| http://purl.uniprot.org/citations/1577711 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1577711 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1577711 | http://www.w3.org/2000/01/rdf-schema#comment | "The major phospholipase A2 activity in sheep platelets is mediated by at least three chromatographically resolvable isoforms of a 30-kDa dimeric polypeptide which are responsive to physiologic increments in calcium ion and possess a dramatic substrate selectivity (Loeb, L. A., and Gross, R. W. (1986) J. Biol. Chem. 261, 10467-10470). Herein, we describe the cloning and expression of the human equivalent of one such isoform and demonstrate that it catalyzes the cleavage of the sn-2 fatty acid of choline and ethanolamine glycerophospholipids through the formation of a stable acyl-enzyme intermediate. Transesterification of the sn-2 acyl group of phosphatidylcholine to the recombinant 30-kDa polypeptide is over 50-fold selective for arachidonic acid, is augmented by calcium ion, and results in the formation of an arachidonoyl-thioester intermediate. Homology analysis demonstrated that the polypeptide mediating this transesterification is one member of a family of proteins collectively designated as 14-3-3 proteins. These results demonstrate that at least one intracellular mammalian phospholipase A2 employs a catalytic strategy distinct from that utilized by extracellular phospholipases A2 (i.e. formation of an acyl-enzyme intermediate by nucleophilic attack versus activation of a water molecule) and that arachidonic acid in endogenous phospholipid storage depots can, in principle, be sequentially transferred through an acyl-enzyme intermediate without the prior obligatory release of free arachidonic acid."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)50334-9"xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)50334-9"xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Berry C.A."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Berry C.A."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Gross R.W."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Gross R.W."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Landt M.L."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Landt M.L."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Steffens D.L."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Steffens D.L."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Zupan L.A."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/author | "Zupan L.A."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/pages | "8707-8710"xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/pages | "8707-8710"xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/title | "Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/title | "Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis."xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1577711 | http://purl.uniprot.org/core/volume | "267"xsd:string |