Exopeptidase

Exopeptidases are a broad functional class of proteolytic enzymes that catalyze the hydrolysis of peptide bonds specifically at the terminal ends of polypeptide chains. They are sub-classified into aminopeptidases, which release single amino acids or small peptides from the N-terminus, and carboxypeptidases, which act on the C-terminus. These enzymes play essential roles in biological processes such as the final digestion of dietary proteins, the processing of antigens for immune recognition, and the regulation of vital peptide hormones including angiotensin II and glucagon-like peptide 1 (GLP-1). In clinical practice, exopeptidases are among the most validated therapeutic targets; for instance, the inhibition of Angiotensin-Converting Enzyme (ACE) is a cornerstone of hypertension treatment, while Dipeptidyl Peptidase-4 (DPP-4) inhibitors are widely used to manage type 2 diabetes. Because the term "Exopeptidase" encompasses a large and diverse family of enzymes with varying substrate specificities and tissue distributions, it is generally considered a classification rather than a single specific drug target.

Other names

ExoproteaseTerminal peptidaseExopeptidase class

Exopeptidase inhibitors act by binding to and blocking the catalytic active site of terminal peptidases, preventing the hydrolysis of peptide bonds at the amino (N-) or carboxyl (C-) ends of a substrate, which modulates the half-life and activity of bioactive peptides.