| IED ID | IndEnz0002011557 |
| Enzyme Type ID | protease011557 |
| Protein Name |
Thrombin-like enzyme AhV_TL-I SVTLE AhV_TL-I EC 3.4.21.- |
| Gene Name | |
| Organism | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
| 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) Gloydius Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
| Enzyme Sequence | IIGGDECNINEHRFLVALYTSRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSKHIAPFSLPSSPPSVGSVCRIMGWGRISPTEGTYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCKGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP |
| Enzyme Length | 238 |
| Uniprot Accession Number | I4CHP3 |
| Absorption | |
| Active Site | ACT_SITE 43; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 88; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 184; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF, L-cysteine and partially by SBTI and leupeptin. {ECO:0000269|PubMed:23052203}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like enzyme that shows fibrinogenolytic activity against both the Aalpha (FGA) and Bbeta (FGB) chains of bovine fibrinogen. This enzyme has poor esterolytic activity upon BAEE substrate. It induces mouse thoracic aortic ring contraction with EC(50)=147 nmol/L. It shows vasoconstrictor effects that are independent of the enzymatic activity, but related to the release of calcium ions form the calcium store, potentially through the activation of ryanodine receptors. {ECO:0000269|PubMed:23052203}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Erroneous initiation (1); Glycosylation (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23052203}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated at Asn-81 by a disaccharide composed of two N-acetylglucosamine (NAG). The presence of this N-glycan deforms the enzyme and Removing the carbohydrate moiety increases the esterase activity, but induces a complete loss of contractile response on mouse thoracic aorta. {ECO:0000269|PubMed:23052203}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4E7N; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,387 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |