| IED ID | IndEnz0002010615 |
| Enzyme Type ID | protease010615 |
| Protein Name |
Thrombin-like enzyme gabonase SVTLE EC 3.4.21.55 Fibrinogen-clotting enzyme Snake venom serine protease SVSP Venombin-AB Fragment |
| Gene Name | |
| Organism | Bitis gabonica (Gaboon adder) (Gaboon viper) |
| 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) Bitis Bitis gabonica (Gaboon adder) (Gaboon viper) |
| Enzyme Sequence | VVGGAECKIDGHRCLALLY |
| Enzyme Length | 19 |
| Uniprot Accession Number | P0C577 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF, but not by heparin, hirudin and antithrombin-III. {ECO:0000269|PubMed:3522580}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.55; |
| DNA Binding | |
| EC Number | 3.4.21.55 |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease. Releases both fibrinopeptides A and B from fibrinogen (FGA and FGB) to form fibrin clots. Also activates factor XIII (F13A). The activity of the enzyme is stabilized by calcium ion. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius with tosyl-Arg-methyl ester (TAME) as substrate and 37 degrees Celsius with natural substrates. {ECO:0000269|PubMed:3522580}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated.; PTM: Contains five disulfide bonds. {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,017 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for Tosyl-L-arginine methyl ester (TAME) {ECO:0000269|PubMed:3522580}; KM=0.13 mM for Tosyl-Gly-Pro-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=0.82 mM for H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=0.88 mM for H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=2.72 mM for Tosyl-Gly-Pro-Lys 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=3.4 mM for H-D-Phenylglycine-Phe-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |