Detail Information for IndEnz0002012325
IED ID IndEnz0002012325
Enzyme Type ID protease012325
Protein Name Thrombin-like enzyme leucurobin
Leuc
SVTLE
EC 3.4.21.74
Fibrinogen-clotting enzyme
Snake venom serine protease
SVSP
Gene Name
Organism Bothrops leucurus (Whitetail 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 leucurus (Whitetail lancehead)
Enzyme Sequence VIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIXXXXHAGSVANYDEVVRXXXXXFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP
Enzyme Length 231
Uniprot Accession Number P0DJ86
Absorption
Active Site ACT_SITE 41; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 86; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by PMSF and benzamidine. Its clotting effect is strongly inhibited by antibothropic serum. Is not inhibited by heparin. {ECO:0000269|PubMed:16481207}.
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; Evidence={ECO:0000269|PubMed:16481207};
DNA Binding
EC Number 3.4.21.74
Enzyme Function FUNCTION: Thrombin-like snake venom serine protease that cleaves Arg-Gly bonds in alpha-chain of fibrinogen (FGA). Induces temporary episodes of opisthotonos and rapid rolling around the long axis of the animal (gyroxin-like effect), when injected into the tail veins of mice (0.143 ug/g mouse). {ECO:0000269|PubMed:16481207}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:16481207};
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Site (1)
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 {ECO:0000269|PubMed:16481207}.
Modified Residue
Post Translational Modification PTM: Glycosylated.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 25,425
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.9 uM for H-D-Val-Leu-Arg-pNA (S-2266) {ECO:0000269|PubMed:16481207}; KM=7.9 uM for H-D-Pro-Phe-Arg-pNA (S-2302) {ECO:0000269|PubMed:16481207}; KM=2.7 uM for Bz-Phe-Val-Arg-pNA (S-2160) {ECO:0000269|PubMed:16481207}; KM=5.7 uM for H-D-Val-Leu-Lys-pNA (S-2251) {ECO:0000269|PubMed:16481207};
Metal Binding
Rhea ID
Cross Reference Brenda