| IED ID | IndEnz0002011030 |
| Enzyme Type ID | protease011030 |
| Protein Name |
Thrombin-like enzyme F202 SVTLE EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Crotalus durissus cascavella (Northeastern Brazilian rattlesnake) |
| 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) Crotalus Crotalus durissus (tropical rattlesnake) Crotalus durissus cascavella (Northeastern Brazilian rattlesnake) |
| Enzyme Sequence | VVGGDECNINEHRFLVALYANSSLLCGGTLINQEWVLIAAHCDR |
| Enzyme Length | 44 |
| Uniprot Accession Number | P0DKY5 |
| 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: Enzyme activity is markedly inhibited by TLCK and PMSF, and moderately by SBTi. Platelet aggregating activity is strongly inhibited by TLCK. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that coagulates fibrinogen by inducing a fast degradation of the alpha chain (FGA) from human citrated plasma, and a slow degradation of beta chain (FGB). Potently induces platelet aggregation in both platelet rich plasma and washed platelet preparations in a concentration-dependent fashion. Shows amidolytic activities. {ECO:0000269|PubMed:16729248}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;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: Contains 6 disulfide bonds. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 4,815 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for BApNA {ECO:0000269|PubMed:16729248}; Vmax=5.64 umol/min/mg enzyme {ECO:0000269|PubMed:16729248}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |