| IED ID | IndEnz0002010735 |
| Enzyme Type ID | protease010735 |
| Protein Name |
Beta-fibrinogenase jerdofibrase EC 3.4.21.- 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 | VIGGDECNINEHPFLVLVYY |
| Enzyme Length | 20 |
| Uniprot Accession Number | P0DMU1 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF and soybean trypsin inhibitor. Partially inhibited by DTT and cysteine. Not affected by EDTA. {ECO:0000269|PubMed:11306131}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Fibrin(ogen)olytic serine protease degrades Bbeta-chain of human fibrinogen (FGB) and shows a lower activity on Aa-chain (FGA). Also degrades fibrin directly. Releases fibrinopeptide B and a small amount of fibrinopeptide A. Has also be shown to catalyze the hydrolysis of some chromogenic substrates such as S2238, S2160, S2302 and S2251. {ECO:0000269|PubMed:11306131}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11306131}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,295 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.8 uM for S-2160 (Bz-Ile-Glu-Gly-Arg-pNA) {ECO:0000269|PubMed:11306131}; KM=27 uM for S-2302 (H-D-Pro-Phe-Arg-pNA) {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097}; KM=46.7 uM for S-2238 (H-D-Phe-Pip-Arg-pNA) {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097}; KM=399.2 uM for S-2251 (H-D-Val-Leu-Lys-pNA) {ECO:0000269|PubMed:11306131, ECO:0000269|PubMed:12091097}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |