| IED ID | IndEnz0002013647 |
| Enzyme Type ID | protease013647 |
| Protein Name |
Snake venom metalloproteinase BpirMP SVMP EC 3.4.24.- Alpha-fibrinogenase Fibrinolytic metalloproteinase Zinc metalloproteinase Fragment |
| Gene Name | |
| Organism | Bothrops pirajai (Piraja's lancehead) |
| 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 pirajai (Piraja's lancehead) |
| Enzyme Sequence | TYIEVAVVADHRMFKKYNSNLNTIRKWVHEMVNSMNGVYRSMDVHLSLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAIVFDQQTIGRAYIGGMCDPRHSVGVVMDHSKINLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMXXXXXXXXXXXXXXCXXXXXXXXXTKHNPQCILNEPL |
| Enzyme Length | 198 |
| Uniprot Accession Number | P0DL29 |
| Absorption | |
| Active Site | ACT_SITE 138; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the chelating agents EDTA, EGTA and 1,10-phenanthroline. Is not inhibited by serine proteinase inhibitors aprotinin, leupeptin and benzamidine. {ECO:0000269|PubMed:23385358}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloprotease that preferentially degrades Aalpha chain of fibrinogen (FGA) (at a dose of 5 ug, whereas at a dose of 10 ug, both FGA and FGB are completely degraded). Degrades fibrin gel in a dose-dependent manner, as well blood clots formed in vitro (thrombolytic activity). Induces hemorrhage (in the dorsal skin of mice), with an MHD of 50 ug. The basal membrane components collagen (all chains of type IV) (COL4A4), fibronectin (FN1), laminin and nidogen are all degraded by this toxin. {ECO:0000269|PubMed:23385358}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:23385358}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:23385358}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (7); Non-terminal residue (1); Sequence uncertainty (36) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| 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 | 22,586 |
| Kinetics | |
| Metal Binding | METAL 4; /note=Calcium; /evidence=ECO:0000250; METAL 88; /note=Calcium; /evidence=ECO:0000250; METAL 137; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 141; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 147; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 192; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 195; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |