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nmdcat.online July 11, 2026

The conversion of an inactive zymogen like trypsinogen into the active enzyme trypsin involves

A. The reversible binding of a coenzyme to the zymogen protein
B. A conformational change induced by the binding of an allosteric activator
C. Specific and limited proteolytic cleavage of peptide bonds
✓
D. The phosphorylation of a key serine residue in the active site

📝 Explanation

Activation of zymogens requires specific, irreversible proteolytic cleavage to remove a blocking peptide, allowing the protein to fold into its active conformation.

📖 Additional Information

  • The reversible binding of a coenzyme to the zymogen protein
  • A conformational change induced by the binding of an allosteric activator
  • Specific and limited proteolytic cleavage of peptide bonds
  • The phosphorylation of a key serine residue in the active site

Activation of zymogens requires specific, irreversible proteolytic cleavage to remove a blocking peptide, allowing the protein to fold into its active conformation.

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