| IED ID | IndEnz0002009202 |
| Enzyme Type ID | protease009202 |
| Protein Name |
Snake venom metalloproteinase bothrojaractivase SVMP EC 3.4.24.- Fragments |
| Gene Name | |
| Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| 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 Crotalinae (pit vipers) Bothrops Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| Enzyme Sequence | RYIELAVVADHGMFTKYRVHELVNTVNGFFRSKQDLIKVQKDKTLTSFGEWRERDLLPRI |
| Enzyme Length | 60 |
| Uniprot Accession Number | P0C7A9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by EDTA and EGTA. Partially inhibited by serine proteinase inhibitors PMSF and benzamidine. Not inhibited by cysteine proteinase inhibitors mercury ions and E-64. Is active without cofactors, although the presence of low concentrations of calcium and zinc ions enhanced its ability to convert prothrombin (F2) into active thrombin. {ECO:0000269|PubMed:18262582}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Prothrombin (F2) activator that is cofactor-independent. Also has fibrinolytic and fibrinogenolytic activity. It degrades the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen, while the gamma-chain is only partially and slowly affected. A dose-dependent procoagulant activity is shown in human plasma. {ECO:0000269|PubMed:18262582}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:18262582}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (1); Non-adjacent residues (2); Non-terminal residue (2) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18262582}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 7,166 |
| Kinetics | |
| Metal Binding | METAL 4; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |