| IED ID | IndEnz0002011946 |
| Enzyme Type ID | protease011946 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like acurhagin Acur EC 3.4.24.- Acutolysin e2 Snake venom metalloproteinase SVMP Zinc metalloproteinase-disintegrin-like acutolysin-E |
| 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 | MIQVLLVTICLAAFPYQGSSIILESGDVNDYEVVYPRKVTALPKGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKHLFSKDYSETHYSPDGREITINPPVEDHCYYHGRIENDGDSTASISACNGLKGNFKLQGETYLIEPMKLSDSEAHAVFKYENVEKEDEAPKMCGVTQKWKSYEPIKKISQLNLIPEQQIYDPFKYVETVVVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTYLLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEPLGTDIISPPLCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPADVFHKNGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFESNKKGNYYGYCRKENGKKIPCASEDVKCGRLYCKDDSPGQNNPCKMFYSNDDEHKGMVLPGTKCADGKVCSNGHCVDVTTAY |
| Enzyme Length | 610 |
| Uniprot Accession Number | Q9W6M5 |
| Absorption | |
| Active Site | ACT_SITE 335; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: The proteinase activity is slightly enhanced by Ca(2+) and Mg(2+), but is completely inhibited by Zn(2+). Is completely inhibited by phenanthroline and EDTA. Not inhibited by PMSF. {ECO:0000269|PubMed:12008947, ECO:0000269|PubMed:16023283}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that causes hemorrhage and dose-dependently inhibits platelet aggregation triggered by collagen. This inhibition is due to its binding to glycoprotein VI (GP6) and collagen. The binding to GP6 results in inhibition of the signaling pathway (decrease of tyrosine phosphorylation of signaling proteins such as Syk, LAT, PI3-K and PLCgamma2). Preferentially cleaves alpha chain (FGA) of fibrinogen, followed by beta chain (FGB). Also degrades the extracellular matrix protein fibronectin (FN1), and cleaves collagen and von Willebrand factor (VWF). {ECO:0000269|PubMed:12008947, ECO:0000269|PubMed:16023283}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (1); Metal binding (17); Modified residue (1); Motif (1); Propeptide (1); Sequence conflict (9); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: N-glycosylated. |
| 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 | 68,542 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for NFF-2 (fluorogenic substrates with cleavage at Ala-Nva) {ECO:0000269|PubMed:18554518}; |
| 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 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 |