Abstract
Summary Glutamyl aminopeptidase (aminopeptidase A, EC 3.4.11.7) was first described in 1961 as a calcium-stimulated aminopeptidase with specificity for N-terminal acidic amino acids. The enzyme was subsequently purified and characterized as a membrane-bound ectoenzyme particularly abundant in the brush border fractions of kidney and intestine. Early interest in this enzyme was stimulated by its conversion of angiotensin II to des-aspartyl angiotensin II (angiotensin III). More recently, glutamyl 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.
Published Version
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