Detail Information for IndEnz0010001518
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