| IED ID | IndEnz0002011427 |
| Enzyme Type ID | protease011427 |
| Protein Name |
Thrombin-like enzyme jerdonobin SVTLE EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii) |
| 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) Protobothrops Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii) |
| Enzyme Sequence | VIGGDECNINEHRFLVALYDF |
| Enzyme Length | 21 |
| Uniprot Accession Number | P0DM43 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Amidolytic and clotting activities are completely inhibited by NPGB and PMSF, but not inhibited by EDTA. {ECO:0000269|PubMed:10736476}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that has fibrinogen-clotting activity (217 NIH units/mg). It releases fibrinopeptide A and a small amount of fibrinopeptide B from fibrinogen alpha (FGA) and beta (FGB). {ECO:0000269|PubMed:10736476, ECO:0000269|PubMed:12091097}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10736476}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,425 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for H-D-Phe-Pip-Arg-pNA (S-2238) {ECO:0000269|PubMed:10736476, ECO:0000269|PubMed:12091097}; KM=53 uM for H-D-Pro-Phe-Arg-pNA (S-2302) {ECO:0000269|PubMed:10736476, ECO:0000269|PubMed:12091097}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |