| IED ID | IndEnz0002011107 |
| Enzyme Type ID | protease011107 |
| Protein Name |
Thrombin-like enzyme gloshedobin SVTLE EC 3.4.21.- Defibrase Fibrinogen-clotting enzyme Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis) |
| 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 shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis) |
| Enzyme Sequence | MVLIRVQANLLILQLSYAQKSSELIIGGDECNINEHRFLVALYTSRSRRFYCGGTLINQEWVLTAAHCDRKNIRIKLGMHSEKVPNEDAETRVPKEKFFCLSSKTYTKWDKDIMLMRLKRPVNNSTHIAPVSLPSNPPSVDSVCRVMGWGTITSPQETYPDVPHCANINILDYEVCQAAHGGLPATSRTLCAGILKGGKDSCKGDSGGPLICNGQFQGIASWGAHPCGQSLKPGVYTKVFDYTEWIQSIIAGNTDATCPP |
| Enzyme Length | 260 |
| Uniprot Accession Number | P0C5B4 |
| Absorption | |
| Active Site | ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by PMSF, and N-tosyl-Lphenylalanine chloromethyl ketone (TPCK) and poorly inhibited by benzamidine and derivates. Not inhibited by EDTA, heparin and hirudin. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313, ECO:0000269|PubMed:20969888}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease. The recombinant form clots fibrinogen by cleaving fibrinogen Aalpha chain (FGA), and slowly Bbeta chain (FGB). Has amidolytic activities. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,616 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |