| IED ID | IndEnz0002009957 |
| Enzyme Type ID | protease009957 |
| Protein Name |
Beta-fibrinogenase brevinase EC 3.4.21.- Snake venom serine protease SVSP Cleaved into: Beta-fibrinogenase brevinase chain A; Beta-fibrinogenase brevinase chain B |
| Gene Name | |
| Organism | Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi) |
| 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) Gloydius Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi) |
| Enzyme Sequence | VIGGDECNINEHRFLALLYSERFQCGGTLINEEWVLTAAHCDMGNMYIYLGVHNVSVQYDDEQRRYPKKKYFCLSSRNYNQWDNDIMLIRLNRPVRNSAHIAPLSLPSGPPSVGSVCRVMGWGTITSPNETYPDVPHCANINILDYEVCRAAYAGLPATSRTLCAGILEGGKDSCRGDSGGPLICNGEIQGIVSWGGNICAQPREPGLYTKVFDYIDWIQSIIAGNTTVNCPP |
| Enzyme Length | 233 |
| Uniprot Accession Number | Q9PT51 |
| Absorption | |
| Active Site | ACT_SITE 40; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 85; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 179; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: The fibrinolytic activity is completely inhibited by PMSF, diisopropylfluorophosphate (DFP), pefabloc, dithiothreitol (DTT) and Zn(2+), but not by Pepstatin A, E64, iodoacetate, chymostatin, tosyl-Lphenylalanine chloromethyl ketone (TPCK), soybean trypsin inhibitor (SBTI), phosphoramidon, Ca(2+), Co(2+), Cu(2+), Fe(2+), Mg(2+), Mn(2+), K(+), and Na(+). {ECO:0000269|PubMed:10403823}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that has fibrinogenolytic activities. Preferentially cleaves the Bbeta-chain (FGB) and more slowly the Aa-chain (FGA) of fibrinogen, but does not affect the gamma-chain. Has also fibrinolytic activity. May play a role in antithrombotic reaction as well as thrombolytic reaction. {ECO:0000269|PubMed:10403823}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is from 5.5 to 8.5. {ECO:0000269|PubMed:10403823}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (6); Domain (1); Glycosylation (3); Motif (1); Site (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10403823}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 176..178; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 25,725 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |