| IED ID | IndEnz0002010309 | 
| Enzyme Type ID | protease010309 | 
| Protein Name | Zinc metalloproteinase-disintegrin-like VaH1 EC 3.4.24.- Snake venom metalloprotease SVMP Fragments | 
| Gene Name | |
| Organism | Vipera ammodytes ammodytes (Western sand viper) | 
| 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 Viperinae (vipers) Vipera Vipera ammodytes (Nose-horned viper) Vipera ammodytes ammodytes (Western sand viper) | 
| Enzyme Sequence | MVTKYSSIFMSPILSNPPILYFSDCSREXYQKXLTN | 
| Enzyme Length | 36 | 
| Uniprot Accession Number | P0DJ44 | 
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, but not inhibited by iodoacetamide, PMSF and pepstatin A. {ECO:0000269|PubMed:11602279}. | 
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- | 
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that exhibits strong hemorrhagic activity. It also degrades alpha-chain of fibrinogen (FGA), but not the beta- and the gamma-chains. Possesses potent azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at positions Ala(14)-Leu(15), followed by Tyr(16)-Leu(17) and His(10)-Leu(11). In vivo, subcutaneous injection into mice induces strong hemorrhage. {ECO:0000269|PubMed:11602279}. | 
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:11602279}; | 
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Non-adjacent residues (1); Non-terminal residue (2) | 
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc | 
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. | 
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked.; PTM: Glycosylated. | 
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 4,197 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B36; |