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A small peptide bound to a sugar molecule can bind to an allosteric site on an enzyme stimulating its activity. This enzyme is a protein kinase (meaning that it can phosphorylate proteins) that activates sugar hydrolase enzymes (meaning that they hydrolyze sugars).

As more hydrolase enzymes are activated, they will eventually hydrolyze the sugar attached to the peptide, preventing the peptide from binding to the allosteric site of the kinase and inhibiting the enzyme.

Of the answers below, select the BEST answer to the question, "What this process is called?" (among Choices 'A' through 'C') and the BEST answer to "Why this is useful to the cell?" (among Choices 'D' through 'F').

Select ALL that apply.


Allosteric modulation.


Feedback inhibition.


Covalent active site modification.


This process allows the cell to only activate as many hydrolases as needed and prevents too many sugars from being hydrolyzed.


This process ensures that the kinases will remain active.


This process will affect the production of the small peptide.

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