Enkephalin Dipeptidyl Carboxypeptidase (EDP), also known as enkephalinase or neprilysin, is an enzyme that plays a critical role in the degradation and inactivation of endogenous opioid peptides, particularly enkephalins. It belongs to the class of metalloendopeptidases, specifically the family of zinc-dependent neuropeptidases.
Enkephalins are small peptides that act as natural painkillers and mood regulators within the central nervous system. However, their effects are transient, as they are rapidly hydrolyzed by EDP to inactive metabolites. EDP cleaves the peptide bond between two amino acids, specifically the carboxyl terminal of an enkephalin molecule, leading to the liberation of amino acids and the termination of enkephalin's biological activity.
The role of EDP is not limited to the degradation of enkephalins. It is also involved in the metabolism of a wide range of other neuropeptides, including substance P, neurotensin, bradykinin, and angiotensin I, among others. By controlling the levels of these bioactive peptides, EDP contributes to the regulation of pain perception, inflammation, blood pressure, and various neuronal functions.
Given its importance in the regulation of neuropeptide signaling, EDP and its inhibitors are of interest in pharmaceutical research, particularly in the development of therapeutics targeting chronic pain, neurodegenerative disorders, psychiatric diseases, and cardiovascular conditions.
