| IED ID | IndEnz0002011047 |
| Enzyme Type ID | protease011047 |
| Protein Name |
Snake venom metalloproteinase fibrolase SVMP EC 3.4.24.72 Fibrinolytic metalloproteinase Fibrinolytic proteinase Alfimeprase |
| Gene Name | |
| Organism | Agkistrodon contortrix contortrix (Southern copperhead) |
| 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) Agkistrodon Agkistrodon contortrix (Copperhead) Agkistrodon contortrix contortrix (Southern copperhead) |
| Enzyme Sequence | QQRFPQRYVQLVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIQFTLVGLEIWSNQDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKHSTGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMAAMLSDQPSKLFSDCSKKDYQTFLTVNNPQCILNKP |
| Enzyme Length | 203 |
| Uniprot Accession Number | P28891 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited by EDTA, o-phenanthroline and tetraethylenepentamine. {ECO:0000269|PubMed:1898066}. |
| 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: Snake venom zinc metalloprotease that exhibits direct fibrinolytic activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (3); Modified residue (1); Natural variant (3) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Pharmaceutical;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1304358, ECO:0000269|PubMed:1898066}. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:1304358 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,908 |
| Kinetics | |
| Metal Binding | METAL 143; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 147; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 153; /note=Zinc; catalytic; /evidence=ECO:0000305 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.72; |