| IED ID | IndEnz0002012440 |
| Enzyme Type ID | protease012440 |
| Protein Name |
Thrombin-like enzyme RP34 SVTLE EC 3.4.21.74 Fibrinogen-clotting enzyme Snake venom serine protease SVSP Venombin A Fragment |
| Gene Name | |
| Organism | Cerastes cerastes (Horned desert 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 cerastes (Horned desert viper) |
| Enzyme Sequence | VIGGDEXDINEHRSLALMYXSWSHRFIXXGXLI |
| Enzyme Length | 33 |
| Uniprot Accession Number | Q9PS28 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; |
| DNA Binding | |
| EC Number | 3.4.21.74 |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that displays clotting activity on fibrinogen. Shows both arginine-ester hydrolase and amidase activities on synthetic substrates. Also shows proteolytic activity toward casein. {ECO:0000269|PubMed:1485336}. |
| Temperature Dependency | |
| PH Dependency | |
| 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;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 | 3,786 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=65 nM for CBS 34-47 {ECO:0000269|PubMed:1485336}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |