| IED ID | IndEnz0002013179 |
| Enzyme Type ID | protease013179 |
| Protein Name |
Snake venom metalloproteinase BmooMPalpha-I SVMP EC 3.4.24.- Zinc metalloproteinase BmooMPalfa-I |
| Gene Name | |
| Organism | Bothrops moojeni (Lance-headed viper) (Caissaca) |
| 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 moojeni (Lance-headed viper) (Caissaca) |
| Enzyme Sequence | EQQKFSPRYIELVVVADHGMFKKYNSNLNTIRKWVHEMVNSMNGFYRSVDVTASLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAIVFDGHTIGRAYTGGMCDPRHSVGVVMDHSPKNLQVAVTMAHELGHNLGMHHDGNQCHCDAASCIMADSLSVVLSYEFSDCSQNQYQTYLTKHNPQCILNEPL |
| Enzyme Length | 205 |
| Uniprot Accession Number | P85314 |
| Absorption | |
| Active Site | ACT_SITE 145; /evidence="ECO:0000250|UniProtKB:P83512, ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. Not inhibited by the serine proteinase inhibitors aprotinin and benzamidine. {ECO:0000269|PubMed:18187176}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that cleaves the alpha chain of fibrinogen (FGA) first followed by the beta chain (FGB) and shows no effect on the gamma chain. Cleaves only the beta chain of fibrin, leaving the gamma-dimer untouched. Shows proteolytic activity towards azocasein. Causes defibrinogenation when intraperitoneally administered on mice. {ECO:0000269|PubMed:18187176}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:18187176}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Chain (1); Disulfide bond (3); Domain (1); Helix (8); Metal binding (7); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18187176}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3GBO; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,279 |
| Kinetics | |
| Metal Binding | METAL 11; /note=Calcium; METAL 95; /note=Calcium; METAL 144; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:19706302; METAL 148; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:19706302; METAL 154; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:19706302; METAL 199; /note=Calcium; via carbonyl oxygen; METAL 202; /note=Calcium |
| Rhea ID | |
| Cross Reference Brenda |