| IED ID | IndEnz0002011193 |
| Enzyme Type ID | protease011193 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like BjussuMP-1 EC 3.4.24.- BjussuMP-I Snake venom metalloproteinase SVMP Fragment |
| Gene Name | |
| Organism | Bothrops jararacussu (Jararacussu) |
| 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 jararacussu (Jararacussu) |
| Enzyme Sequence | EFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGRQITTYPPVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTETNWEYEEPIKKASKLVVTAEQQKFPYRYVEIVVVVDRRMVTKYNGDLKKIRKWVYELVNIVNNIYRSLNVHVALVGLEIWSKGDKITVQPDSDYTLNSFGEWRERDLLPRKKHDNAQLLTAVVFDGPTIGRAYIAGMCDPRHSVGVVMDHSKENLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMASVLSVVLSYEFSDCSQNQYQTYLTKHNPQCILNEPLLTVSGNELLEAGEECDCGAPENPCCDAATCKLRPGAQCAEGLCCDQCRFKGAGKICRRARGDNPDDRCTGQSADCPRNRFHRNGQPCLYNHGYCYNGKCPIMFYQCYFLFGSNATVAEDDCFNNNKKGDKYFYCRKENEKYIPCAQEDVKCGRLFCDNKKYPCHYNYSEDLDFGMVDHGTKCADGKVCSNRQCVDVNEAYKSTTVFSLI |
| Enzyme Length | 547 |
| Uniprot Accession Number | Q1PHZ4 |
| Absorption | |
| Active Site | ACT_SITE 278; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by EDTA, EGTA, 1,10-phenanthroline, and partially by beta-mercaptoethanol. Is not inhibited by aprotinin and leupeptin. {ECO:0000269|PubMed:15246772}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This protein is a zinc metalloprotease from snake venom that causes hemorrhage in mice after intradermal injection. It inhibits platelet aggregation induced by collagen and ADP. Has moderate edema activity, but no myotoxic activity. It hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrinogen, without affecting the gamma-chains. It also shows proteolytic activity on casein. It is unable to clot plasma. It also shows bactericidal activity against E.coli and S.aureus. {ECO:0000269|PubMed:15246772, ECO:0000269|PubMed:17081786}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:15246772}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-8.0. {ECO:0000269|PubMed:15246772}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (14); Domain (2); Glycosylation (2); Metal binding (13); Non-terminal residue (1); Propeptide (1); Sequence conflict (2) |
| Keywords | Antibiotic;Antimicrobial;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,985 |
| Kinetics | |
| Metal Binding | METAL 144; /note=Calcium 1; /evidence=ECO:0000250; METAL 228; /note=Calcium 1; /evidence=ECO:0000250; METAL 277; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 281; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 287; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 332; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 335; /note=Calcium 1; /evidence=ECO:0000250; METAL 341; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 344; /note=Calcium 2; /evidence=ECO:0000250; METAL 346; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 348; /note=Calcium 2; /evidence=ECO:0000250; METAL 351; /note=Calcium 2; /evidence=ECO:0000250; METAL 354; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |