IED ID | IndEnz0010001518 |
Enzyme Type ID | esterase001518 |
Protein Name |
Thrombin-like enzyme gyroxin analog LM-TL SVTLE EC 3.4.21.74 Fibrinogen-clotting enzyme Snake venom serine protease SVSP Venombin A |
Gene Name | |
Organism | Lachesis muta muta (Bushmaster) |
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) Lachesis Lachesis muta (South American bushmaster) Lachesis muta muta (Bushmaster) |
Enzyme Sequence | VIGGDECNINEHRFLVALYDGLSGTFLCGGTLINQEWVLTAQHCNRSLMNIYLGMHNKNVKFDDEQRRYPKKKYFFRCNKNFTKWDEDIRLNRPVRFSAHIEPLSLPSNPPSEDSVCRVMGWGQITSPPETLPDVPHCANINLFNYTVCRGAYPRMPTKVLCAGVLEGGIDTCNRDSGGPLICNGQFQGIVFWGPDPCAQPDKPGVYTKVFDYLDWIQSVIAGNTTCS |
Enzyme Length | 228 |
Uniprot Accession Number | P33589 |
Absorption | |
Active Site | ACT_SITE 43; /note=Charge relay system; ACT_SITE 88; /note=Charge relay system; ACT_SITE 177; /note=Charge relay system |
Activity Regulation | ACTIVITY REGULATION: Inhibited competitively by amidines and guanidines, and irreversibly inhibited by diisopropylfluorophosphate. |
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 cleaves alpha-chain of fibrinogen (FGA) releases only fibrinopeptide A. Shows coagulant, esterase and amidase activities. Induces the barrel rotation syndrome in mice, which is manifested by gyroxin-like, rapid rolling motions. May also reversibly increase the permeability of the blood brain barrier (BBB) in mice. {ECO:0000269|PubMed:11137545, ECO:0000269|PubMed:2781576, ECO:0000269|PubMed:8354384}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (4); Sequence conflict (2) |
Keywords | Blood coagulation cascade activating toxin;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 | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,629 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |