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In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
Pepsin is expressed as a zymogen called pepsinogen, whose primary structure has an additional 44 amino acids compared to the active enzyme. In the stomach, gastric chief cells release pepsinogen. This zymogen is activated by hydrochloric acid (HCl), which is released from parietal cells in the stomach lining.
Chief cells release the zymogen (enzyme precursor) pepsinogen when stimulated by a variety of factors including cholinergic activity from the vagus nerve and acidic condition in the stomach. Gastrin and secretin may also act as secretagogues. [4]
Chief cells (zymogen cells/peptic cells) – They are found in the basal regions of the gland and release proenzymes or zymogens – pepsinogen (precursor to pepsin), and prorennin (precursor to rennin or chymosin). [10] Prorennin is secreted in young mammals (childhood stage). It is not secreted in adult mammals.
It is produced in the stomach by gastric chief cells in its inactive form pepsinogen, which is a zymogen. Pepsinogen is then activated by the stomach acid into its active form, pepsin. Pepsin breaks down the protein in the food into smaller particles, such as peptide fragments and amino acids.
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Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the ...
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