| IED ID | IndEnz0002012300 |
| Enzyme Type ID | protease012300 |
| Protein Name |
Chymotrypsin-like protease VLCTLP EC 3.4.21.- Snake venom serine protease SVSP Vipera Lebetina with chymotrypsin-like proteolytic activity |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MVLIRVLANLLLLQLSYAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQQWVLSAAHCDMENVQIYLGLHNLRLRNQDEQIRVAEEKFFCLSNKSYTKWDKDIMLIRLNSSVTYNTHIAPLSLPSSPPRVGSVCRIMGWGAITSPNETFPNVPHCANINILRYSVCRAAYRGLPAQSRTLCAGILQGGIGSCMGDSGGPLICNGEIQGIVSWGDDICAQPHKPVHYTKVFDYSDWIQSIIAGNTTATCPL |
| Enzyme Length | 257 |
| Uniprot Accession Number | E0Y421 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 203; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:20950666}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease with tyrosine-specific chymotrypsin-like activity. Hydrolyzes the N-acetyl-L-tyrosine ethyl ester (ATEE). Has weak fibrinogenolytic activity. Weakly hydrolyzes azocasein, Aalpha-chain (FGA) and more slowly Bbeta-chain (FGB) of fibrinogen. Optimal substrates are angiotensins I and II (AGT). {ECO:0000269|PubMed:20950666}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (5); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Partial deglycosylation has not effect on enzyme activity. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,278 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |