| IED ID | IndEnz0002010866 |
| Enzyme Type ID | protease010866 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase brevilysin L6 SVMP Snake venom metalloproteinase Mt-c EC 3.4.24.- ; Disintegrin |
| Gene Name | |
| Organism | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
| 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) Gloydius Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
| Enzyme Sequence | MIQVLLVIICLADFPYQGTSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKGYSETHYSPDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKHQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQTNWKSDEPIKASQQQRFPQRYIELVVVADHGMFTKYDSNLDTIRTWVHELVNSINEFYRSLNIDVSLTELEIWSNQDLINVQSAAGDTLEAFGDWRETDLLNRISHDNAQLLTATELDGNTIGLAHVASMCDPKRSTGVVQDHSAINLLVAVTMAHETGHNLGMNHDGNQCHCGANSCVMGDVLSEGVSYEFSDCSENEYQTYLTDRNPQCILNEPLRTDTVSTPVSGNELLEAGKECDCGAPANPCCDAETCKLRPGQQCAEGLCCDQCRFMKEGTICQEAKGDWNDDTCNGISAGCPRNGFYG |
| Enzyme Length | 476 |
| Uniprot Accession Number | Q9YI19 |
| Absorption | |
| Active Site | ACT_SITE 328; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
| Activity Regulation | ACTIVITY REGULATION: The metalloproteinase is inhibited by EDTA, o-phenanthroline, and cysteine. Glutathione does not inhibit the enzymatic activity. {ECO:0000269|PubMed:9880798}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Snake venom metalloproteinase brevilysin L6]: Shows weak degradation of alpha-fibrinogen, but has no activity on beta- and gamma-chains. Digests luteinizing hormone-releasing hormone (LH-RH) and oxidized insulin at X-Leu, X-Phe, and X-Val bonds as well as X-His bond. Does not show fibrinogen-clotting activity. Does not show hemorrhagic activity. {ECO:0000269|PubMed:9880798}.; FUNCTION: [Disintegrin]: Inhibits ADP-induced platelet aggregation. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 9. {ECO:0000269|PubMed:9880798}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (7); Domain (2); Metal binding (7); Modified residue (1); Motif (1); Propeptide (2); Sequence conflict (5); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 185; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:9880798 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 454..456; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 52,802 |
| Kinetics | |
| Metal Binding | METAL 194; /note=Calcium; /evidence=ECO:0000250; METAL 278; /note=Calcium; /evidence=ECO:0000250; METAL 327; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 331; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 382; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 385; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |