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http://purl.uniprot.org/citations/8119970http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8119970http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8119970http://www.w3.org/2000/01/rdf-schema#comment"Lysophospholipase transacylase was purified 214,360-fold to homogeneity from the rat liver 100,000 x g supernatant. After DEAE chromatography, total activity increased 12.9-fold, due to the removal of endogenous inhibitors. The inhibitors were isolated and identified as phosphatidic acid and fatty acid. The final preparation showed a single band on SDS-polyacrylamide electrophoresis with an M(r) of 60,000. Gel filtration through Sephacryl S-200 gave a similar value, suggesting that the enzyme exists as a monomer. Activity was highest at pH 6.0 and was not affected by Ca2+, Mg2+, and EDTA. The enzyme produced glycerophosphocholine (GPC), palmitic acid, and dipalmitoyl-GPC on incubation with 1-palmitoyl-GPC, indicating that the enzyme catalyzed both deacylation and transacylation. The relative rates of deacylation and transacylation were 1:0.3 under standard assay conditions. Km for 1-palmitoyl-GPC and Vmax of hydrolase activity were 91 microM and 12.9 mumol/min/mg, respectively. The enzyme was selective for choline lysophospholipid. Ethanolamine, inositol, and serine lysophospholipids were not good substrates of the enzyme. Phosphatidic acid was a potent, competitive inhibitor of the enzyme with Ki of about 10 microM as determined with 1-stearoyl-2-arachidonoyl glycerophosphate. Although less potent, lysophosphatidic acid, palmitoyl-L-carnitine, and fatty acid were also inhibitory to the enzyme."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)37595-6"xsd:string
http://purl.uniprot.org/citations/8119970http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)37595-6"xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/author"Yamashita S."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/author"Yamashita S."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/author"Sugimoto H."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/author"Sugimoto H."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/pages"6252-6258"xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/pages"6252-6258"xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/title"Purification, characterization, and inhibition by phosphatidic acid of lysophospholipase transacylase from rat liver."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/title"Purification, characterization, and inhibition by phosphatidic acid of lysophospholipase transacylase from rat liver."xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/8119970http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/8119970http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8119970
http://purl.uniprot.org/citations/8119970http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8119970
http://purl.uniprot.org/citations/8119970http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8119970
http://purl.uniprot.org/citations/8119970http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8119970
http://purl.uniprot.org/uniprot/O88202http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8119970
http://purl.uniprot.org/uniprot/O88202#attribution-346DA1FDED6396F3271913C9C5B3981Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8119970