Km of an enzyme would change in the presence of inhibitors having the given effect on a and a'. Increased a=a²=1.0 Decreased a> a 10 Answer Bank Unchanged a' > 1.0
Where does inhibitor binds on enzyme in mixed inhibition? A Allosteric site B Binds on substrate C At active site D Does not bind on enzyme
From the chart below, comment on the effect of substrate concentration on the rate of reaction.
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.
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.
Km of LDH with substrate 1 is 60 M and Km with substrate 2 is 45 M. The enzyme has a higher affinity for substrate 2. true or false
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.
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

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