| IED ID | IndEnz0010001815 |
| Enzyme Type ID | esterase001815 |
| Protein Name |
Thrombin-like enzyme acutobin-2 SVTLE EC 3.4.21.- Acutobin II Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| 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) Deinagkistrodon Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
| Enzyme Sequence | VIGGVECDINEHRFL |
| Enzyme Length | 15 |
| Uniprot Accession Number | P0DJG7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF (100%), AEBSF (100%), aprotinin (50%), benzamidine (50%), guanidinium chloride (48%) and urea (66%). {ECO:0000269|PubMed:18643779}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that has high fibrinogen-clotting activity (2025 NIH units/mg) on human fibrinogen. Shows esterase and amidase activities. {ECO:0000269|PubMed:17904430}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-50 degrees Celsius (at pH 7.0). {ECO:0000269|PubMed:18643779}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (at 25 degrees Celsius). {ECO:0000269|PubMed:18643779}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Seems to be only O-glycosylated (is not affected by PNGase F which only removes N-linked glycans, but is affected by TFMS that removes both O- and N-linked glycans). |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,701 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=403 uM for BAEE (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:18643779}; KM=68.5 nM for DL-BAPA (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:18643779}; Vmax=1560 nmol/sec/mg enzyme (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:18643779}; Vmax=490 nmol/min/mg enzyme with DL-BAPA as substrate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:18643779}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |