endoproteaser
Endoproteases are a class of proteolytic enzymes that cleave peptide bonds within polypeptide chains, as opposed to exoproteases, which act at the ends of the chain. These enzymes play critical roles in various biological processes, including protein degradation, signal transduction, and the regulation of metabolic pathways. Endoproteases are categorized based on their catalytic mechanisms and specificities, with the most well-known types including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.
Serine proteases, such as trypsin and chymotrypsin, utilize a serine residue at their active site to hydrolyze
Aspartic proteases, such as pepsin and renin, utilize two aspartic acid residues to facilitate hydrolysis. These
Endoproteases are widely distributed in living organisms, from bacteria to humans, and are often involved in