| IED ID | IndEnz0002011804 |
| Enzyme Type ID | protease011804 |
| Protein Name |
Snake venom serine protease Dav-PA SVSP AaV-SP-I AaV-SP-II EC 3.4.21.- |
| Gene Name | |
| Organism | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| 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) Deinagkistrodon Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| Enzyme Sequence | MVLIRVLANLLILQLSYAQKSSELVIGGNECDINEHRFLVAFFNTTGFFCGGTLINPEWVVTAAHCDSTDFQMQLGVHSKKVLNEDEQTRNPKEKFICPNKNNNEVLDKDIMLIKLDKPISNSKHIAPLSLPSSPPSVGSVCRIMGWGSITPVKETFPDVPYCANINLLDHAVCQAGYPELLAEYRTLCAGIVQGGKDTCGGDSGGPLICNGQFQGIVSYGAHPCGQGPKPGIYTNVFDYTDWIQRNIAGNTDATCPP |
| Enzyme Length | 258 |
| Uniprot Accession Number | Q9I8X1 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15632114; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15632114; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15632114 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by NPGB, leupeptin, aprotinin and PMSF, but not by EDTA, SBTI, heparin and hirudin. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that has fibrinogenolytic activities. Also possess esterolysis and amidolytic activities. Selectively cleaves Arg-|-Xaa bonds. {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (4); Natural variant (1); Propeptide (1); Signal peptide (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1OP0; 1OP2; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,033 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.152 uM for TAME {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}; KM=265 uM for D-Phe-L-Pip-Arg-p-NA (S-2238) {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}; KM=113 uM for D-Pro-Phe-Arg-p-NA (S-2302) {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}; KM=28 uM for N-p-Tosyl-Gly-Pro-Arg-p-NA {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}; KM=202 uM for N-p-Tosyl-Gly-Pro-Lys-p-NA {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114}; Note=AaV-SP-II.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |