Pepsin

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Pepsin
Image:1PSO.png 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 in 1836. It was the first animal enzyme to be discovered.

1 Precursor
2 See also
3 External links
4 References

[edit] Precursor

Pepsin are 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 will digest up to 20% of ingested proteins by cleaving preferentially at carboxylic groups 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.