Detail Information for IndEnz0002007779
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