| IED ID | IndEnz0002012123 |
| Enzyme Type ID | protease012123 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like brevilysin H6 Mt-a EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: p45K; Disintegrin-like p29K |
| 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 | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLGKNKQLFSKDYSETHYSPDGREITTNPPVEDHCYYHGRIENDADSTRSISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENILKEDEAPKMCGVTQNWESYEPIKKASQLNLTPEQQRYNPFRFVELVLVADKGMVTKNNGDLNKIKTRMYELANNLNDIYRYMYIHVALVGVEIWSDGDKITVTPNVDDTLSSFAEWRKTHLLTRKKHDNAQLLTAIDFNGPTIGYAYIASMCHPKRSVGIVQDYSPINLVLSVVMAHEMGHNLGIHHDHSYCSCGDYACIMGATISHEPSTFFSNCSYIQCWDFIMDHNPECIVNEPLGTDIVSPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRESMSECDPAEHCTGQSSECPADVFHKNGQPCLHNYGYCYNGNCPIMYHQCYALWGADVYEAEDSCFESNKKGNYYGYCRKENGKKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCGDGKVCSNGHCVDVATAY |
| Enzyme Length | 610 |
| Uniprot Accession Number | P0C7B0 |
| Absorption | |
| Active Site | ACT_SITE 335; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by chelating agents. Calcium ions enhance its activity, they also suppress autoproteolysis, and contribute to the stability of the enzyme against pH, heating, urea and cysteine. {ECO:0000269|PubMed:10920250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Shows weak hemorrhagic activity. Rapidly degrades the alpha-chain of fibrinogen (FGA). {ECO:0000269|PubMed:10920250}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The activity is markedly reduced above 40 degrees Celsius. Calcium ions increases the thermal stability by 10 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8 in the absence of calcium ions. Optimum pH is 5.6-8.5 in the presence of calcium ions.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (3); Disulfide bond (26); Domain (2); Glycosylation (1); Metal binding (18); Modified residue (1); Motif (1); Propeptide (1); Sequence conflict (9); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10920250}. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:10920250 |
| Post Translational Modification | PTM: In the absence of calcium ions, is autocatalytically degraded giving 29 (p29K) and 45 kDa (p45K) fragments. In presence of calcium ions, the p45K is not detected (PubMed:10920250). {ECO:0000269|PubMed:10920250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 466..468; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,218 |
| Kinetics | |
| Metal Binding | METAL 201; /note=Calcium 1; /evidence=ECO:0000250; METAL 285; /note=Calcium 1; /evidence=ECO:0000250; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 389; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 392; /note=Calcium 1; /evidence=ECO:0000250; METAL 404; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 407; /note=Calcium 2; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; /evidence=ECO:0000250; METAL 414; /note=Calcium 2; /evidence=ECO:0000250; METAL 417; /note=Calcium 2; /evidence=ECO:0000250; METAL 468; /note=Calcium 3; /evidence=ECO:0000250; METAL 469; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 471; /note=Calcium 3; /evidence=ECO:0000250; METAL 483; /note=Calcium 3; /evidence=ECO:0000250; METAL 484; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |