Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 9, Problem 17RQ
What is the effect of an inhibitor binding an enzyme?
- The enzyme is degraded.
- The enzyme is activated.
- The enzyme is inactivated.
- The complex is transported out of the cell
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Students have asked these similar questions
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
The site where a noncompetitive inhibitor
binds to an enzyme is called:
Active site
Receptor site
Coenzyme
O Allosteric site
Enzyme linked receptors:
PMSF is a protease inhibitor that binds to enzyme active site. What is the
possible mode of inhibition?
Competitive
O Irreversible
O Non-competitive
O Mixed
Chapter 9 Solutions
Biology 2e
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- Which of the following statements is/are correct?a) Enzyme quantities depend on the rate of their synthesis and degradationb) Enzyme quantity is decreased if an amino-acid involved in the catalytic activity is modifiedc) Protein kinase A activity is regulated through protein interaction.d) Kinases control the activity of other enzymes by covalent modification; irreversiblephosphorylation explain each of the following optionarrow_forwardIn the diagram below, the orange circle represents an effector and the dark purple shapes (both the diamond and the rod) represent a substrate. Based on this information, which statement(s) about the diagram is/are true? Select all that apply. A Allosteric site B Allosteric site C Allosteric site Allosteric effector Active site Allosteric effector Active site, Allosteric effector Novel binding sitearrow_forwardInducers and repressors Both of them increase in the rate of enzyme synthesis Both of them decrease in the rate of enzyme synthesis They control the enzyme quantity They control the enzyme activityarrow_forward
- With the aid of a diagram, explain feedback inhibition and feedback repression.arrow_forwardWhen protein kinase A (PKA) is inactive, which of the following statements is true? ATP is bound to the regulatory subunit to inhibit subunit dissociation. CAMP is bound to the catalytic site to inhibit the regulatory subunit. The regulatory subunit has cyclic GMP bound in place of cyclic AMP. The intrinisic pseudosubstrate peptide is bound to the active site.arrow_forwardWhat are the cellular advantages to feedback inhibition?arrow_forward
- A segment of cell's collection of biochemical pathways is shown below. P is a product of one series of these reactions. It is also a regulatory molecule. Look at the pathway below and indicate the position(s) at which M is most likely to act as a feedback inhibitor when its concentration gets too high. 1 2 3 4 5 A----->B -----> C----->E----->J------>M----->P----->X----->Zarrow_forwardWhich of the following regulatory methods could never increase enzyme activity? phosphate removal by a phosphatase phosphate addition by a kinase allosteric regulation negative feedback positive feedbackarrow_forwardwhen enzymes are placed into not optimal conditions. the enzymes’s active site shape is altered and the enzyme loses its function. when this occurs, the enzyme is said to have: denatured decarboxylated dephosphorylated desensitized depolarized -in the “DNA extraction from fruit” laboratory, what solution disrupted the cell and nuclear membrane? methyl orange hydrogen peroxide tap water detergent and a salt-based lysis solution ice-cold ethanol. -which of the following parts of the spectrophotometer covents light energy into electrical energy. photometric energy light energy monochromator phototube sample holderarrow_forward
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