Glutamyl aminopeptidase (aminopeptidase A, EC 3.4.11.7) was first desc
ribed in 1961 as a calcium-stimulated aminopeptidase with specificity
for N-terminal acidic amino acids. The enzyme was subsequently purifie
d and characterized as a membrane-bound ectoenzyme particularly abunda
nt in the brush border fractions of kidney and intestine. Early intere
st in this enzyme was stimulated by its conversion of angiotensin II t
o des-aspartyl angiotensin II (angiotensin III). More recently, glutam
yl aminopeptidase has been identified as a pre-B cell differentiation
antigen BP-1/6C3. This review focuses on the biochemical properties of
this enzyme and its role in the immune and non-immune systems.