IED ID | IndEnz0005000799 |
Enzyme Type ID | lipase000799 |
Protein Name |
Phospholipase A1 EC 3.1.1.32 allergen Pol g 1 Fragment |
Gene Name | |
Organism | Polistes gallicus (Paper wasp) |
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) Polistinae (paper wasps) Polistini Polistes Polistes gallicus (Paper wasp) |
Enzyme Sequence | GITPDCTFNEKDIELHVYSRDKRNGIILKKEILKNYDLFKES |
Enzyme Length | 42 |
Uniprot Accession Number | P83542 |
Absorption | |
Active Site | |
Activity Regulation | |
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:14572904}; |
DNA Binding | |
EC Number | 3.1.1.32 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 (EC 3.1.1.32) activity (PubMed:14572904). Shows hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB7, ECO:0000269|PubMed:14572904}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (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:14572904}. |
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 | 4,985 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=283.2 umol/min/mg enzyme {ECO:0000269|PubMed:14572904}; |
Metal Binding | |
Rhea ID | RHEA:18689 |
Cross Reference Brenda |