The Enzyme Database

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EC 3.4.11.7     
Accepted name: glutamyl aminopeptidase
Reaction: Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
Other name(s): 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
Comments: Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family)
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-83-3
References:
1.  Glenner, G.G., McMillan, P.J. and Folk, J.E. A mammalian peptidase specific for the hydrolysis of N-terminal α-L-glutamyl and aspartyl residues. Nature 194 (1962) 867. [PMID: 13899213]
2.  Chulkova, T.M. and Orekhovich, V.N. Isolation and properties of aminopeptidase A from bovine kidneys. Biokhimiya 43 (1978) 964–969. [PMID: 508862]
3.  Danielsen, E.M., Norén, O., Sjöström, H., Ingram, J. and Kenny, J. Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Biochem. J. 189 (1980) 591–603. [PMID: 7011318]
4.  Tobe, H., Kojima, F., Aoyagi, T. and Umezawa, H. Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney. Biochim. Biophys. Acta 613 (1980) 459–468. [DOI] [PMID: 7448199]
5.  Wu, Q., Lahti, J.M., Air, G.M., Burrows, P.D. and Cooper, M.D. Molecular cloning of the murine BP-1/6C3 antigen: a member of the zinc-dependent metallopeptidase family. Proc. Natl. Acad. Sci. USA 87 (1990) 993–997. [DOI] [PMID: 1689065]
[EC 3.4.11.7 created 1972]
 
 


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