Chymotrypsinogen

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Chymotrypsinogen

Chymotrypsinogen is a precursor enzyme, or zymogen, that is converted into the active enzyme chymotrypsin in the small intestine. This conversion is an essential step in the digestive system, facilitating the breakdown of proteins into smaller peptides and amino acids, which can then be absorbed by the body. Chymotrypsinogen is produced by the pancreas and secreted into the small intestine, where it undergoes activation.

Production and Activation[edit | edit source]

Chymotrypsinogen is synthesized in the acinar cells of the pancreas. The process of its activation begins when it is secreted into the small intestine. Here, it encounters another enzyme, enteropeptidase (also known as enteropeptidase), which is produced by the cells lining the intestine. Enteropeptidase catalyzes the conversion of chymotrypsinogen to chymotrypsin by cleaving a specific peptide bond within the chymotrypsinogen molecule. This initial cleavage activates the enzyme, which then autocatalytically accelerates the activation of other chymotrypsinogen molecules as well as its own further activation.

Function[edit | edit source]

Once activated, chymotrypsin is a potent proteolytic enzyme, meaning it breaks down proteins. It does this by cleaving peptide bonds, which are the links between amino acids in a protein, at specific points. Chymotrypsin prefers to cleave at peptide bonds adjacent to aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. This specificity allows chymotrypsin to play a crucial role in the digestive process, breaking down dietary proteins into smaller, more easily absorbed molecules.

Clinical Significance[edit | edit source]

The proper functioning of chymotrypsinogen and its conversion to chymotrypsin is vital for normal digestion. Disorders in the production or activation of chymotrypsinogen can lead to digestive problems and malabsorption of nutrients. Additionally, because of its role in protein digestion, chymotrypsin (and by extension, chymotrypsinogen) has been studied for its potential therapeutic applications, including its use in treating conditions that involve inflammation or dead tissue removal.

See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD