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Chapter 15: Problem 2

Why do you suppose proteolytic enzymes are often synthesized as inactive zymogens?

Short Answer

Expert verified
Proteolytic enzymes are often synthesized as inactive zymogens to prevent them from digesting the cells and tissues in which they are produced. This protects the cell from autodigestion or self-digestion, ensuring that the enzymes only function in suitable areas where protein digestion is needed, such as in the digestive tract.

Step by step solution

01

Understanding Proteolytic Enzymes

Proteolytic enzymes are a type of enzyme that break down proteins into their smaller components, which are primarily peptides and amino acids. These enzymes execute proteolysis, which involves the cleaving or hydrolysis of peptide bonds that link amino acids together in polypeptide chains.
02

Understanding Zymogens

Zymogens are inactive precursors to enzymes. They must undergo a change in their structural conformation in order to become active. This change is commonly triggered by the cleavage of specific peptide bonds in the zymogen molecule, which typically reveals the enzyme's active site.
03

Reason for Synthesis of Inactive Zymogens

Proteolytic enzymes are often synthesized as inactive zymogens to prevent them from digesting the cells and tissues that produce them. If these enzymes were synthesized in their active form, they would begin breaking down the proteins within the cells as soon as they were produced. By producing them as inactive zymogens, the cells are able to prevent this from happening. The enzymes remain inactive until they are secreted into the digestive tract, where they are then activated to carry out their function.

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Most popular questions from this chapter

Allosteric enzymes that sit at branch points leading to several essental products sometimes display negative cooperativity for feedback inhibition (allosteric inhibition) by one of the products. What might be the advantage of negative cooperativity instead of positive cooperativity in feedback inhibitor binding by such enzymes?

If no precautions are taken, blood that has been stored for some time becomes depleted in \(2,3-\mathrm{BPG}\). What happens if such blood is used in a transfusion?

Under appropriate conditions, nitric oxide (NO ') combines with Cys \(93 \beta\) in hemoglobin and influences its interaction with \(\mathrm{O}_{2} .\) Is this interaction an example of allosteric regulation or covalent modification?

Cholera toxin is an enzyme that covalently modifies the \(G_{\alpha}\) -subunit of G proteins. (Cholera toxin catalyzes the transfer of ADP-ribose from NAD \(^{+}\) to an arginine residue in \(G_{\alpha},\) an ADP-ribosylation reaction.) Covalent modification of \(\mathrm{G}_{\alpha}\) inactivates its GTPase activity. Predict the consequences of cholera toxin on cellular cAMP and glycogen levels.

What are the relative advantages (and disadvantages) of allosteric regulation versus covalent modification?
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