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Case Studies In Health Information Management

Case Studies In Health Information Management

3rd Edition

ISBN:9781337676908

Author:SCHNERING

Publisher:SCHNERING

Chapter4: Revenue Management

Section: Chapter Questions

Problem 4.14.5C

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Which of the following statements are true for enzymes? Check all that apply.
The activity of some enzymes can be modulated by allosteric effectors.
All enzymes are more active when dephosphorylated.
Enzymes are subjected to a rapid turnover.
All enzymes are more active when phosphorylated.
The activity of some enzymes can be modulated by regulatory proteins.

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In the regulation of enzyme activity by phosphorylation (as discussed in class), the introduction of phosphate to the enzyme being controlled: requires a protein phosphatase enzyme but not ATP requires a protein phosphatase enzyme plus ATP O requires a protein kinase enzyme but not ATP O requires a protein kinase enzyme plus ATP
Compare and contrast the actions of an allosteric effector, a competitive enzyme inhibitor, and a noncompetitive inhibitor.
Describe the mechanism of feedback inhibition and the role this process plays in controlling enzyme activity.
You have a reaction that is very slow on its own, but is accelerated in the presence of an enzyme. Which of the listed effects would be brought about by an enzyme catalyzing this reaction? (Select all that apply) increased kcat increased Keq increased biochemical standard free energy change decreased activation energy
List two means by which enzyme activity is directly regulated.
List three ways to alter the rate of an enzyme-mediated reaction.
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
For a protein that binds multiple ligands with negative cooperativity, which of the following is true? Each ligand bound increases the dissociation constant for subsequent ligands. Ligands cannot bind to the protein. The dissociation constant is not affected by binding of other ligands. Each ligand bound decreases the dissociation constant for subsequent ligands.
List the local effectors of enzyme kinetics and give an example for one of them.
Select the graph that correctly illustrates the effect of a positive modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector. R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that this is a positively cooperative enzyme, meaning that the affinity for substrate increases with increasing substrate concentration.
An inactive form of an enzyme becomes active after being phosphorylated. When glucose is converted to glucose-6-phosphate by hexokinase, the accumulation of glucose-6-phosphate inhibits the reaction. A foreign substance is added to the reaction above. This substance binds to hexokinase and prevents its ability to catalyze the reaction.
In allosteric activation_ O the substrate only binds to the low affinity enzyme. the effector binds to the high affinity enzyme. less product is formed in the absence of the effector. more product is formed in the absence of the effector. the effector binds to the low affinity enzyme. Select all that apply.

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