| IED ID | IndEnz0002010890 |
| Enzyme Type ID | protease010890 |
| Protein Name |
Snake venom metalloproteinase neuwiedase SVMP EC 3.4.24.- Fragment |
| Gene Name | |
| Organism | Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
| 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 neuwiedi group Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
| Enzyme Sequence | QQRFFPQRYIELVIVADRRMYTKYNSDSNKIRTRVHELVNTVNGFFRSMNVDASLANLEVWSKKDLIKVEKDSSKTLTSFGEWRERDLLRRKSHDNAQLLTAIDFNGNTIGRAYLGSMCNPKRSVGIVQDHSPINLLVGVTMAHELGHNLGMEHDGKDCLCGASLCIMSPGLTDGPSYEFSDCSKDYYQTFLTNHNPQ |
| Enzyme Length | 198 |
| Uniprot Accession Number | Q9I9R4 |
| Absorption | |
| Active Site | ACT_SITE 145; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, EGTA and 1,10-phenanthroline, partially inhibited by beta-mercaptoethanol and not inhibited by serine protease inhibitors (leupeptin and aprotinin). Also inhibited by an excess of zinc, mercury and magnesium ions. Extracts of the plant Casearia mariquitensis neutralizes the decrease of platelets and plasma fibrinogen induced by the protease. The same extracts also partially inhibit Bbeta chain cleavage, but not Aalpha chain cleavage. {ECO:0000269|PubMed:11032408, ECO:0000269|PubMed:14505822}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This non-hemorrhagic metalloprotease hydrolyzes the Aalpha chain of fibrin and fibrinogen first followed by the Bbeta chain and shows no effect on the gamma chain. It is also able to degrade type I collagen, fibronectin, laminin and induces inflammatory reaction. It is devoid of hemorrhagic and thrombotic activities, but induces pulmonary bleeding. It also induces a mild myotoxic reaction. It is not able to inhibit platelet aggregation, but it induces decrease of platelets and plasma fibrinogen. It contributes to local tissue damage by inducing edema, inflammatory infiltrate and mild myotoxicity, and by degrading extracellular matrix components. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds (PubMed:11032408). {ECO:0000269|PubMed:11032408, ECO:0000269|PubMed:11506891, ECO:0000269|PubMed:14505822}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:11032408}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-8.0. {ECO:0000269|PubMed:11032408}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Metal binding (5); Non-terminal residue (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic 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 | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,524 |
| Kinetics | |
| Metal Binding | METAL 11; /note=Calcium; /evidence=ECO:0000250; METAL 95; /note=Calcium; /evidence=ECO:0000250; METAL 144; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 148; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 154; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |