| IED ID | IndEnz0002012671 |
| Enzyme Type ID | protease012671 |
| Protein Name |
Snake venom metalloproteinase leucurolysin-A Leuc-A SVMP EC 3.4.24.- |
| 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 | QQFSPRYIELVVVADHGMFKKYNSNLNTIRKWVHEMLNTVNGFFRSMNVDASLVNLEVWSKKDLIKVEKDSSKTLTSFGEWRERDLLPRISHDHAQLLTVIFLDEETIGIAYTAGMCDLSQSVAVVMDHSKKNLRVAVTMAHELGHNLGMRHDGNQCHCNAPSCIMADTLSKGLSFEFSDCSQNQYQTYLTKHNPQCILNKP |
| Enzyme Length | 202 |
| Uniprot Accession Number | P84907 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and 2-mercaptoethanol. Inhibited by 1 mM zinc ion and to a lesser extent by 1 mM calcium ion. {ECO:0000269|PubMed:16139412}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM. {ECO:0000269|PubMed:16139412, ECO:0000269|PubMed:17482228}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius with a complete loss of activity above 60 degrees Celsius. {ECO:0000269|PubMed:16139412}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for dimethylcasein with a complete loss of activity above pH 11.0. {ECO:0000269|PubMed:16139412}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Disulfide bond (3); Domain (1); Helix (9); Metal binding (7); Modified residue (1); Sequence conflict (3); Turn (2) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16139412}. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:19652343 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4Q1L; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,019 |
| Kinetics | |
| Metal Binding | METAL 9; /note=Calcium 1; /evidence=ECO:0007744|PDB:4Q1L; METAL 93; /note=Calcium 1; /evidence=ECO:0007744|PDB:4Q1L; METAL 142; /note=Zinc; catalytic; /evidence=ECO:0007744|PDB:4Q1L; METAL 146; /note=Zinc; catalytic; /evidence=ECO:0007744|PDB:4Q1L; METAL 152; /note=Zinc; catalytic; /evidence=ECO:0007744|PDB:4Q1L; METAL 197; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0007744|PDB:4Q1L; METAL 200; /note=Calcium 1; /evidence=ECO:0007744|PDB:4Q1L |
| Rhea ID | |
| Cross Reference Brenda |