Applying the knowledge that proteolytic cleavage activates trypsin between the L

Question

Applying the knowledge that proteolytic cleavage activates trypsin between the Lysine and Isoleucine residues occurs, what does this allow of Trypsin once this cleavage occurs?

Introduces a rapid cascade of Trypsinogen molecules to produce even more Trypsin molecules.

To hault any additional amino acids from entering the oxyanion hole.

Introduces a rapid cascade of Trypsin molecules to produce even more Trypsinogen molecules

To allow additional amino acids to enter the oxyanion hole.

Introduces a rapid cascade of Trypsinogen molecules to produce even more Trypsin molecules.

To hault any additional amino acids from entering the oxyanion hole.

Introduces a rapid cascade of Trypsin molecules to produce even more Trypsinogen molecules

To allow additional amino acids to enter the oxyanion hole.

Explanation / Answer

a. Introduces a rapid cascade of Trypsinogen molecules to produce even more Trypsin molecules.

The process is called Autocatalysis where trypsin produced in cleavage of Lysine 15 -Isoleucine 16, participates in the cleavage of its own zymogen that is trypsinogen, and generates more trypsin.

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