Alpha-chymotrypsin
Alpha-chymotrypsin is a type of protease enzyme that is secreted by the pancreas and aids in the digestion of proteins. It is a member of the serine protease family, which is characterized by a catalytic triad of serine, histidine, and aspartate residues.
Structure[edit | edit source]
Alpha-chymotrypsin is a globular protein composed of 245 amino acids. It is formed from a single polypeptide chain that is folded into a compact shape. The molecule has three disulfide bridges and a single free cysteine residue. The active site of the enzyme, where the catalytic triad is located, is found in a deep pocket on the surface of the molecule.
Function[edit | edit source]
The primary function of alpha-chymotrypsin is to break down proteins into smaller peptides during digestion. It does this by cleaving peptide bonds, specifically those on the carboxyl side of large hydrophobic amino acids such as tryptophan, tyrosine, and phenylalanine. This process is essential for the absorption of dietary proteins.
Clinical significance[edit | edit source]
Alpha-chymotrypsin has been used in various medical applications. It is used in ophthalmic surgery to facilitate the removal of the lens in cataract surgery. It has also been used in the treatment of chronic pancreatitis and other conditions that result from the insufficient production of digestive enzymes by the pancreas.
See also[edit | edit source]
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