PROSITE documentation PDOC00548Cytosol aminopeptidase signature
Cytosol aminopeptidase is a eukaryotic cytosolic zinc-dependent exopeptidase that catalyzes the removal of unsubstituted amino-acid residues from the N-terminus of proteins. This enzyme is often known as leucine aminopeptidase (EC 3.4.11.1) (LAP) but has been shown [1] to be identical with prolyl aminopeptidase (EC 3.4.11.5). Cytosol aminopeptidase is a hexamer of identical chains, each of which binds two zinc ions.
Cytosol aminopeptidase is highly similar to Escherichia coli pepA, a manganese dependent aminopeptidase. Residues involved in zinc ion-binding [2] in the mammalian enzyme are absolutely conserved in pepA where they presumably bind manganese. Most bacterial species contain a pepA-type enzyme.
As a signature pattern for these enzymes, we selected a perfectly conserved octapeptide which contains two residues involved in binding metal ions: an aspartate and a glutamate.
Note:These proteins belong to family M17 in the classification of peptidases [3,E1].
Last update:April 2006 / Pattern revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Matsushima M. Takahashi T. Ichinose M. Miki K. Kurokawa K. Takahashi K. |
| Title | Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. | |
| Source | Biochem. Biophys. Res. Commun. 178:1459-1464(1991). | |
| PubMed ID | 1908238 |
| 2 | Authors | Burley S.K. David P.R. Sweet R.M. Taylor A. Lipscomb W.N. |
| Title | Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. | |
| Source | J. Mol. Biol. 224:113-140(1992). | |
| PubMed ID | 1548695 |
| 3 | 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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