| IED ID | IndEnz0002005757 |
| Enzyme Type ID | protease005757 |
| Protein Name |
Leishmanolysin EC 3.4.24.36 Cell surface protease Major surface glycoprotein Major surface protease Promastigote surface endopeptidase Protein gp63 |
| Gene Name | gp63 |
| Organism | Leishmania donovani |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Leishmaniinae Leishmania Leishmania Leishmania donovani species complex Leishmania donovani |
| Enzyme Sequence | MSVDSSSTHRHRSVAARLVRLAAAGAAVIAAVGTAAAWAHAGAVQHRCIHDAMQARVRQSVARHHTAPGAVSAVGLSYVTLGAAPTVVRAANWGALRIAVSTEDLTDSAYHCARVGQRISTRDGRFAICTAEDILTDEKRDILVKYLIPQALQLHTERLKVRQVQDKWKVTGMGNEICGHFKVPPAHITDGLSNTDFVMYVASVPSEGDVLAWATTCQVFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSVVFFRDARILESISNVRHKDFDVPVINSSTAVAKAREQYGCGTLEYLEMEDQGGAGSAGSHIKMRNAQDELMAPASDAGYYSALTMAIFQDLGFYQADFSKAEEMPWGRNAGCAFLSEKCMEDGITKWPAMFCNENEVTMRCHTGRLSLGVCGLSSSDIPLPPYWQYFTDPLLAGISAFMDYCPVVVPFGDGSCAQRASEAGAPFKGFNVFSDAARCIDGAFRPKTTETVTNSYAGLCANVRCDTATRTYSVQVHGGSGYANCTPGLRVELSTVSSAFEEGGYITCPPYVEVCQGNVQAAKDGGNAAAGRRGPRAAATALLVAALLAVAL |
| Enzyme Length | 590 |
| Uniprot Accession Number | P23223 |
| Absorption | |
| Active Site | ACT_SITE 252; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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-.; EC=3.4.24.36; |
| DNA Binding | |
| EC Number | 3.4.24.36 |
| Enzyme Function | FUNCTION: Has an integral role during the infection of macrophages in the mammalian host. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (9); Glycosylation (1); Lipidation (1); Metal binding (3); Propeptide (2); Signal peptide (1) |
| Keywords | Cell adhesion;Cell membrane;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 62,950 |
| Kinetics | |
| Metal Binding | METAL 251; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 255; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 321; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.36; |