The enzyme phosphofructokinase catalyzes the conversion of fructose-6-phosphate and adenosine triphosphate (ATP) to fructose 1,6-bisphosphate and adenosine diphosphate (ADP). Adenosine monophosphate (AMP) activates the enzyme phosphofructokinase (PFK) by binding at a site distinct from the substrate-binding site. This is an example of:__________.

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04-03-2020
Biology

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The enzyme phosphofructokinase catalyzes the conversion of fructose-6-phosphate and adenosine triphosphate (ATP) to fructose 1,6-bisphosphate and adenosine diphosphate (ADP). Adenosine monophosphate (AMP) activates the enzyme phosphofructokinase (PFK) by binding at a site distinct from the substrate-binding site. This is an example of:__________.

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olatunbosunadeoke olatunbosunadeoke · Answer 1 · 2020-03-04T10:38:05+01:00

Answer: Allosteric activation

The enzyme phosphofructokinase catalyzes the conversion of fructose-6-phosphate and adenosine triphosphate (ATP) to fructose 1,6-bisphosphate and adenosine diphosphate (ADP). Adenosine monophosphate (AMP) activates the enzyme phosphofructokinase (PFK) by binding at a site distinct from the substrate-binding site. This is an example of allosteric activation.

Explanation:

The enzyme, phosphofructokinase is an allosteric enzyme since it possess more than one active site. The other active site is called an allosteric site.

Thus, since AMP binding at the allosteric site of PFK increases its affinity for its substrate (fructose-6-phosphate and ATP) conversion, then it is said to be an example of allosteric activation.