Glutamyl aminopeptidase (EC 3.4.11.7, aminopeptidase A, aspartate aminopeptidase, angiotensinase A, glutamyl peptidase, Ca2+-activated glutamate aminopeptidase, membrane aminopeptidase II, antigen BP-1/6C3 of mouse B lymphocytes, L-aspartate aminopeptidase, angiotensinase A2) is an enzyme encoded by the ENPEP gene. Glutamyl aminopeptidase has also recently been designated CD249 (cluster of differentiation 249).
Glutamyl aminopeptidase is a zinc-dependent membrane-bound aminopeptidase that catalyzes the cleavage of glutamatic and aspartatic amino acid residues from the N-terminus of polypeptides. The enzyme degrades vasoconstricting angiotensin II into angiotensin III and therefore helps to regulate blood pressure.[1]
^Reaux A, Iturrioz X, Vazeux G, Fournie-Zaluski MC, David C, Roques BP, Corvol P, Llorens-Cortes C (2000). "Aminopeptidase A, which generates one of the main effector peptides of the brain renin-angiotensin system, angiotensin III, has a key role in central control of arterial blood pressure". Biochem. Soc. Trans. 28 (4): 435–40. doi:10.1042/0300-5127:0280435. PMID 10961935.
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extent, glutamylaminopeptidase (aminopeptidase A), as well as other aminopeptidases. It does not inhibit arginyl aminopeptidase (aminopeptidase B). Amastatin...
that is formed by removing an amino acid from angiotensin II by glutamylaminopeptidase A, which cleaves the N-terminal Asp residue. Activation of the...
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amino group not present in pyroglutamic acid. The enzyme pyroglutamate aminopeptidase can restore a free N-terminus by cleaving off the pyroglutamate residue...
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