PROSITE documentation PDOC00417Aminopeptidase P and proline dipeptidase signature
Aminopeptidase P (EC 3.4.11.9) is the enzyme responsible for the release of any N-terminal amino acid adjacent to a proline residue. Proline dipeptidase (EC 3.4.13.9) (prolidase) splits dipeptides with a prolyl residue in the carboxyl terminal position.
Bacterial aminopeptidase P II (gene pepP) [1], proline dipeptidase (gene pepQ) [2], and human proline dipeptidase (gene PEPD) [3] are evolutionary related. These proteins are manganese metalloenzymes.
Yeast hypothetical proteins YER078c and YFR006w and Mycobacterium tuberculosis. hypothetical protein MtCY49.29c also belong to this family.
As a signature pattern for these enzymes we selected a conserved region that contains three histidine residues.
Note:These proteins belong to family M24B in the classification of peptidases [4,E1].
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Yoshimoto T. Tone H. Honda T. Osatomi K. Kobayashi R. Tsuru D. |
| Title | Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101. | |
| Source | J. Biochem. 105:412-416(1989). | |
| PubMed ID | 2659585 |
| 2 | Authors | Nakahigashi K. Inokuchi H. |
| Title | Nucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli. | |
| Source | Nucleic Acids Res. 18:6439-6439(1990). | |
| PubMed ID | 2243799 |
| 3 | Authors | Endo F. Tanoue A. Nakai H. Hata A. Indo Y. Titani K. Matsuda I. |
| Title | Primary structure and gene localization of human prolidase. | |
| Source | J. Biol. Chem. 264:4476-4481(1989). | |
| PubMed ID | 2925654 |
| 4 | Authors | Rawlings N.D. Barrett A.J. |
| Title | Evolutionary families of metallopeptidases. | |
| Source | Methods Enzymol. 248:183-228(1995). | |
| PubMed ID | 7674922 |
| E1 | Title | https://www.uniprot.org/docs/peptidas |
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