Exopeptidase

Exopeptidase is an enzyme that acts on the terminal bonds of peptide chains and catalyzes the removal of amino acids from the N- and C-terminus of polypeptide chains. This enzyme plays an important role in the process of protein digestion in the small intestine, as it helps break down proteins into smaller peptides that are more easily absorbed by the body.

Exopeptidases are part of the group of hydrolases and act on the terminal bonds of peptides, which allows them to cleave amino acid residues from the N or C end of the polypeptide chain. They play an important role in protein digestion as they help break down large protein molecules into smaller pieces that can be more easily absorbed by the body.

There are several types of exopeptidases, which differ in their activity and specificity. Some of them can act only on the terminal residues of amino acid chains, while others can act on any terminal bonds.

In addition, exopeptidases can be used as therapeutic agents to treat various diseases associated with protein metabolism disorders. For example, some exopeptidases are used to treat Alzheimer's disease because they can help break down beta-amyloid proteins that accumulate in the brain in this disease.

In general, exopeptidases play an important role in protein metabolism and may be useful in the treatment of various diseases associated with disorders of protein metabolism.

Exopeptidases

**Exopeptidases** are cellular metalloproteins (enzymes consisting of protein and non-protein parts) or carbohydrates that catalyze the cleavage of “short-lived” peptide bonds (amino acids) in polymer molecules (for example, proteins, polysaccharides, glycoproteins, glycolipids). These include more than two thousand different chemical compounds