Detail Information for IndEnz0005000803
IED ID IndEnz0005000803
Enzyme Type ID lipase000803
Protein Name Phospholipase A1
vPLA2
EC 3.1.1.32
Gene Name
Organism Vespa basalis (Hornet)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Vespoidea Vespidae (wasps) Vespinae (hornets and yellowjackets) Vespa Vespa basalis (Hornet)
Enzyme Sequence FNPCPYSDDTVKMIILTRENKKHDFYTLDTIKKHNEFKKSTIKHQVVFITHGFTSSADTENFLAMAKALSDKGNYLVILIDWRVAACTEEMSGIQLAYYSYAASNTRLVGNYIATVTKMLVQKYNVPMANIRLIGHSLGAHTSGFAGKKVQELGLGKYSEIIGLDPAGPSFKSNDCSERICKTDAHYVQIIHTSNHLGTLVTLGTVDFMNNGYNQPGCGLPLIGETCSHTRAVKYFTECIKHECCLIGVPQSKKPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII
Enzyme Length 300
Uniprot Accession Number A0A0M3KKW3
Absorption
Active Site ACT_SITE 137; /note=Nucleophile; ACT_SITE 165; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 229; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation ACTIVITY REGULATION: Local inflammatory effects are inhibited by antiserotonin drugs (cyproheptadine and methysergide), indomethacin, betamethasone, and antihistamine (chlorpheniramine). {ECO:0000269|PubMed:7687388}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:P0DMB4};
DNA Binding
EC Number 3.1.1.32
Enzyme Function FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (By similarity). Shows potent hemolytic activity that is responsible for its lethal effect (PubMed:26603193). In vivo, induces local inflammatory effects (PubMed:7687388). {ECO:0000250|UniProtKB:P0DMB4, ECO:0000269|PubMed:7687388, ECO:0000305|PubMed:26603193}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (10); Chain (1); Disulfide bond (6); Helix (10); Turn (4)
Keywords 3D-structure;Cytolysis;Disulfide bond;Hemolysis;Hydrolase;Secreted
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7687388}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4QNN;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,185
Kinetics
Metal Binding
Rhea ID RHEA:18689
Cross Reference Brenda