| IED ID | IndEnz0002013487 |
| Enzyme Type ID | protease013487 |
| Protein Name |
Snake venom metalloproteinase CatroxMP-II SVMP EC 3.4.24.- Fibrinogenolytic metalloproteinase Fragment |
| Gene Name | |
| Organism | Crotalus atrox (Western diamondback rattlesnake) |
| 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) Crotalus Crotalus atrox (Western diamondback rattlesnake) |
| Enzyme Sequence | NPEHQRYVELFI |
| Enzyme Length | 12 |
| Uniprot Accession Number | P0DTB7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by carbon monoxide (CO) (PubMed:29761254). This inhibition is explained by the presence of heme attached to the enzyme and modulated by CO (PubMed:29761254). The state change of heme induced by CO (carboxyheme or metheme) may inhibit the enzyme (PubMed:29761254). {ECO:0000269|PubMed:29761254}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that cleaves both alpha- and beta-chains of fibrinogen, but not the gamma-chain (PubMed:29761254). {ECO:0000269|PubMed:29761254}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29761254}. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains 3 disulfide bonds. {ECO:0000250|UniProtKB:P34182}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,545 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |