| IED ID | IndEnz0002011819 |
| Enzyme Type ID | protease011819 |
| Protein Name |
Snake venom metalloproteinase ACLF SVMP EC 3.4.24.- ACLF-I Metalloproteinase VMP-I AclVMP-I |
| Gene Name | ACLPREF |
| Organism | Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| 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 laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| Enzyme Sequence | MIQVLLVTLCLAAFPYQGSSIILESGNVNDYEVVYPRKVTPVPRGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLELSDSEAHAVYKYENVEKEDEAPKMCGVTQNWESYEPIKKAFQLNLTPEQQGFPQRYVELVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIRFALVGLEIWSNQDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKHSTGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMPSVLSDQPSKLFSDCSKKDYQTFLPVNNPQCILNKPLRTDTASTPVSGNELLEA |
| Enzyme Length | 411 |
| Uniprot Accession Number | Q92031 |
| Absorption | |
| Active Site | ACT_SITE 334; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline, but not by PMSF. {ECO:0000269|PubMed:10833388, ECO:0000269|PubMed:12651104}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that has fibrinolytic activity. The recombinant enzyme cleaves both alpha- and beta-chains of fibrinogen, but not the gamma-chain. The recombinant protein does not produce hemorrhage in mice. Cleaves the peptide substrate Abz-LVEALYQ-EDDnp at the Ala-Leu bond in vitro (PubMed:12651104). {ECO:0000269|PubMed:10833388, ECO:0000269|PubMed:12651104}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (11); Propeptide (1); Sequence conflict (6); Signal peptide (1) |
| Keywords | Calcium;Disulfide bond;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,231 |
| Kinetics | |
| Metal Binding | METAL 200; /note=Calcium 1; /evidence=ECO:0000250; METAL 284; /note=Calcium 1; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 388; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 391; /note=Calcium 1; /evidence=ECO:0000250; METAL 403; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 406; /note=Calcium 2; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 410; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |