| IED ID | IndEnz0002005069 |
| Enzyme Type ID | protease005069 |
| Protein Name |
Cathepsin L-like proteinase EC 3.4.22.- |
| Gene Name | Cat-1 |
| 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 | MRLFILAVLTVGVLGSNDDLWHQWKRMYNKEYNGADDQHRRNIWEKNVKHIQEHNLRHDLGLVTYTLGLNQFTDMTFEEFKAKYLTEMSRASDILSHGVPYEANNRAVPDKIDWRESGYVTEVKDQGNCGSCWAFSTTGTMEGQYMKNERTSISFSEQQLVDCSGPWGNNGCSGGLMENAYQYLKQFGLETESSYPYTAVEGQCRYNKQLGVAKVTGYYTVHSGSEVELKNLVGARRPAAVAVDVESDFMMYRSGIYQSQTCSPLRVNHAVLAVGYGTQGGTDYWIVKNSWGTYWGERGYIRMARNRGNMCGIASLASLPMVARFP |
| Enzyme Length | 326 |
| Uniprot Accession Number | Q24940 |
| Absorption | |
| Active Site | ACT_SITE 132; /evidence=ECO:0000250|UniProtKB:P07711; ACT_SITE 269; /evidence=ECO:0000250|UniProtKB:P07711; ACT_SITE 289; /evidence=ECO:0000250|UniProtKB:P07711 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by Antipain, E64 and Leupeptin, and weakly inhibited by iodoacetic acid (IAA) and phenylmethylsulfonyl fluoride (PMSF). Requires the presence of dithiothreitol (DTT) for activity. {ECO:0000269|PubMed:8192668}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Thiol protease. Probably involved in interaction with host tissues. Displays a similar activity to that of papain. Has high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec. {ECO:0000269|PubMed:8192668, ECO:0000303|PubMed:8192668}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 in a mixed-buffer system. In a Tris buffer high levels of activity were detected at very alkaline pHs. {ECO:0000269|PubMed:8192668}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (10); Chain (1); Disulfide bond (3); Helix (14); Modified residue (2); Propeptide (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Hydroxylation;Protease;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8192668}. |
| Modified Residue | MOD_RES 109; /note=3-hydroxyproline; partial; /evidence=ECO:0000269|PubMed:8192668; MOD_RES 196; /note=3-hydroxyproline; partial; /evidence=ECO:0000269|PubMed:8192668 |
| Post Translational Modification | PTM: Contains cysteine residues involved in intramolecular disulfide bonding. {ECO:0000269|PubMed:8192668}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2O6X; |
| Mapped Pubmed ID | 18160404; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,896 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for Z-Phe-Arg-NHMec (at pH 7.45) {ECO:0000269|PubMed:8192668}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B49;3.4.22.B60; |