Glutamyl Aminopeptidase[edit | edit source]

Glutamyl aminopeptidase, also known as aminopeptidase A (APA), is an enzyme that plays a crucial role in the metabolism of peptides by catalyzing the cleavage of N-terminal glutamyl residues from peptide substrates. This enzyme is a member of the M1 family of metallopeptidases and is encoded by the ENPEP gene in humans.

Structure[edit | edit source]

Glutamyl aminopeptidase is a type II membrane-bound glycoprotein. It consists of a short N-terminal cytoplasmic domain, a single transmembrane domain, and a large extracellular domain that contains the active site. The enzyme requires zinc as a cofactor for its catalytic activity, which is characteristic of metallopeptidases.

Function[edit | edit source]

The primary function of glutamyl aminopeptidase is to regulate the activity of peptide hormones and neuropeptides by removing glutamyl residues from their N-terminus. This activity is important in the renin-angiotensin system, where it converts angiotensin II to angiotensin III, thereby modulating blood pressure and electrolyte balance.

Clinical Significance[edit | edit source]

Glutamyl aminopeptidase has been implicated in various physiological and pathological processes. Its role in the renin-angiotensin system makes it a potential target for the treatment of hypertension and heart failure. Additionally, altered expression of this enzyme has been observed in certain types of cancer, suggesting a role in tumor progression and metastasis.

Research and Therapeutic Potential[edit | edit source]

Research into glutamyl aminopeptidase is ongoing, with studies focusing on its potential as a therapeutic target. Inhibitors of this enzyme are being investigated for their ability to modulate blood pressure and for their potential anti-cancer properties.