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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.
Zymogen Granule Protein 16 is a protein that is encoded by the ZG16 gene.Other common names include hZG16, FLJ43571, FLJ92276, secretory lectin ZG16, jacalin-like lectin domain containing, JCLN, JCLN1, MGC183567, MGC34820, ZG16A, zymogen granule membrane protein 16, zymogen granule protein 16 homolog, and zymogen granule protein.
It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. Release of the granules from the cell is stimulated by either a hormonal signal or a nerve impulse, and the granules spill into a duct leading into the duodenum .
Duodenal glands are situated within the mucosa and submucosa of the duodenum. They are most abundant near the pylorus, growing shorter and more sparse distally towards the terminal portion of the duodenum. [1] The duodenum can be distinguished from the jejunum and ileum by the presence of Brunner's glands in the submucosa. [citation needed]
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 ...
Enteropeptidase is a type II transmembrane serine protease (TTSP) localized to the brush border of the duodenal and jejunal mucosa and synthesized as a zymogen, proenteropeptidase, which requires activation by duodenase or trypsin. [9] TTSPs are synthesized as single chain zymogens with N-terminal propeptide sequences of different lengths.
After processing to proelastase, it is stored in the zymogen granules and then activated to elastase in the duodenum by the tryptic cleavage of a peptide bond in the inactive form of the precursor molecule. [8] This process results in the removal of an activation peptide from the N-terminal, that enables the enzyme to adopt its native conformation.
The following are enzymes produced by the stomach and their respective function: Pepsin is the main gastric enzyme. 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.