| IED ID | IndEnz0002013481 |
| Enzyme Type ID | protease013481 |
| Protein Name |
Snake venom metalloproteinase atroxase SVMP EC 3.4.24.43 Nonhemorrhagic metalloprotease atroxase |
| Gene Name | |
| Organism | Crotalus atrox (Western diamondback rattlesnake) |
| 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) Crotalus Crotalus atrox (Western diamondback rattlesnake) |
| Enzyme Sequence | EDQQNLSQRYIELVVVADHRVFMKYNSDLNIIRKRVHELVNTINGFYRSLNIDVSLTDLEIWSDQDFITVDSSAKNTLNSFGEWREADLLRRKSHDHAQLLTAINFEGKIIGRAYTSSMCNPRKSVGIXKDHSPINLLVGVTMAHELGHNLGMNHDGEKCLRGASLCIMRPGLTPGRSYEFSDDSMGYYQSFLKQYNPQIXNK |
| Enzyme Length | 203 |
| Uniprot Accession Number | Q91401 |
| Absorption | |
| Active Site | ACT_SITE 146; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and alpha2-macroglobulin. {ECO:0000269|PubMed:3167016}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of 5-His-|-Leu-6, 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain.; EC=3.4.24.43; |
| DNA Binding | |
| EC Number | 3.4.24.43 |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that has Aalpha, Bbeta fibrin(ogen)olytic activities. It cleaves the Aalpha chain of fibrinogen first followed by the Bbeta chain and shows no effect on the gamma chain. Does not induce or inhibit platelet aggregation, and is unable to activate plasminogen. Exhibits low lethality when tested on mice. Intravenous administration results in thrombolysis within one hour followed by recanalization. Fibrinogenolytic activity results in a 60% decrease in the rat's plasma fibrinogen level. Histological examination of kidney, liver, heart and lung tissue shows no necrosis nor hemorrhage. {ECO:0000269|PubMed:2646751, ECO:0000269|PubMed:3167016}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:3167016}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:3167016}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (6); Modified residue (1); Sequence conflict (7) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Potassium;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7893150}. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid (Glu); /evidence=ECO:0000250 |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7893150}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,204 |
| Kinetics | |
| Metal Binding | METAL 12; /note=Calcium; /evidence=ECO:0000250; METAL 96; /note=Calcium; /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; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |