| IED ID | IndEnz0002012442 |
| Enzyme Type ID | protease012442 |
| Protein Name |
Thrombin-like enzyme barnettobin Bb-TLE SVTLE EC 3.4.21.- Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti) |
| 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 barnetti (Barnett's lancehead) (Trimeresurus barnetti) |
| Enzyme Sequence | APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP |
| Enzyme Length | 249 |
| Uniprot Accession Number | K4LLQ2 |
| Absorption | |
| Active Site | ACT_SITE 56; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 101; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Both coagulant and amidolytic activities are inhibited by PMSF. Amidolytic activity is partially inhibited by DTT, chymostatin, SBTI and TLCK, but not by heparin and EDTA. {ECO:0000269|PubMed:23578498}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that releases only fibrinopeptide A from human Aalpha chain of fibrinogen (specific coagulant activity was 251.7 NIH thrombin units/mg). Also shows fibrino(geno)lytic activities in vitro and defibrinogenating effects in vivo. {ECO:0000269|PubMed:23578498}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23578498}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:23578498}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (3); Non-terminal residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23578498}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycoprotein, contains approx. 52% carbohydrate which could be removed by N-glycosidase. Glycosylation is important, since deglycosylated barnettobin loses its clotting and defibrinogenating effects. {ECO:0000269|PubMed:23578498}. |
| Signal Peptide | SIGNAL <1..10; /evidence=ECO:0000250|UniProtKB:P04971 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,585 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |