| IED ID | IndEnz0002005709 |
| Enzyme Type ID | protease005709 |
| 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 major |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Leishmaniinae Leishmania Leishmania Leishmania major species complex Leishmania major |
| Enzyme Sequence | MSVDSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCVHDAMQARVRQSVADHHKAPGAVSAVGLPYVTLDAAHTAAAADPRPGSARSVVRDVNWGALRIAVSTEDLTDPAYHCARVGQHVKDHAGAIVTCTAEDILTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGDICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVANVPNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYLEVEDQGGAGSAGSHIKMRNAQDELMAPAAAAGYYTALTMAIFQDLGFYQADFSKAEVMPWGQNAGCAFLTNKCMEQSVTQWPAMFCNESEDAIRCPTSRLSLGACGVTRHPGLPPYWQYFTDPSLAGVSAFMDYCPVVVPYSDGSCTQRASEAHASLLPFNVFSDAARCIDGAFRPKATDGIVKSYAGLCANVQCDTATRTYSVQVHGSNDYTNCTPGLRVELSTVSNAFEGGGYITCPPYVEVCQGNVQAAKDGGNTAAGRRGPRAAATALLVAALLAVAL |
| Enzyme Length | 602 |
| Uniprot Accession Number | P08148 |
| Absorption | |
| Active Site | ACT_SITE 265; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094" |
| 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); Beta strand (26); Chain (1); Disulfide bond (9); Glycosylation (3); Helix (20); Lipidation (1); Metal binding (3); Mutagenesis (8); Propeptide (2); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Cell adhesion;Cell membrane;Direct protein sequencing;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 | PTM: The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0). |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1LML; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 63,953 |
| Kinetics | |
| Metal Binding | METAL 264; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094"; METAL 268; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094"; METAL 334; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9739094" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.36; |