| 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, Gene, 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. [DOI] [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. [DOI] [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] |
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| [EC 3.4.11.9 created 1972] |
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