| IED ID | IndEnz0002014369 |
| Enzyme Type ID | protease014369 |
| Protein Name |
Alkaline serine protease NJP EC 3.4.21.- Fragments |
| Gene Name | |
| Organism | Hediste japonica (Polychaete worm) (Neanthes japonica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Polychaeta (polychaetes) Errantia Phyllodocida Nereididae (sandworms) Hediste Hediste japonica (Polychaete worm) (Neanthes japonica) |
| Enzyme Sequence | VTVVQYRSTNASSGYLNLRVYLLDTGLR |
| Enzyme Length | 28 |
| Uniprot Accession Number | P86834 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF. Not or very weakly inhibited by EDTA, EGTA, beta-mercaptoethanol, benzamidine, aprotinin, iodoacetic acid, pepstatin A and SBTI. {ECO:0000269|PubMed:21276864}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Alkaline thrombin-like serine protease. Has fibrinolytic and fibrinogenolytic but not plasminogenolytic activity. Cleaves fibrinogen chains Aalpha, Bbeta and gamma chains in that order. Cleaves after Arg and Lys residues. {ECO:0000269|PubMed:21276864}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Activity is stable from 30 to 60 degrees Celsius and. {ECO:0000269|PubMed:21276864}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. Activity is stable from pH 7 to 11. {ECO:0000269|PubMed:21276864}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-adjacent residues (2); Non-terminal residue (2) |
| Keywords | Blood coagulation;Direct protein sequencing;Fibrinogenolytic toxin;Fibrinolysis;Hemostasis;Hemostasis impairing toxin;Hydrolase;Protease;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,160 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |