| IED ID | IndEnz0005000772 |
| Enzyme Type ID | lipase000772 |
| Protein Name |
Phospholipase A1 verutoxin-2a VT-2a EC 3.1.1.32 EC 3.1.1.5 Fragment |
| Gene Name | |
| Organism | Vespa velutina (Asian yellow-legged 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 velutina (Asian yellow-legged hornet) |
| Enzyme Sequence | FNPCPYSDDTVKMIILTRENKKHDF |
| Enzyme Length | 25 |
| Uniprot Accession Number | P0DMB7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activity is maximal in the presence of calcium. However, unlike phospholipases A2 whose catalytic activity is strictly calcium-dependent, this enzyme shows considerable catalytic activity on phosphatidylcholine emulsified in calcium free solution; the catalytic activity of VT-2a assayed in the absence of calcium ions is 18-20% of that assayed in solution containing calcium ions. {ECO:0000269|PubMed:10484737}. |
| 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:0000269|PubMed:10484737};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000269|PubMed:10484737}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74667, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:10484737};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38788; Evidence={ECO:0000269|PubMed:10484737}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:10484737};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000269|PubMed:10484737}; |
| DNA Binding | |
| EC Number | 3.1.1.32; 3.1.1.5 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of glycerophospholipids such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) and has a moderate activity to hydrolyze lysoglycerophospholipids such as lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine), but is unable to hydrolyze sphingomyelin. In addition to acting as allergens, it possesses a potent hemolytic activity on red blood cells of mice (98.8% of hemolysis at 3.0 ug/ml). {ECO:0000269|PubMed:10484737}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:10484737}. |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Allergen;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484737}. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains six disulfide bonds. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,012 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:18689; RHEA:18690; RHEA:38787; RHEA:38788; RHEA:15177; RHEA:15178 |
| Cross Reference Brenda |