| IED ID | IndEnz0002003409 |
| Enzyme Type ID | protease003409 |
| Protein Name |
Leech-derived tryptase inhibitor C LDTI-C Cleaved into: Leech-derived tryptase inhibitor B LDTI-B ; Leech-derived tryptase inhibitor A LDTI-A |
| Gene Name | |
| Organism | Hirudo medicinalis (Medicinal leech) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Clitellata Hirudinea (leeches) Hirudinida Hirudiniformes Hirudinidae Hirudo Hirudo medicinalis (Medicinal leech) |
| Enzyme Sequence | KKVCACPKILKPVCGSDGRTYANSCIARCNGVSIKSEGSCPTGILN |
| Enzyme Length | 46 |
| Uniprot Accession Number | P80424 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Chain (3); Disulfide bond (3); Domain (1); Helix (1); Site (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Protease inhibitor;Serine protease inhibitor |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (4); X-ray crystallography (2) |
| Cross Reference PDB | 1AN1; 1LDT; 2KMO; 2KMP; 2KMQ; 2KMR; |
| Mapped Pubmed ID | 19820233; |
| Motif | |
| Gene Encoded By | |
| Mass | 4,744 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |