endopeptidázokkal

Endopeptidases are a class of enzymes that catalyze the hydrolysis of peptide bonds within a protein molecule. Unlike exopeptidases, which cleave amino acids from the ends of a polypeptide chain, endopeptidases act on internal peptide bonds. This action can lead to the fragmentation of larger proteins into smaller peptides or individual amino acids.

These enzymes are crucial for a wide variety of biological processes. In digestion, for example, endopeptidases secreted in the stomach and small intestine break down dietary proteins into smaller peptides that can be further processed by exopeptidases and absorbed. In cellular metabolism, endopeptidases play roles in protein turnover, the activation and inactivation of proteins, and the processing of precursor proteins into their active forms.

The specificity of endopeptidases varies, with some cleaving at particular amino acid sequences, while others are less specific. This specificity is determined by the enzyme's active site, which is structured to bind to and interact with specific amino acid residues in the substrate protein.

Common examples of endopeptidases include trypsin and chymotrypsin in the digestive system, and caspases involved in programmed cell death (apoptosis). Their activity is tightly regulated to ensure proper protein processing and prevent uncontrolled degradation. Aberrant endopeptidase activity has been implicated in various diseases, including cancer and inflammatory conditions.