| IED ID | IndEnz0002011201 |
| Enzyme Type ID | protease011201 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like moojenin EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: Disintegrin-like Fragment |
| 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 | LGPDIVSPPVCGNELLEVGEECDCGTPENCQNE |
| Enzyme Length | 33 |
| Uniprot Accession Number | P0DKR0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The fibrinogenolytic and coagulant activities of the moojenin were abolished by preincubation with EDTA, 1,10-phenanthroline and beta-mercaptoethanol. {ECO:0000269|PubMed:22975266}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloproteinase moojenin: snake venom metalloproteinase that cleaves both alpha- and beta-chains of fibrinogen, but not the gamma-chain. Shows a coagulant activity on bovine plasma about 3.1 fold lower than crude venom. Renders the blood incoagulable when intraperitoneally administered into mice. Induces necrosis in liver and muscle, but does not cause histological alterations in mouse lungs, kidney or heart. {ECO:0000269|PubMed:22975266}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:22975266}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:22975266}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Disulfide bond (4); Domain (1); Metal binding (6); Non-terminal residue (2) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus (from the N-terminal region of the metalloproteinase domain) is blocked. {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,461 |
| Kinetics | |
| Metal Binding | METAL 10; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 13; /note=Calcium 1; /evidence=ECO:0000250; METAL 15; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 17; /note=Calcium 1; /evidence=ECO:0000250; METAL 20; /note=Calcium 1; /evidence=ECO:0000250; METAL 23; /note=Calcium 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |