| Official Name |
| Leishmanolysin.
|
| Alternative Name(s) |
| Glycoprotein gp63. |
| Promastigote surface endopeptidase. |
| Reaction catalysed |
| Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys- |
| Cofactor(s) |
| Calcium; Zinc.
|
| Comment(s) |
- A membrane-bound glycoprotein found on the promastigote of various
species of Leishmania protozoans.
- Contains consensus sequence for a zinc binding site; Z-Tyr-Leu-NHOH
is a strong inhibitor.
- The enzyme can activate its proenzyme by cleavage of the 100-
Val-|-Val-101 bond.
- An acidic pH optimum is found with certain protein substrates.
- Belongs to peptidase family M8.
|
| Cross-references |
| PROSITE | PDOC00129 |
| BRENDA | 3.4.24.36 |
| PUMA2 | 3.4.24.36 |
| PRIAM enzyme-specific profiles | 3.4.24.36 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.24.36 |
| IUBMB Enzyme Nomenclature | 3.4.24.36 |
| IntEnz | 3.4.24.36 |
| MEDLINE | Find literature relating to 3.4.24.36 |
| MetaCyc | 3.4.24.36 |
| UniProtKB/Swiss-Prot |
|