| IED ID | IndEnz0002012996 |
| Enzyme Type ID | protease012996 |
| Protein Name |
Snake venom metalloproteinase BjussuMP-2 SVMP EC 3.4.24.- BOJUMET I BjussuMP-II Nonhemorrhagic metalloprotease MP-II Fragment |
| Gene Name | |
| Organism | Bothrops jararacussu (Jararacussu) |
| 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 jararacussu (Jararacussu) |
| Enzyme Sequence | TELPKGAVQPKYEDAMQYEFKGNGEPVVLHLEKNKGLFSEDYSETHYSPDGRQIITYPPFEDHCYYHGRIENDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTETNWESYEPIKKASPSNLTPEQQKFSPRYIEVAVVADHRMFKKYNSNLNTIRKWVHEMVNSMNGVYRSMDVHLSLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAVVFDQQTIGRAYIAGMCDPRHSVGVVMDHSKENLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMASVLSVVLSYEFSDCSQNQYQTYLTKHNPQCILNEPLLTVSGNELLEAGE |
| Enzyme Length | 369 |
| Uniprot Accession Number | Q7T1T4 |
| Absorption | |
| Active Site | ACT_SITE 296; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by EDTA, EGTA, 1,10-phenanthroline, and partially by beta-mercaptoethanol. Is not inhibited by aprotinin and leupeptin. Conserves its activity upon fibrinogen when incubated with cobalt, magnesium ions up to 40 mM, but loses the proteolytic activity when incubated with manganese, fer, zinc or calcium ions. {ECO:0000269|PubMed:18006118}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This metalloproteinase displays proteolytic activity on fibrin, fibrinogen, collagen, casein and gelatin. It inhibits ADP- and collagen-induced platelet aggregation and displays a very low edema inducing activity. {ECO:0000269|PubMed:18006118}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:18006118}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (12); Non-terminal residue (1); Propeptide (1); Sequence conflict (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18006118}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,957 |
| Kinetics | |
| Metal Binding | METAL 162; /note=Calcium 1; /evidence=ECO:0000250; METAL 246; /note=Calcium 1; /evidence=ECO:0000250; METAL 295; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 299; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 305; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 350; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 353; /note=Calcium 1; /evidence=ECO:0000250; METAL 359; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 362; /note=Calcium 2; /evidence=ECO:0000250; METAL 364; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 366; /note=Calcium 2; /evidence=ECO:0000250; METAL 369; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |