| IED ID | IndEnz0002011816 |
| Enzyme Type ID | protease011816 |
| Protein Name |
Snake venom metalloproteinase BpMP-1 SVMP EC 3.4.24.- Fibrinogenolytic metalloproteinase Fragments |
| 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 | YIELAVVADHGMFTKYNSNVNTIRTWVHEMVNSLNGFFRSMXVDDASLVNLEVWSKTLTSFGEWRDLLPRISHDHAQLLTTIVFDQQTIGIAYTAGMCDPSQSVAVVMDHVAVTMAHELGHNLGMDHDDTCTCGAKSCIMASTISKGLSFEFSDCSQNQYQTYVTKHNPQCILNK |
| Enzyme Length | 175 |
| Uniprot Accession Number | C0HJU2 |
| Absorption | |
| Active Site | ACT_SITE 118; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, 1,10-phenanthroline and beta-mercaptoethanol. Not inhibited by the serine protease inhibitors aprotinin and benzamidin. {ECO:0000269|PubMed:22008900}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Non-hemorrhagic snake venom zinc metalloprotease that hydrolyzes the Aalpha-chain of fibrinogen, more slowly the Bbeta-chain and shows no effect on the gamma chain. Has no coagulant activity on bovine plasma and fibrinogen. {ECO:0000269|PubMed:22008900}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity is highest at 4 degrees Celsius, decreases with increasing temperatures and is lost at 60 degrees Celsius. {ECO:0000269|PubMed:22008900}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Highest activity at neutral to basic pH. Reduced activity at pH 3.0. {ECO:0000269|PubMed:22008900}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (7); Non-adjacent residues (1); Non-terminal residue (2) |
| Keywords | Calcium;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:22008900}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,538 |
| Kinetics | |
| Metal Binding | METAL 3; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P85314; METAL 74; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P85314; METAL 117; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P85314; METAL 121; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P85314; METAL 127; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P85314; METAL 171; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P85314; METAL 174; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P85314 |
| Rhea ID | |
| Cross Reference Brenda |