IED ID | IndEnz0002019090 |
Enzyme Type ID | protease019090 |
Protein Name |
Cathepsin L2 EC 3.4.22.15 Fragment |
Gene Name | |
Organism | Fasciola hepatica (Liver fluke) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Platyhelminthes Trematoda Digenea (flukes) Plagiorchiida Echinostomata Echinostomatoidea Fasciolidae Fasciola Fasciola hepatica (Liver fluke) |
Enzyme Sequence | AVPDKIDRRESGYV |
Enzyme Length | 14 |
Uniprot Accession Number | P80342 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; |
DNA Binding | |
EC Number | 3.4.22.15 |
Enzyme Function | FUNCTION: Thiol protease that assists the parasite in burrowing through the gut wall and liver of its mammalian host. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Non-terminal residue (1) |
Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Lysosome;Protease;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 1,605 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B60; |