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Why does pepsinogen exist?
Inactive pepsinogen is converted to active pepsin by HCl. But why can't pepsin be secreted directly in its active state, i.e. why does pepsinogen have to exist?
The same question applies for rennin and prorennin?
1 Answer
- Merlin's FelineLv 71 decade agoFavorite Answer
proteolytic enzymes ( proteases ) exist in the inactive ( zymogen or pro form ) to keep the enzyme from digesting the proteins of the cell making /storing the enzyme. When the enzyme enters the stomach , with the lining protected by protease insensitive mucus..the enzyme can be activated to digest dietary proteins. Trypsin in produced in the pancreas in the inactive trypsinogen which is activated in the lumen of the small intestine by enteropeptidase ( then the active trypsin can activate more trypsinogen to trypsin).
Source(s): Ph.D. Biochem BS Chem
