| IED ID | IndEnz0002012830 |
| Enzyme Type ID | protease012830 |
| Protein Name |
Beta-fibrinogenase VLBF EC 3.4.21.- Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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 Viperinae (vipers) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MVLIRVLANLLLLQLSHAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQEWVLSAAHCDMENMRIYLGWHNFSLPNMNQKRRVAKEKFFCLSSKNYTEWDKDIMLIKMNRPVTYSTHVAPLSLPSSPPSVGSVCRIMGWGAITSPNETYPDVPHCANINILNYTVCRAAHPWLPAQSRTLCAGILQGGIDTCKGDSGGPLICNGQIQGIVSWGDNPCAQPLKPGHYTNVFDYTDWIQSIIAGNTTATCPP |
| Enzyme Length | 257 |
| Uniprot Accession Number | E0Y419 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 203; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and PMSF. {ECO:0000269|PubMed:2028469}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that has fibrinogenolytic activities by hydrolyzing the beta chain of fibrinogen (FGB). Typical arginine esterase which hydrolyzes esters and amides of arginine. {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:2028469}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Sialic acid;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. Contains 23.0% of hexoses, 8.3% of hexosamines and 1.0% of sialic acids. {ECO:0000269|PubMed:11602278}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,297 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for N-alpha-benzoyl-L-arginine ethyl ester (BAEE) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.36 mM for Tosyl-L-arginine methyl ester (TAME) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.18 mM for BAPNA (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |