| IED ID | IndEnz0002013528 |
| Enzyme Type ID | protease013528 |
| Protein Name |
Thrombin-like enzyme cerastobin SVTLE EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Cerastes vipera (Sahara sand viper) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Viperinae (vipers) Cerastes Cerastes vipera (Sahara sand viper) |
| Enzyme Sequence | VIGGAKCNINEHRSIVLLYSSRLFGHTLINKEWVL |
| Enzyme Length | 35 |
| Uniprot Accession Number | P18692 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP). |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease, that cleaves both alpha-chain (FGA) and beta-chain (FGB) of fibrinogen. Partially degrades factor X (F10), and release bradykinin from kininogen (KNG). Potently induces platelet aggregation. Shows a proteolytic activity towards protein constituents of the platelets cytoskeleton. Hydrolyzes actin, actin-binding protein, and P235. Shows a preferential cleavage at Arg-|-Xaa bonds. {ECO:0000269|PubMed:1963167, ECO:0000269|PubMed:2539861}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:2539861}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:2539861}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,982 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |