| IED ID | IndEnz0002013525 |
| Enzyme Type ID | protease013525 |
| Protein Name |
Venom plasminogen activator LV-PA EC 3.4.21.- LMUT0402S Plasminogen activating proteinase Snake venom serine protease SVSP |
| 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 | MVLITVLANLLILQLSYAQKSSKLVFGGDECNINEHRSLVVLFNSSGFLCAGTLINKEWVLTAAHCDSENFQMQLGVHSKKVPNKDEETRDPKEKFICPNRKKNDEKDKDIMLIRLNRPVSNSEHIALLSLPSSPPSVGSVCRIMGWGTISPTKEIYPDVPHCADINILDHAVCRAAYSGWLATSTTLCAGILEGGKDSCHGDSGGPLICNGQFQGIVSLGRHPCGHPDEPGVYTKVFDYTDWIQSIIAGNTDAACPP |
| Enzyme Length | 258 |
| Uniprot Accession Number | Q27J47 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the serine protease inhibitors NPGB, PMSF, p-aminobenzamidine and aprotinin. Not inhibited by soybean trypsin inhibitor or EDTA. {ECO:0000269|PubMed:10871053}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that activates plasminogen. Weakly hydrolyzes the alpha chain of human fibrinogen without releasing fibrinopeptide A. Does not hydrolyze plasma kallikrein or factor Xa. Does not clot fibrinogen. Does not affect platelet function. Induces hypotensive effects on rats. Shows a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds. {ECO:0000269|PubMed:10871053, ECO:0000269|PubMed:17034951}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (8); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Hypotensive agent;Plasminogen activation;Protease;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17034951}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. PubMed:17034951 shows that it contains approximately 10% carbohydrates, PubMed:10871053 shows that it contains approximately 20% carbohydrates. {ECO:0000269|PubMed:10871053, ECO:0000269|PubMed:17034951}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,062 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=174 uM for H-D-Val-Leu-Arg-pNA (S-2266) {ECO:0000269|PubMed:17034951}; KM=131 uM for H-D-Val-Leu-Lys-pNA (S-2251) {ECO:0000269|PubMed:17034951}; KM=67 uM for N-p-Tos-Gly-Pro-Lys-pNA {ECO:0000269|PubMed:17034951}; KM=231 uM for H-D-Pro-Phe-Arg-pNA (S-2302) {ECO:0000269|PubMed:17034951}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |