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Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
Protein catabolism often begins with pepsin, which converts proteins into polypeptides. These polypeptides are then further degraded. In humans, the pancreatic proteases include trypsin, chymotrypsin, and other enzymes. In the intestine, the small peptides are broken down into amino acids that can be absorbed into the bloodstream.
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.
A peptide hormone, gastrin, produced by G cells in the gastric glands, stimulates the production of gastric juice which activates the digestive enzymes. Pepsinogen is a precursor enzyme produced by the gastric chief cells, and gastric acid activates this to the enzyme pepsin which begins the digestion of proteins. As these two chemicals would ...
The parietal cell releases bicarbonate into the bloodstream in the process, which causes a temporary rise of pH in the blood, known as an alkaline tide. The gastric juice also contains digestive enzymes produced by other cells in the gastric glands – gastric chief cells. Gastric chief cells secrete an inactivated pepsinogen.
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and functions outside that cell. Exoenzymes are produced by both prokaryotic and eukaryotic cells and have been shown to be a crucial component of many biological processes. Most often these enzymes are involved in the breakdown of larger macromolecules.
Erepsin is a mixture of enzymes contained in a protein fraction found in the intestinal juices that digest peptones into amino acids. It is produced and secreted by the intestinal glands in the ileum and the pancreas, but it is also found widely in other cells. However, the term now rarely used in scientific literature as more precise terms are ...