| IED ID | IndEnz0002012066 |
| Enzyme Type ID | protease012066 |
| Protein Name |
Thrombin-like enzyme TLBan SVTLE TLBan EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragments |
| Gene Name | |
| Organism | Bothrocophias andianus (Andean lancehead) (Bothrops andianus) |
| 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) Bothrocophias Bothrocophias andianus (Andean lancehead) (Bothrops andianus) |
| Enzyme Sequence | VIGGDECNINEHPFLVALYYSTFFCGMTLINQEWVLTAAHESEKFPKEKYFIFCPNNKDIMLIRLDKPVSNSEHIAPLSLPSSPPSVGSVCRKPALYTKVFDYLLWIQSIIAGNTATCP |
| Enzyme Length | 119 |
| Uniprot Accession Number | P0DJG3 |
| Absorption | |
| Active Site | ACT_SITE 40; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 59; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by PMSF and slightly inhibited by EDTA and soybean trypsin inhibitor. {ECO:0000269|PubMed:22155303}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease, with high clotting activity in vitro. Has also fibrinogenolytic ability, showing a fast degradation of fibrinogen Aalpha chain (FGA), a slow degradation of Bbeta chain (FGB) and no degradation of gamma chain. Also causes platelet aggregation in platelet rich plasma (PRP) and washed platelet suspension. {ECO:0000269|PubMed:22155303}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:22155303}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22155303}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (4); Domain (1); Non-adjacent residues (4) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Sialic acid;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains both N-linked carbohydrates and sialic acid. {ECO:0000269|PubMed:22155303}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,356 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.79 M for N-alpha-benzoyl-DL-Arg-p-nitroanilide (DL-BApNA) {ECO:0000269|PubMed:22155303}; Vmax=0.54 nmol/min/mg enzyme with N-alpha-benzoyl-DL-Arg-p-nitroanilide (DL-BApNA) as substrate {ECO:0000269|PubMed:22155303}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |