| IED ID | IndEnz0002012146 |
| Enzyme Type ID | protease012146 |
| Protein Name |
Snake venom serine protease rhinocerase SVSP EC 3.4.21.- Fragments |
| Gene Name | |
| Organism | Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) |
| 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 Viperinae (vipers) Bitis Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) |
| Enzyme Sequence | VIGGAECDINEHPSLALIYSTSMRFHCAGTLLNQEWVSFTMWDKDIMLIRTLCAGVLEGGKDTCLAHPCAQPLLPAFYTKVFDYIPWIK |
| Enzyme Length | 89 |
| Uniprot Accession Number | P86497 |
| Absorption | |
| Active Site | ACT_SITE 45; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P09872, ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF. Not inhibited by benzamidine. {ECO:0000269|Ref.1}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that cleaves fibrinogen alpha and beta chains (FGA and FGB), but not gamma chains. Exhibits fibrinolytic and kininogenolytic. Preferentially cleaves after Arg and Lys residues. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (4); Domain (1); Non-adjacent residues (3); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Hypotensive agent;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|Ref.1}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 9,978 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80.05 uM for Arg-AMC {ECO:0000269|Ref.1}; KM=20.29 uM for Ala-Leu-Lys-AMC {ECO:0000269|Ref.1}; KM=32.19 uM for Ala-Leu-Arg-AMC {ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |