| IED ID | IndEnz0002009836 |
| Enzyme Type ID | protease009836 |
| Protein Name |
Snake venom serine protease VaSP1 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 | VIGGDECNINEHPFLVALHTARXXRFYCAGTLINQEWVLTAARCDRXXXXXILGVHSKXXXXXXXXXXXXXXXXXXXXXXTYTRWDKDIMLIRLKRXXXXXXXXXXXXXXXXXXXXXXXXXIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKXXXKLPEKSRTLCAGILQGGIDSCKGISGGPLICNGEIQGIVSYGK |
| Enzyme Length | 200 |
| Uniprot Accession Number | P0DPS3 |
| Absorption | |
| Active Site | ACT_SITE 88; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C5B4; ACT_SITE 182; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P0C5B4 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Pefabloc (90% inhibition), DTT (90%), Zn(2+) (80%), trypsin inhibitor II (50%), and benzamidine (45%), but not inhibited by EDTA, Ca(2+), Mg(2+) AND L-Cys. {ECO:0000269|PubMed:24269689}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Snake venom serine protease active on several blood coagulation enzymes. It completely cleaves fibrinogen Aalpha chain (FGA) after 120 minutes, partially cleaves Bbeta chain (FGB) (overnight) and has no activity on gamma chain. It does not release fibrinopeptides A and/or B exclusively, since the enzyme does not provoke fibrin polymerisation. It also degrades fibrin as efficiently as plasmin, and exhibits potent ability to cleave plasminogen and prothrombin, as well as heavy chain of factor X (F10). In vitro, it cleaves insulin B-chain (at positions His38-Leu39, Ala40-Leu41 and Tyr16-Leu17). {ECO:0000269|PubMed:24269689}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:24269689}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1); Site (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24269689}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. The protein exist in multiple isoforms. {ECO:0000269|PubMed:24269689}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,208 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.2 uM for N-benzoyl-Phe-Val-Arg-p-nitroanilide {ECO:0000269|PubMed:24269689}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |