How Does Pepsinogen Become Active?

Pepsinogen is a proenzyme secreted by chief cells

chief cells
Cell types

The gastric chief cell (also known as a zymogenic cell or peptic cell) is a cell in the stomach that releases pepsinogen and chymosin. Pepsinogen is activated into the digestive enzyme pepsin when it comes in contact with hydrochloric acid produced by gastric parietal cells.

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. It is converted into active form i.e pepsin by HCl. ... Once pepsin is formed it itself converts pepsinogen into pepsin. This proces is called autocatalysis.

How does pepsinogen change into its active form?

Complete answer:

Pepsinogen is a digestive enzyme that helps within the digestion of proteins. The hydrochloric acid secreted in the stomach provides the optimum pH, which activates the pepsinogen enzyme required to digest proteins. Enzyme pepsinogen is converted to pepsin, which converts the proteins into amino acids.

How is inactive pepsinogen converted to active pepsin?

Answer: Inactive pepsinogen is converted into active pepsin by Hydrochloric acid.

Robert Thorne

Robert Thorne

Automotive & Future Transportation Editor

Robert Thorne covers electric vehicle innovations, autonomous driving systems, global mobility trends, and automotive engineering developments.