| IED ID | IndEnz0002009951 |
| Enzyme Type ID | protease009951 |
| Protein Name |
Thrombin-like enzyme ancrod SVTLE EC 3.4.21.74 Fibrinogen-clotting enzyme Snake venom serine protease SVSP Venombin A |
| Gene Name | |
| Organism | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| 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) Calloselasma Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| Enzyme Sequence | VIGGDECNINEHRFLVAVYEGTNWTFICGGVLIHPEWVITAEHCARRRMNLVFGMHRKSEKFDDEQERYPKKRYFIRCNKTRTSWDEDIMLIRLNKPVNNSEHIAPLSLPSNPPIVGSDCRVMGWGSINRRIDVLSDEPRCANINLHNFTMCHGLFRKMPKKGRVLCAGDLRGRRDSCNSDSGGPLICNEELHGIVARGPNPCAQPNKPALYTSIYDYRDWVNNVIAGNATCSP |
| Enzyme Length | 234 |
| Uniprot Accession Number | P26324 |
| Absorption | |
| Active Site | ACT_SITE 43; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 88; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 182; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; |
| DNA Binding | |
| EC Number | 3.4.21.74 |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that acts as an anticoagulant. It cleaves fibrinogen (FGA) to split off the A-fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The resulting fibrin polymers are imperfectly formed and much smaller in size (1 to 2 um long) than the fibrin polymers produced by the action of thrombin. These ancrod-induced microthrombi are friable, unstable, urea-soluble and have significantly degraded alpha chains. They do not cross-link to form thrombi. They are markedly susceptible to digestion by plasmin and are rapidly removed from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the removal of fibrinogen from the blood is rapid, occurring within hours following its administration. It does not activate plasminogen and does not degrade preformed, fully cross-linked thrombin fibrin. It also reduces the level of plasminogen activator inhibitor (PAI) and may stimulate the release of tissue plasminogen activator (PLAT) from the endothelium. The profibrinolytic effect of these 2 actions appears to be limited to local microthrombus degradation. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (5) |
| Keywords | Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Pharmaceutical;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,570 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |