| IED ID | IndEnz0002010312 |
| Enzyme Type ID | protease010312 |
| Protein Name |
Snake venom metalloproteinase fibrolase SVMP EC 3.4.24.72 Fibrinolytic proteinase Non-hemorrhagic fibrinolytic metalloproteinase VlF |
| 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 | ERFAPRYIELVIVADHSVATKYNDNVTAILSWVHQLVNNIILFYRDLNVHFTLSAVEVWSNGDLINVQPEATVTLNLFGEWRERDLLNRRMHDNAQLLNNVALDDNTIGLAYDEGMCDPKYSVGIVKDHSAINRMVAATMAHEIGHNLGMNHDGSQCNCGGNGCVMSAVLMQQHSYQFSDCSKDEYQRYLTNHNPQCILNQP |
| Enzyme Length | 202 |
| Uniprot Accession Number | P83255 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium and magnesium ions. Inhibited by EDTA, DTT and L-cysteine. Activity is not affected by PMSF or heparin. {ECO:0000269|PubMed:1926182}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of 14-Ala-|-Leu-15 in insulin B chain and 413-Lys-|-Leu-414 in alpha-chain of fibrinogen.; EC=3.4.24.72; |
| DNA Binding | |
| EC Number | 3.4.24.72 |
| Enzyme Function | FUNCTION: Has fibrino(geno)lytic activity on the alpha and beta chains of fibrinogen (FGA and FGB). Inhibits human ADP- and collagen-induced platelet aggregation on platelet-rich plasma but does not affect the thrombin-induced aggregation of rabbit washed platelets. Slightly degrades plasminogen. {ECO:0000269|PubMed:1926182, ECO:0000269|PubMed:9175244}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Metal binding (7) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Magnesium;Metal-binding;Metalloprotease;Plasminogen activation;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:1926182}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,851 |
| Kinetics | |
| Metal Binding | METAL 9; /note=Calcium; /evidence=ECO:0000250; METAL 93; /note=Calcium; /evidence=ECO:0000250; METAL 142; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 146; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 152; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 197; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 200; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |