EC Number   |
General Information |
Reference |
|---|
   3.4.11.1 | evolution |
leucine aminopeptidases (LAPs) are members of the aminopeptidase M1/M17 family |
753402 |
| 3.4.11.1 | evolution |
phylogenetic analysis reveals that AcLAP clusters into a clade closely related with LAPs from Amoebozoa, including Dictyostelium sp.. The enzyme contains the highly conserved M17 aminopeptidase family signature sequence (NTDAEGRL, residues 425-432) and highly conserved amino acid residues for metal binding (D350, D368, D427, E429) and catalytic site formation (K357, R431). The enzyme belongs to the M17 family of proteases |
755091 |
| 3.4.11.1 | evolution |
the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases |
752649 |
| 3.4.11.1 | evolution |
the enzyme belongs to the M17 family of proteases |
-, 753519, 755209 |
| 3.4.11.1 | evolution |
the enzyme belongs to the M17 peptidase family |
753913 |
| 3.4.11.1 | evolution |
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases |
754807 |
| 3.4.11.1 | evolution |
the leucine aminopeptidases (LAPs) are members of the M17 family of Zn metalloproteases |
754671 |
| 3.4.11.1 | evolution |
the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases |
-, 753366 |
| 3.4.11.1 | malfunction |
bestatin and knockdown of LAP3 upregulate phosphorylation of Hsp27 and downregulate expression of fascin. Phosphorylation of Akt and expression of matrix metalloproteinase-2/9 can also be downregulated. LAP3 overexpression showed the opposite results |
754242 |
| 3.4.11.1 | malfunction |
disruption of the LAP-A hexameric structure increases chaperone activity |
732053 |
