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Inhibition of hexokinase by glucose-6-phosphate is an example of
- a)Competitive and reversible process
- b)Allosteric modulation
- c)Competitive and irreversible process
- d)Non-competitive and irreversible process
Correct answer is option 'B'. Can you explain this answer?
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Inhibition of hexokinase by glucose-6-phosphate is an example of allosteric modulation.
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Allosteric Modulation of Hexokinase by Glucose-6-phosphate:
Hexokinase is an important enzyme in glycolysis that catalyzes the phosphorylation of glucose to form glucose-6-phosphate. Glucose-6-phosphate is a product of this reaction and acts as an allosteric inhibitor of hexokinase.
Allosteric Inhibition:
Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is distinct from the active site, causing a conformational change in the enzyme that reduces its activity. In this case, glucose-6-phosphate binds to hexokinase in a non-competitive manner, meaning it does not compete with glucose for the active site.
Reversible Process:
The inhibition of hexokinase by glucose-6-phosphate is reversible, meaning that once the inhibitor is removed, the enzyme activity can be restored. In this case, the binding of glucose-6-phosphate to hexokinase is not permanent and can be reversed.
Significance:
This allosteric modulation of hexokinase by glucose-6-phosphate plays a crucial role in regulating glycolysis. As the product of the reaction, glucose-6-phosphate acts as a feedback inhibitor to prevent the excessive accumulation of this intermediate in the pathway. This helps to maintain metabolic homeostasis and prevent wasteful consumption of ATP.
In conclusion, the inhibition of hexokinase by glucose-6-phosphate is an example of allosteric modulation, a reversible process that helps regulate glycolysis by controlling enzyme activity in response to the levels of intermediates in the pathway.
Hexokinase is an important enzyme in glycolysis that catalyzes the phosphorylation of glucose to form glucose-6-phosphate. Glucose-6-phosphate is a product of this reaction and acts as an allosteric inhibitor of hexokinase.
Allosteric Inhibition:
Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is distinct from the active site, causing a conformational change in the enzyme that reduces its activity. In this case, glucose-6-phosphate binds to hexokinase in a non-competitive manner, meaning it does not compete with glucose for the active site.
Reversible Process:
The inhibition of hexokinase by glucose-6-phosphate is reversible, meaning that once the inhibitor is removed, the enzyme activity can be restored. In this case, the binding of glucose-6-phosphate to hexokinase is not permanent and can be reversed.
Significance:
This allosteric modulation of hexokinase by glucose-6-phosphate plays a crucial role in regulating glycolysis. As the product of the reaction, glucose-6-phosphate acts as a feedback inhibitor to prevent the excessive accumulation of this intermediate in the pathway. This helps to maintain metabolic homeostasis and prevent wasteful consumption of ATP.
In conclusion, the inhibition of hexokinase by glucose-6-phosphate is an example of allosteric modulation, a reversible process that helps regulate glycolysis by controlling enzyme activity in response to the levels of intermediates in the pathway.
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Inhibition of hexokinase by glucose-6-phosphate is an example ofa)Competitive and reversible processb)Allosteric modulationc)Competitive and irreversible processd)Non-competitive and irreversible processCorrect answer is option 'B'. Can you explain this answer?
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