**WHY PROTEOLYTIC ENZYMES RELEASED IN ZYMOGEN FORM??**

  * Several proteolytic enzymes found in the blood or in the digestive tract are present in an inactive (precursor) form, called zymogen or proenzymes.
  * For example, chymotrypsin is secreted by the pancreas as chymotrypsinogen. It is activated in the digestive tract by the proteolytic enzyme trypsin.
  * Zymogens are also associated with blood clotting, formation of insulin, formation of collagen and apoptosis.
  * Pepsinogen, trypsinogen, chymotrypsinogen and procarboxypeptidases are some examples of proteolytic zymogens
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  * Proteolytic enzymes are released in zymogen form to prevent them from prematurely digesting proteins within the cells where they are synthesized.
  * This helps to avoid damage to cellular structures and ensures that digestion only occurs where and when it’s needed.
  * This inactive form acts as a safety mechanism until the enzyme reaches its target site, where it’s activated by specific cleavage events.
  *  Process of cleavage : Activation of zymogen usually occurs through cleavage of a specific peptide bond, triggered by other enzymes
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