Trypsin 1

Trypsin 1 is a type of enzyme that is produced in the pancreas and plays a crucial role in the digestion of proteins in the small intestine. It is part of the serine protease family and is encoded by the PRSS1 gene in humans.

Structure

Trypsin 1 is a single chain polypeptide composed of 223 amino acids. It has a molecular weight of approximately 24,000 Daltons. The structure of trypsin 1 is characterized by its deep active site pocket, which is responsible for its specific substrate recognition and catalytic activity.

Function

The primary function of trypsin 1 is to break down proteins in the small intestine. It does this by cleaving peptide bonds, the links between amino acids in a protein. Specifically, trypsin 1 targets the peptide bonds following the amino acid residues lysine and arginine. This process is essential for the absorption of proteins in the diet.

Clinical significance

Mutations in the PRSS1 gene that encodes trypsin 1 can lead to conditions such as hereditary pancreatitis and pancreatic cancer. These conditions are often characterized by the premature activation of trypsin 1 within the pancreas, leading to autodigestion and inflammation of the organ.

See also

• Trypsin 2
• Trypsinogen
• Protease
• Digestive enzyme

References

   This article is a medical stub. You can help WikiMD by expanding it!