BIOLOGY 2E
2nd Edition
ISBN: 9781506699851
Author: OpenStax
Publisher: XANEDU PUBLISHING
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Chapter 6, Problem 24CTQ
Explain in your own words how enzyme feedback inhibition benefits a cell.
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Explain how enzymes are regulated by feedback inhibition.
Describe the mechanism of feedback inhibition and the role this process plays in controlling enzyme activity.
List three ways to alter the rate of an enzyme-mediated reaction.
Chapter 6 Solutions
BIOLOGY 2E
Ch. 6 - Figure 6.8 Look at each of the processes shown,...Ch. 6 - Figure 6.10 If no activation energy were required...Ch. 6 - Figure 6.14 The hydrolysis of one ATP molecule...Ch. 6 - Energy is stored long-term in the bonds of and...Ch. 6 - DNA replication involves unwinding two strands of...Ch. 6 - Consider a pendulum swinging. Which type(s) of...Ch. 6 - Which of the following comparisons or contrasts...Ch. 6 - Which of the following is the best way to judge...Ch. 6 - Which of the following is not an example of an...Ch. 6 - In each of the three systems, determine the state...
Ch. 6 - The energy released by the hydrolysis of ATP is...Ch. 6 - Which of the following molecules is likely to have...Ch. 6 - Which of the following is not true about enzymes...Ch. 6 - An allosteric inhibitor does which of the...Ch. 6 - Which of the following analogies best describes...Ch. 6 - Does physical exercise involve anabolic and/or...Ch. 6 - Name two different cellular functions that require...Ch. 6 - Explain in your own words the difference between a...Ch. 6 - Describe the position of the transition state on a...Ch. 6 - Imagine an elaborate ant farm with tunnels and...Ch. 6 - Energy transfers take place constantly in everyday...Ch. 6 - Do you think that the Ea for ATP hydrolysis is...Ch. 6 - With regard to enzymes, why are vitamins necessary...Ch. 6 - Explain in your own words how enzyme feedback...
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- Define the word "enzyme inhibition."arrow_forwardList factors that affect the rate of an enzyme-controlled reaction.arrow_forwardThe effect of on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) an allosteric effector a noncompetitive inhibitor a competitive inhibitorarrow_forward
- All of the following are mechanisms for regulating enzyme activity in the cell, except: a. Rate of enzyme synthesis (at the gene level) b. Changes in temperature C. Covalent modification (like phosphorylation) d. Allosteric feedback inhibitionarrow_forwardDifferentiate between competitive and non competitive inhibition of enzymes.arrow_forwardMany biosynthetic pathways are regulated by feedback control, where the product of a pathway turns off an enzyme that catalyzes an early step in the pathway. Usually, this control comes from an allosteric interaction. Of the types of reversible enzyme inhibition (Competitive inhibition, Noncompetitive inhibition, and Uncompetitive inhibition), what type is most likely to occur in a feedback control mechanism like this and why?arrow_forward
- Describe and explain the Examples of two common control mechanisms for enzymes.arrow_forwardenzymes can be inhibited or competition can occur. Explain each of these.arrow_forwardWhich 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.arrow_forward
- 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.arrow_forwardWhich of the following statements are true about enzyme regulation via noncovalent interactions? Select all that apply. Molecules can cause a change in enzyme shape because they're able to bind to the enzyme somewhere other than the active site The function of an enzyme is altered by a chemical change in its primary structure, which is called phosphorylation Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to the enzyme's active site Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to a location other than the active sitearrow_forwardThe inhibition that make permanent damage to an enzyme is called: O Noncompetitive O Competitive O Reversible Irreversiblearrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License