| IED ID | IndEnz0002013329 |
| Enzyme Type ID | protease013329 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like brevilysin H2a EC 3.4.24.- Snake venom metalloproteinase SVMP |
| 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 | QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGKPCQNNAGYCYNGKCPIMLNQCISFYGSNATVAPDICFNYNLKGEGNFYCRKEQATIFPCAQKDKKCGRLFCVLGPTGKRISCKNTYSEDDPNYGMVDLGTKCEDGKVCNSNRECVDVNTAY |
| Enzyme Length | 424 |
| Uniprot Accession Number | P0DM89 |
| Absorption | |
| Active Site | ACT_SITE 146; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Its proteolytic activity is inhibited by EDTA, TPEN, 1,10-phenanthroline, and some thiol compounds, but is enhanced by alkaline earth metal ions (Mg2+, Ca2+, Sr2+, and Ba2+). Its activity is not modulated by urea (4 M). {ECO:0000269|Ref.1}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Non-hemorrhagic metalloproteinase that degrades fibrinogen. The alpha chain (FGA) is rapidly degraded, the beta chain (FGB) is degraded very slowly, while the gamma chain is left intact. Shows a prefential cleavage at X-Leu bonds. Cleaves insulin B chain at '29-His-|-Leu-30', '33-Ser-|-His-34', '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. {ECO:0000269|Ref.1}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (3); Metal binding (15); Modified residue (1); Motif (1); Sequence uncertainty (2) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|Ref.1 |
| Post Translational Modification | PTM: Glycosylated (Ref.1). {ECO:0000269|Ref.1}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 279..281; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 46,785 |
| Kinetics | |
| Metal Binding | METAL 96; /note=Calcium 1; /evidence=ECO:0000250; METAL 145; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 149; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 155; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 202; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 205; /note=Calcium 1; /evidence=ECO:0000250; METAL 217; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 220; /note=Calcium 2; /evidence=ECO:0000250; METAL 222; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 224; /note=Calcium 2; /evidence=ECO:0000250; METAL 227; /note=Calcium 2; /evidence=ECO:0000250; METAL 230; /note=Calcium 2; /evidence=ECO:0000250; METAL 281; /note=Calcium 3; /evidence=ECO:0000250; METAL 284; /note=Calcium 3; /evidence=ECO:0000250; METAL 296; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |