| IED ID | IndEnz0002010886 |
| Enzyme Type ID | protease010886 |
| Protein Name |
Snake venom metalloproteinase lebetase-4 Le-4 Le4 EC 3.4.24.- Fragment |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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 Viperinae (vipers) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | SCRKKASQLNLTPEQQRFDPRYIELVIVADHSMVTKYDGDLAAIRTWAHQLVNNIIVFYRDLNVHITLSAVEVWTNGDLINVQPAASVTLNLFGEWRERDLLNRRMHDHAQLLTAINLDDNTIGLAYNEGMCDPKYSVGIVQDHSAINRMVAATMAHEIGHNLGMDHDGNQCNCGANGCVMSAVITQQRSYQFSDCSKNKYQTYLTNHNPQCILNQP |
| Enzyme Length | 217 |
| Uniprot Accession Number | Q3ZD74 |
| Absorption | |
| Active Site | ACT_SITE 158; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Fibrinolytic and caseinolytic activities are inhibited by Cd(2+), Cu(2+) and Co(2+) ions. Not inhibited by Mg(2+), Ca(2+) and Ba(2+). Also inhibited by EDTA, EGTA and 1,10-phenanthroline (By similarity). {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen. Also hydrolyzes casein and B-chain of oxidized insulin. Its fibrinolytic activity is direct, without any plasminogen activation. Inhibits ADP-induced and collagen-induced platelet aggregation. Shows low hemorrhagic activity. Cleaves the plasma proteinase inhibitors alpha(2)-macroglobulin (A2M) and alpha(2)M-related pregnancy zone protein (PZP), and is inhibited by them (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (7); Modified residue (1); Non-terminal residue (1); Propeptide (1) |
| Keywords | Calcium;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 15; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,487 |
| Kinetics | |
| Metal Binding | METAL 24; /note=Calcium; /evidence=ECO:0000250; METAL 108; /note=Calcium; /evidence=ECO:0000250; METAL 157; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 161; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 167; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 212; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 215; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |