Alanyl aminopeptidase, membrane (ANPEP)

Alanyl aminopeptidase, membrane (ANPEP), also known as aminopeptidase N (APN) or CD13, is a zinc-dependent metalloprotease located primarily on the brush border of small-intestinal and renal tubular epithelial cells, as well as on various other cell types including macrophages and granulocytes[1][2][5]. It catalyzes the removal of N-terminal amino acids from peptides, playing a critical role in terminal peptide digestion, hormone and neuropeptide processing, and immune response regulation. ANPEP also functions as a receptor for several viruses, including human coronavirus 229E, facilitating viral entry into the host cell[1][2][5]. Pathologically, ANPEP is implicated in cancer progression (e.g., angiogenesis, metastasis), hematologic malignancies, and certain infections, making it an established therapeutic and diagnostic target[2][1][5]. Its enzymatic activity and cell-surface expression have prompted the development of inhibitors such as bestatin for therapeutic applications, though safety concerns arise due to its physiological importance in peptide metabolism.

Other names

Aminopeptidase NAPNCD13PEPNAP-NhAPNAP-MLAP1gp150p150Aminopeptidase MMicrosomal aminopeptidaseMyeloid plasma membrane glycoprotein CD13

Inhibition of aminopeptidase activity (blocks peptide processing); Interference with viral entry (blocks virus-receptor interaction); Modulation of immune cell function