| IED ID | IndEnz0002012269 |
| Enzyme Type ID | protease012269 |
| Protein Name |
Thrombin-like enzyme TLBm SVTLE TLBm EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Bothrops marajoensis (Marajo lancehead) |
| 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) Bothrops Bothrops marajoensis (Marajo lancehead) |
| Enzyme Sequence | VIGGDECNINESPFLAFLYSQLLSSRRYFCGMTLINQEWVLTAAHCNLYPDRKDMNWWLLIKLGKHSGSTRRWVANYDEQVRYWPKEKFIWWYCPNKKKDVINNYVWVWWDKDILLWELWMLIRLNRPVKYSEHIAPLSLPSSPPSAKWWHVGSVCRIMGWGQITETWWNSEDTLPDVPRCANINLFNYEVCRAYNQRWWRGLPAKTLCAGDLEGIIRGGWDTCVGDSGGPLICDGQYQGIAYWGSKPCAEPDEPAAYSKVFDHLDWSQSVIAGGTWWRGDDTCP |
| Enzyme Length | 285 |
| Uniprot Accession Number | P0DJE9 |
| Absorption | |
| Active Site | ACT_SITE 45; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 113; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF, disodium-EDTA, S(Dm) and soybean trypsin inhibitor (SBTI). SBTI and S(Dm) (the anti-hemorrhagic protein) acts as non-competitive inhibitors that decrease the enzymatic activity. {ECO:0000269|PubMed:19931298}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like enzyme that induces the formation of fibrin clot. Cleaves the Aalpha-chain of fibrinogen (FGA) with higher activity than the Bbeta-chain (FGB). Induces platelet aggregation in both platelet-rich plasma and in washed platelet preparations. This aggregation is strongly inhibited by preincubation of the enzyme with PMSF. {ECO:0000269|PubMed:19931298}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 38-40 degrees Celsius. {ECO:0000269|PubMed:19931298}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:19931298}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Homologous thrombin-like enzymes are N-glycosylated. This enzyme does not contain the consensus glycosylation sites, suggesting it is not glycosylated. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,241 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 M for N-alpha-benzoyl-DL-arginine-p-nitroanilide {ECO:0000269|PubMed:19931298}; Vmax=0.052 nmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-nitroanilide {ECO:0000269|PubMed:19931298}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |