IED ID | IndEnz0002007779 |
Enzyme Type ID | protease007779 |
Protein Name |
Acidic phospholipase A2 Vur-PL2B Vur-PL2 svPLA2 EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase |
Gene Name | |
Organism | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
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) Vipera Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
Enzyme Sequence | MRILWIVAVCLIGVEGNLYQFGKMIRYKTGKSALLSYSDYGCYCGWGGQGKPKDATDRCCFVHDCCYGRVNGCDPKLTIYSYSFENGDIVCGGDDSCKRAVCECDRVAAICFGENLNTYDKKYKNYPSSQCTETEQC |
Enzyme Length | 137 |
Uniprot Accession Number | F8QN53 |
Absorption | |
Active Site | ACT_SITE 63; /evidence=ECO:0000250; ACT_SITE 105; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:21185324}; |
DNA Binding | |
EC Number | 3.1.1.4 |
Enzyme Function | FUNCTION: Snake venom phospholipase A2 that causes internal bleeding, shows very strong anticoagulant activities and inhibits ADP-induced platelet aggregation (PubMed:21185324). Shows very low cytotoxicity (PubMed:21185324). Is not able (or very weakly) to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)>30 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is similarly active against T.californica nAChR (IC(50)>100 uM), human alpha-7 nAChR (IC(50)=29 uM), and L.stagnalis AChBP (IC(50)>30 uM) (PubMed:25522251). {ECO:0000269|PubMed:21185324, ECO:0000269|PubMed:25522251}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (7); Metal binding (4); Signal peptide (1) |
Keywords | Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000269|PubMed:21185324 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 15,316 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3592 umol/min/mg enzyme (Vur-PL2B) {ECO:0000269|PubMed:21185324}; Note=Vmax=1736 umol/min/mg enzyme (Vur-PL2A). {ECO:0000269|PubMed:21185324}; |
Metal Binding | METAL 43; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 45; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 47; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 64; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | RHEA:15801 |
Cross Reference Brenda |