The Enzyme Database

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EC 3.4.11.2     
Accepted name: membrane alanyl aminopeptidase
Reaction: Release of an N-terminal amino acid, Xaa┼Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Other name(s): microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13
Comments: A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9054-63-1
References:
1.  Wachsmuth, D., Fritze, I. and Pfleiderer, G. An aminopeptidase occurring in pig kidney. I. An improved method of preparation. Physical and enzymatic properties. Biochemistry 5 (1966) 169–174. [PMID: 5938934]
2.  Kim, Y.S. and Brophy, E.J. Rat intestinal brush border membrane peptidases. I. Solubilization, purification of two different forms of enzyme. J. Biol. Chem. 251 (1976) 3199–3205. [PMID: 931983]
3.  Gray, G.M. and Santiago, N.A. Intestinal surface amino-oligopeptidases. I. Isolation of two weight isomers and their subunits from rat brush border. J. Biol. Chem. 252 (1977) 4922–4928. [PMID: 873921]
4.  Sjöström, H., Norén, O., Jeppesen, L., Staun, M., Svensson, B. and Christiansen, L. Purification of different amphiphilic forms of a microvillus aminopeptidase from pig small intestine using immunoadsorbent chromatography. Eur. J. Biochem. 88 (1978) 503–511. [PMID: 357150]
5.  Ferracci, H. and Maroux, S. Rabbit intestinal aminopeptidase N. Purification and molecular properties. Biochim. Biophys. Acta 599 (1980) 448–463. [PMID: 6105876]
[EC 3.4.11.2 created 1961 as EC 3.4.1.2, transferred 1972 to EC 3.4.11.2 (EC 3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC 3.4.13.6, incorporated 1997)]
 
 


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