| IED ID | IndEnz0002013239 |
| Enzyme Type ID | protease013239 |
| Protein Name |
Zinc metalloproteinase recombinant fibrinogenase II FIIa rF II EC 3.4.24.- Snake venom metalloproteinase SVMP Fragment |
| Gene Name | |
| Organism | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| 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) Deinagkistrodon Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| Enzyme Sequence | KREAEANRTPEQQIYDPYKYVETVFVVDKAMVTKYNGDLDKIKTRMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTYLLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEPLGTDIISPPLCGNELLEA |
| Enzyme Length | 233 |
| Uniprot Accession Number | A2TK72 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF and EDTA. Slightly inhibited by Cu(2+) and Zn(2+). Not inhibited by aprotinin, SBTI, Ca(2+), Mg(2+), Na(+) and K(+). {ECO:0000269|PubMed:19013210}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that acts at several levels. It has direct fibrino(geno)lytic activity (Aalpha chain of fibrinogen is cleaved quickly, Bbeta chain slowly, and gamma chain even more slowly) and degradation of TNF-alpha. These activities permit to protect against sepsis and disseminated intravascular coagulation (PubMed:18634754, PubMed:17964518, PubMed:19013210, PubMed:19070354). It inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50)=65.4 ug/ml) (PubMed:19013210). It decreases the activity of complement by degrading human C5, C6 and C9 in vitro, decreasing serum levels of C1q, C3 and C4 in rat, and inhibiting the MAC deposition on HUVECs membrane. This inhibition of complement protects against hyperacute rejection that is the main barrier in xenotransplantation (PubMed:23178656). Has preference for Lys at the P1 position. Cleaves insulin B chain at '36-Val-|-Glu-37', '39-Leu-|-Tyr-40', and '48-Phe-|-Phe-49' bonds. Also cleaves fibronectin and type IV collagen (PubMed:19013210). {ECO:0000269|PubMed:17964518, ECO:0000269|PubMed:18634754, ECO:0000269|PubMed:19013210, ECO:0000269|PubMed:19070354, ECO:0000269|PubMed:23178656}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-50 degrees Celsius. {ECO:0000269|PubMed:19013210}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-10.5. {ECO:0000269|PubMed:19013210}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Metal binding (10); Non-terminal residue (2) |
| Keywords | Calcium;Complement system impairing toxin;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9W6M5}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,713 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=538.2 uM for N-(p-Tosyl)-Gly-Pro-Lys-pNA {ECO:0000269|PubMed:19013210}; |
| Metal Binding | METAL 22; /note=Calcium 1; /evidence=ECO:0000250; METAL 106; /note=Calcium 1; /evidence=ECO:0000250; METAL 155; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 159; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 165; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 210; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 213; /note=Calcium 1; /evidence=ECO:0000250; METAL 228; /note=Calcium 2; /evidence=ECO:0000250; METAL 230; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 232; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B39; |