| IED ID | IndEnz0002012648 |
| Enzyme Type ID | protease012648 |
| Protein Name |
Thrombin-like enzyme BpirSP41 SVTLE EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Bothrops pirajai (Piraja's lancehead) |
| 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 pirajai (Piraja's lancehead) |
| Enzyme Sequence | VVGGDECDINEHPFLAFLYSHGYFCGLTLINQEWVLTAAHCDRRFMRIYL |
| Enzyme Length | 50 |
| Uniprot Accession Number | P0DL27 |
| Absorption | |
| Active Site | ACT_SITE 40; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by serine protease inhibitors PMSF, benzamidine, leupeptin and aprotinin, as well as by copper ions (Cu2+). Not inhibited by metalloprotease inhibitors EDTA, EGTA and 1,10-phenanthroline, as well as by barium (Ba2+) and calcium ion (Ca2+). {ECO:0000269|PubMed:22819993}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that interferes with the hemostatic system of the prey. It almost completely degrades both Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen. It presents a higher ability to degrade fibrin clots than BpirSP27. It hydrolyzes chromogenic substrates S-2238 (used for testing thrombin activity), S-2222 (factor Xa), S-2266 (glandular kallikrein and factor XIa), and S-2302 (plasma kallikrein, factor XIa and XIIa). It shows a decrease in the clotting time of human plasma in the presence of increasing doses of the enzyme. Its minimum coagulant dose (MCD) is 20 ug. It promotes platelet aggregation with a maximum of aggregation of 20%, regardless of the concentration increase or the presence of calcium. It also shows 40% inhibition of the hemolytic activity promoted by the complement pathways and possess only a minor role in the induction of edema and pain in rat. {ECO:0000269|PubMed:22819993, ECO:0000269|PubMed:23499645}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-60 degrees Celsius. {ECO:0000269|PubMed:22819993}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:22819993}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Complement system impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:22819993}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 5,836 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |