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[edit | edit source]
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[edit | edit source]
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[edit | edit source]
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[edit | edit source]
References[edit | edit source]
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