
Understanding Allosteric Enzymes

Interactive Video
•
Biology
•
10th - 12th Grade
•
Hard
Jennifer Brown
FREE Resource
10 questions
Show all answers
1.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is a characteristic feature of allosteric enzymes?
They consist of a single polypeptide unit.
They have multiple active sites.
They are always in an active state.
They do not change shape.
2.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
How does an activator affect an allosteric enzyme?
It stabilizes the inactive state.
It prevents substrate binding.
It deactivates the enzyme.
It stabilizes the active state.
3.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What role do non-competitive inhibitors play in enzyme activity?
They bind to the active site.
They increase substrate affinity.
They change the enzyme's shape.
They activate the enzyme.
4.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is an example of a protein that exhibits cooperativity?
Insulin
Collagen
Myoglobin
Hemoglobin
5.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
How does the binding of one oxygen molecule affect hemoglobin?
It decreases the affinity for more oxygen.
It has no effect on other subunits.
It increases the likelihood of other subunits binding oxygen.
It causes the hemoglobin to release all oxygen.
6.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What happens when oxygen is offloaded from hemoglobin?
It increases the chance of other subunits binding oxygen.
It decreases the likelihood of other subunits releasing oxygen.
It has no effect on other subunits.
It increases the chance of other subunits releasing oxygen.
7.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is the main function of allosteric inhibitors?
To enhance enzyme activity.
To stabilize the inactive state.
To increase substrate binding.
To stabilize the active state.
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