{PDOC00548} {PS00631; CYTOSOL_AP} {BEGIN} ************************************ * Cytosol 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. -Consensus pattern: [NS]-[TS]-D-A-E-G-R-[LVMI] [The D and the E are zinc/manganese ligands] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: These proteins belong to family M17 in the classification of peptidases [3,E1]. -Last update: April 2006 / Pattern revised. [ 1] Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K., Takahashi K. "Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase." Biochem. Biophys. Res. Commun. 178:1459-1464(1991). PubMed=1908238 [ 2] Burley S.K., David P.R., Sweet R.M., Taylor A., Lipscomb W.N. "Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin." J. Mol. Biol. 224:113-140(1992). PubMed=1548695 [ 3] Rawlings N.D., Barrett A.J. "Evolutionary families of metallopeptidases." Methods Enzymol. 248:183-228(1995). PubMed=7674922 [E1] https://www.uniprot.org/docs/peptidas -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}