| IED ID | IndEnz0002010044 |
| Enzyme Type ID | protease010044 |
| Protein Name |
Snake venom serine protease LmrSP-4 SVSP EC 3.4.21.- Fragment |
| Gene Name | |
| Organism | Lachesis muta rhombeata (Bushmaster) |
| 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) Lachesis Lachesis muta (South American bushmaster) Lachesis muta rhombeata (Bushmaster) |
| Enzyme Sequence | VFGGDECNINEHRSLVVLFDSDGFLCAGTLINKEWVLTAAHCDSENFQMQLGV |
| Enzyme Length | 53 |
| Uniprot Accession Number | C0HLA3 |
| Absorption | |
| Active Site | ACT_SITE 41; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10078 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the small molecule serine protease inhibitors phenylmethylsulfonyl fluoride (PMSF) and benzamidine. {ECO:0000269|PubMed:31131000}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that has fibrinogenolytic activity. Hydrolyzes the alpha-chain of fibrinogen (FGA), without affecting the beta- and the gamma-chains. Also displays hydrolytic activity towards S-2302 (plasma kalikrein substrate) and S-2251 (substrate for plasmin), but has no hydrolytic activity with S-2238 (thrombin substrate) or S-2222 (factor Xa). {ECO:0000269|PubMed:31131000}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 40 and 55 degrees Celsius (at pH 7). Activity decreases at 60 degrees Celsius. {ECO:0000269|PubMed:31131000}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7-8 (at 40 degrees Celsius). {ECO:0000269|PubMed:31131000}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Non-terminal residue (1) |
| Keywords | 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:31131000}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:31131000}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 5,845 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |