| IED ID | IndEnz0002012279 |
| Enzyme Type ID | protease012279 |
| Protein Name |
Snake venom metalloproteinase BaP1 SVMP EC 3.4.24.- Hemorrhagic metalloproteinase BaP1 Bap-1 |
| Gene Name | |
| Organism | Bothrops asper (Terciopelo) |
| 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 asper (Terciopelo) |
| Enzyme Sequence | MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTELPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGRKIITYPSFEDHCYYHGRIENDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTETNWESYEPIKKASQSNLTPEQQRFSPRYIELAVVADHGIFTKYNSNLNTIRTRVHEMLNTVNGFYRSVDVHAPLANLEVWSKQDLIKVQKDSSKTLKSFGEWRERDLLPRISHDHAQLLTAVVFDGNTIGRAYTGGMCDPRHSVGVVRDHSKNNLWVAVTMAHELGHNLGIHHDTGSCSCGAKSCIMASVLSKVLSYEFSDCSQNQYETYLTNHNPQCILNKPLLTVSGNELLEAGE |
| Enzyme Length | 408 |
| Uniprot Accession Number | P83512 |
| Absorption | |
| Active Site | ACT_SITE 335 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, partially inhibited by o-phenantropine, and not inhibited by PMSF, pepstatin A, and aprotinin. {ECO:0000269|PubMed:20600221, ECO:0000269|PubMed:7778126}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloprotease that exhibits a weak hemorrhagic activity (with a minimum hemorrhagic dose of 20 ug by intradermal and intramuscular injection into mice). The basal membrane components collagen (all chains of type IV) (COL4A4), laminin and nidogen are all degraded by this toxin (PubMed:23385358). Rapidly degrades the Aalpha-chain (FGA) of fibrinogen, and later on, degrades the Bbeta-chain (FGB) of fibrinogen (PubMed:7778126). Also activates the complement system, and induces rat neutrophil chemotaxis (PubMed:11200361). Induces edema in mouse food pad and a mild myotoxicity (PubMed:7778126). {ECO:0000269|PubMed:11200361, ECO:0000269|PubMed:20600221, ECO:0000269|PubMed:23385358, ECO:0000269|PubMed:7778126}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:7778126}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Chain (1); Disulfide bond (3); Domain (1); Helix (8); Metal binding (3); Modified residue (1); Propeptide (2); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Chemotaxis;Complement system impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:14500885 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1ND1; 2W12; 2W13; 2W14; 2W15; |
| Mapped Pubmed ID | 19485419; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,936 |
| Kinetics | |
| Metal Binding | METAL 334; /note=Zinc; catalytic; METAL 338; /note=Zinc; catalytic; METAL 344; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda |