| IED ID | IndEnz0002010107 |
| Enzyme Type ID | protease010107 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like leucurogin EC 3.4.24.- Snake venom metalloproteinase SVMP Fragment |
| 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 | LGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSECGHGDCCEQCKFTKSGTECRASMSECDPAEHCTGQSSECPADVGHK |
| Enzyme Length | 93 |
| Uniprot Accession Number | P0DJ87 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that possesses hemorrhagic activity (By similarity). The disintegrin-like domain has been expressed and named leucurogin. This recombinant disintegrin is able to inhibit collagen-induced platelet aggregation but not ADP- or arachidonic acid-induced platelet aggregation. In addition, this disintegrin has been observed to inhibit the growth of experimental Ehrlich tumor and to have anti-angiogenesis effect on the sponge implant model. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (7); Domain (1); Metal binding (11); Motif (1); Non-terminal residue (2); Region (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 72..74; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 9,710 |
| Kinetics | |
| Metal Binding | METAL 10; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 13; /note=Calcium 1; /evidence=ECO:0000250; METAL 15; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 17; /note=Calcium 1; /evidence=ECO:0000250; METAL 20; /note=Calcium 1; /evidence=ECO:0000250; METAL 23; /note=Calcium 1; /evidence=ECO:0000250; METAL 74; /note=Calcium 2; /evidence=ECO:0000250; METAL 75; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 77; /note=Calcium 2; /evidence=ECO:0000250; METAL 89; /note=Calcium 2; /evidence=ECO:0000250; METAL 90; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |