| IED ID | IndEnz0010001517 |
| Enzyme Type ID | esterase001517 |
| Protein Name |
Thrombin-like enzyme LMR-47 SVTLE LM-47 SVTLE LMR-47 EC 3.4.21.74 Fibrinogen-clotting enzyme Gyroxin analog Snake venom serine protease SVSP Venombin A Fragment |
| Gene Name | |
| Organism | Lachesis muta rhombeata (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 rhombeata (Bushmaster) |
| Enzyme Sequence | VIGGDECNINEHRFLVALYDGLSGTFLCGG |
| Enzyme Length | 30 |
| Uniprot Accession Number | Q9PRP4 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by antipain, PMSF, TPCK, leupeptin, pepstatin, EDTA, and E-64 (trans-epoxysuccinylleucylamido(4-guanidino)butane). |
| 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 specifically hydrolyzes the Aalpha chain of fibrinogen (FGA). Exhibits strong N-p-tosyl-L-arginine methyl esterase activity, and hydrolyzes tripeptide nitroanilide derivatives weakly or not at all. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:8783450}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,171 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for N-p-tosyl-L-arginine methyl ester (TAME) {ECO:0000269|PubMed:8783450}; KM=589 uM for NBz-Pro-Phe-Arg-pNA {ECO:0000269|PubMed:8783450}; KM=1320 uM for NBz-Val-Gly-Arg-pNA {ECO:0000269|PubMed:8783450}; KM=857 uM for NBz-DL-Arg-pNA {ECO:0000269|PubMed:8783450}; Vmax=877.0 nmol/sec/mg enzyme for N-p-tosyl-L-arginine methyl ester (TAME) {ECO:0000269|PubMed:8783450}; Vmax=51.0 nmol/sec/mg enzyme for NBz-Pro-Phe-Arg-pNA {ECO:0000269|PubMed:8783450}; Vmax=75.0 nmol/sec/mg enzyme for NBz-Val-Gly-Arg-pNA {ECO:0000269|PubMed:8783450}; Vmax=39.3 nmol/sec/mg enzyme for NBz-DL-Arg-pNA {ECO:0000269|PubMed:8783450}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |