The Enzyme Database

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EC 3.4.11.9     
Accepted name: Xaa-Pro aminopeptidase
Reaction: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
Other name(s): proline aminopeptidase; aminopeptidase P; aminoacylproline aminopeptidase; X-Pro aminopeptidase
Comments: A Mn2+-dependent, generally membrane-bound enzyme present in both mammalian and bacterial cells. In peptidase family M24 (methionyl aminopeptidase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37288-66-7
References:
1.  Yaron, A. and Mlynar, D. Aminopeptidase-P. Biochem. Biophys. Res. Commun. 32 (1968) 658–663. [PMID: 4878817]
2.  Yaron, A. and Berger, A. Aminopeptidase-P. Methods Enzymol. 19 (1970) 522–534.
3.  Fleminger, G., Carmel, A. and Yaron, A. Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung. Eur. J. Biochem. 125 (1982) 609–615. [PMID: 6749499]
4.  Orawski, A.T., Susz, J.P. and Simmons, W.H. Aminopeptidase-P from bovine lung - solubilization, properties, potential role in bradykinin degradation. Mol. Cell. Biochem. 75 (1987) 123–132. [PMID: 3627107]
5.  Hooper, N.M., Hryszko, J. and Turner, A.J. Purification and characterization of pig kidney aminopeptidase P. Biochem. J. 267 (1990) 509–515. [PMID: 2139778]
[EC 3.4.11.9 created 1972]
 
 


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