Membrane alanyl aminopeptidase

This chapter focuses on the structural chemistry of membrane alanyl aminopeptidase (mAAP). The early history of mAAP relates to its role as Cys-Gly dipeptidase or cysteinyl-glycinase. It was proposed that this peptidase activity present in apparently purified RNA preparations contributed to polypeptide biosynthesis by acting in reverse in a sequential fashion. mAAP has a broad substrate specificity removing N-terminal amino acids (Xaa-Xbb-) from almost all unsubstituted oligopeptides and from an amide or arylamide. mAAP is a type II integral membrane protein located on the plasma membrane as an ectoenzyme. The pI is approximately 5. mAAP is widely distributed among species and tissues although it is of greatest abundance in brush border membranes of the kidney, in the mucosal cells of the small intestine and in the liver. It is also present in the lung where it is identical to the pI46 type II alveolar epithelial cell antigen and is located on endothelial cells in blood vessels. On polarized epithelial cells, mAAP is localized to the apical domain and is targeted there through an apical sorting signal thought to be located in the catalytic head group region of the protein.