| IED ID | IndEnz0002011341 |
| Enzyme Type ID | protease011341 |
| Protein Name |
Snake venom serine protease BPA SVSP EC 3.4.21.- Bothrops protease A BPA |
| Gene Name | |
| Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| 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) Bothrops Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| Enzyme Sequence | MVLIRVIANLLILQLSNAQKSSELVIGGDECNITEHRFLVEIFNSSGLFCGGTLIDQEWVLSAAHCDMRNMRIYLGVHNEGVQHADQQRRFAREKFFCLSSRNYTKWDKDIMLIRLNRPVNNSEHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATFPDVPHCANINLFNYTVCRGAHAGLPATSRTLCAGVLQGGIDTCGGDSGGPLICNGTFQGIVSWGGHPCAQPGEPALYTKVFDYLPWIQSIIAGNTTATCPP |
| Enzyme Length | 258 |
| Uniprot Accession Number | Q9PTU8 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP), but not by SBTI, Antithrombin III/heparin and BPTI, probably due to steric hindrance caused by its huge carbohydrate moietie. {ECO:0000269|PubMed:18433459}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that has a potent and selective fibrinogenolytic activity. Preferentially cleaves the alpha-chain (FGA) of human and rat fibrinogen at Arg-|-Gly bonds, and slowly digests the beta-chain (FGB) (PubMed:18433459). In vivo, completely avoids thrombus formation induced in rat, decreases the fibrinogen plasma level and prolonges the recalcification time. Possesses esterolytic and amidolytic activities. {ECO:0000269|PubMed:14161003, ECO:0000269|PubMed:18433459}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3-9. {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (10); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. The glycosylation has a stabilizing effect on the protein (PubMed:14580991). However, the removal of part of the carbohydrates enhances the proteolytic activity of the SVSP towards human and rat fibrinogen (PubMed:18433459). {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,058 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.94 mM for Bz-Arg-pNa (at pH 3) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.90 mM for Bz-Arg-pNa (at pH 7.2) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.95 mM for Bz-Arg-pNa (at pH 10) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.29 mM for D-Phe-Pip-Arg-pNA {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.31 mM for D-Val-Leu-Arg-pNA {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.53 mM for Tos-Gly-Pro-Arg-pNA {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; KM=0.0 mM for D-Val-Leu-Lys-pNA {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.76 umol/min/mg enzyme with Bz-Arg-pNa as substrate (at pH 3) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.82 umol/min/mg enzyme with Bz-Arg-pNa as substrate (at pH 7.2) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.75 umol/min/mg enzyme with Bz-Arg-pNa as substrate (at pH 10) {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.69 nmol/min/mg enzyme with D-Phe-Pip-Arg-pNA as substrate {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.134 nmol/min/mg enzyme with D-Val-Leu-Arg-pNA as substrate {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.044 nmol/min/mg enzyme with Tos-Gly-Pro-Arg-pNA as substrate {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; Vmax=0.0 nmol/min/mg enzyme with D-Val-Leu-Lys-pNA as substrate {ECO:0000269|PubMed:14580991, ECO:0000269|PubMed:18433459}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |