| IED ID | IndEnz0002012582 |
| Enzyme Type ID | protease012582 |
| Protein Name |
Zinc metalloproteinase leucurolysin-B Leuc-B EC 3.4.24.- Snake venom metalloproteinase SVMP Fragment |
| Gene Name | |
| Organism | Bothrops leucurus (Whitetail lancehead) |
| 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 leucurus (Whitetail lancehead) |
| Enzyme Sequence | DTVLLNRISHDNAQLLAIVFNENVIGKAYTGGMCDPRYSVGVVMDHSPINRLVADTMAHEMGHNLGIHHDTGSCSCGGHSCIMSRVISHQPLQYFSNCSYIEYWDFITKLNPQCILNEPLRTDIVSPPVCGNELLEMGEECDCGSPRNCRDLCCDAATCKLHSWVECESGECCDQCRFIKAGNVCRPPRKECDVAEACTGQSAQCPTDDFKRNGQPCLNNYAYCYQGNCPIMYHQCYALFGSDATMAQDSCFQVNKKGNEYFYCRLENGINIPCAQEDVKCGRLFCHNMKYEQDCNYSDRGMVDNGTKCAEGKVCNSNRQAYQR |
| Enzyme Length | 324 |
| Uniprot Accession Number | P86092 |
| Absorption | |
| Active Site | ACT_SITE 60; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, but not by PMSF. Pre-incubation with 2 mM DTT completely abolishes activity. {ECO:0000269|PubMed:17963685}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that acts as a potent hemorrhagic toxin. Hydrolyzes the insulin B chain at the 14-Ala-|-Leu-15 bond but not the 16-Tyr-|-Leu-17 bond. Degrades the alpha-chain of fibrin and hydrolyzes the Aalpha-chain of fibrinogen (FGA) while leaving the beta and gamma chains unaffected. Degrades type-I collagen and its gelatin. Degrades the alpha-1 chain of type-IV collagen and its gelatin but not the alpha-2 chain. Degrades plasma fibronectin, plasma vitronectin and basement membrane enactin. It inhibits collagen-induced platelet aggregation. {ECO:0000269|PubMed:17963685}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius with dimethyl casein as substrate. {ECO:0000269|PubMed:17963685}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.3 with dimethyl casein as substrate. {ECO:0000269|PubMed:17963685}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (16); Domain (2); Glycosylation (3); Metal binding (12); Motif (1); Non-terminal residue (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17963685}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:17963685}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17963685, ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 191..193; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 36,262 |
| Kinetics | |
| Metal Binding | METAL 11; /note=Calcium 1; /evidence=ECO:0000250; METAL 59; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P30431; METAL 63; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P30431; METAL 69; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P30431; METAL 114; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 117; /note=Calcium 1; /evidence=ECO:0000250; METAL 129; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 132; /note=Calcium 2; /evidence=ECO:0000250; METAL 134; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 136; /note=Calcium 2; /evidence=ECO:0000250; METAL 139; /note=Calcium 2; /evidence=ECO:0000250; METAL 142; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |