ExplorEnz: EC 3.4.11.7

Your query returned 1 entry. Printable version

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]