| IED ID | IndEnz0002011433 |
| Enzyme Type ID | protease011433 |
| Protein Name |
Thrombin-like enzyme BpirSP27 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 | VVGGDECNINEHRSLVAIFNSTGFFCSGILLNQEWVLTASHCDSTNFQMK |
| Enzyme Length | 50 |
| Uniprot Accession Number | P0DL26 |
| Absorption | |
| Active Site | ACT_SITE 41; /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 (Cu2+) and manganese (Mn2+) ions. 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 preferentially degrades the Bbeta chain (FGB) of fibrinogen, with minor effects on the Aalpha chain (FGA). It presents a lower ability to degrade fibrin clots than BpirSP41. It hydrolyzes chromogenic substrates S-2238 (used for testing thrombin activity), S-2222 (factor Xa), S-2266 (glandular kallikrein and factor XIa), S-2302 (plasma kallikrein, factor XIa and XIIa), and S-2251 (plasmin). 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 3.5 ug. It also promotes platelet aggregation in a concentration-dependent manner in the presence or absence of calcium. It also shows 20% 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); Glycosylation (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 | 5,534 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |