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Pepsin
Pepsin in complex with pepstatin
Other names:	Pepsinogen
Genetic data
Gene code:	8885 (HGNCid)
Protein Structure/Function
Protein type:	protease
Functions:	digestion
Other
Molecular interactions:	pepstatin
Database Links
EC number:	3.4.23.1

Pepsin is a digestive protease (EC 3.4.23.1) released by the chief cells in the stomach that functions to degrade food proteins into peptides.

According to American Heritage Dictionary, pepsin derives from the Greek word pepsis, meaning digestion (peptein: to digest).

Pepsin was discovered by Theodor Schwann^[1] in 1836. It was the first animal enzyme to be discovered.

Pepsin is expressed as a pro-form zymogen, pepsinogen, whose primary structure has an additional 44 amino acids.

In the stomach, chief cells release pepsinogen. This zymogen is activated by hydrochloric acid (HCl), which is released from parietal cells in the stomach lining. The hormone gastrin and the vagus nerve trigger the release of both pepsinogen and HCl from the stomach lining when food is ingested. HCl creates an acidic environment which allows pepsinogen to unfold and cleave itself in an autocatalytic fashion, thereby generating pepsin (the active form). Pepsin cleaves the 44 amino acids from pepsinogen to create more pepsin. Pepsin will digest up to 20% of ingested carbon bonds by cleaving preferentially after the N-terminal of aromatic amino acids such as phenylalanine and tyrosine. It will not cleave at bonds containing valine, alanine or glycine. Peptides may be further digested by other proteases (in the duodenum) and eventually absorbed by the body.

Pepsin is stored as pepsinogen so it will only be released when needed, and does not digest the body's own proteins in the stomach's lining.

Pepsin functions best in acidic environments, particularly those in a pH of 3.

Other important digestive proteases are the pancreatic enzymes trypsin and chymotrypsin. Pepsin denatures if the pH is more than 5.0. Pepsin is potently inhibited by the peptide inhibitor pepstatin.

Pepsins should be stored at very cold temperatures (between −20°C and −80°C) to prevent autolysis (self-cleavage). Autolysis may also be prevented by storage of pepsins at pH 11 or by using pepsins modified by e.g. reductive methylation. When the pH is adjusted back to pH 6 activity returns.

• Pepsin A description from BRENDA database
• MeSH Pepsin+A
• MeSH Pepsinogens
• MeSH Pepsinogen+A
• MeSH Pepsinogen+C

1. ^ Florkin M (1957). "Discovery of pepsin by Theodor Schwann.". Rev Med Liege 12 (5): 139-44. PMID 13432398.