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Multiple Choice
How do ADP and ATP interact with the enzyme phosphofructokinase in cellular metabolism?
A
Both ADP and ATP act as allosteric activators.
B
ADP acts as an allosteric activator, while ATP acts as an allosteric inhibitor.
C
ADP acts as an allosteric inhibitor, while ATP acts as an allosteric activator.
D
Both ADP and ATP act as allosteric inhibitors.
Verified step by step guidance
1
Understand the role of phosphofructokinase (PFK) in cellular metabolism: PFK is a key regulatory enzyme in glycolysis, which is the metabolic pathway that converts glucose into pyruvate, generating ATP in the process.
Learn about allosteric regulation: Allosteric regulation involves the binding of molecules at a site other than the enzyme's active site, causing a change in the enzyme's activity. This can either activate or inhibit the enzyme.
Identify the role of ATP in regulating PFK: ATP, being a product of glycolysis, acts as an allosteric inhibitor of PFK. When ATP levels are high, it binds to PFK and decreases its activity, slowing down glycolysis to prevent excess ATP production.
Identify the role of ADP in regulating PFK: ADP, a product of ATP consumption, acts as an allosteric activator of PFK. When ADP levels are high, it indicates a need for more ATP, thus activating PFK to speed up glycolysis.
Conclude the interaction: ADP and ATP have opposite effects on PFK. ADP activates PFK to increase glycolysis and ATP production, while ATP inhibits PFK to decrease glycolysis when energy levels are sufficient.