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http://purl.uniprot.org/citations/6498208http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6498208http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6498208http://www.w3.org/2000/01/rdf-schema#comment"In Dictyostelium discoideum, (N-acyl)ethanolamine glycerophospholipids disappear as the amoebae aggregate, whereas the amount of ethanolamine glycerophospholipids remains relatively constant, suggesting that each type of ethanolamine-containing phospholipid might have a separate metabolic pathway. To study their metabolism, phosphatidylethanolamine and phosphatidyl(N-acyl)ethanolamine containing either [14C]ethanolamine or a 14C-labeled sn-2 fatty acyl group were incubated with D. discoideum homogenates, and the conversion of the substrates into radioactive products was monitored. At pH values 3.8 and 4.5, phosphatidyl(N-acyl)ethanolamine was hydrolyzed by a phospholipase A1 to form the sn-2 acyl form of the lipid. Only minor hydrolysis occurred at pH values of 5.2 or higher. (N-acyl)Ethanolamine was also released by a phospholipase D type activity at 0.1 the rate of the lysophospholipid formation. Phosphatidyl(N-acyl)ethanolamine was not hydrolyzed to form phosphatidylethanolamine or water soluble components. At pH 7.2 and at the low pH range of 3.8-4.5, phosphatidylethanolamine was hydrolyzed to lysophosphatidylethanolamine, which was then further degraded to water-soluble components. At pH 7.2, a phospholipase A2 initially hydrolyzed the phosphatidylethanolamine, whereas at the low pH range a phospholipase A1 was the most active enzyme. Although both types of ethanolamine-containing phospholipid were hydrolyzed by a phospholipase A1 at the low pH range, phosphatidylethanolamine hydrolysis was more sensitive to inhibition by Trition X-100, and phosphatidylethanolamine was hydrolyzed to water-soluble components, whereas phosphatidyl(N-acyl)ethanolamine was not. At pH 7.2, phosphatidylethanolamine was hydrolyzed, but phosphatidyl(N-acyl)ethanolamine was not hydrolyzed at all. These results indicate that there are separate routes of degradation for the two types of ethanolamine-containing phospholipid in D. discoideum."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(84)90343-6"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(84)90343-6"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/author"Dischinger H.C."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/author"Dischinger H.C."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/author"Ellingson J.S."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/author"Ellingson J.S."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/pages"155-162"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/pages"155-162"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/title"Comparison of the hydrolysis of phosphatidylethanolamine and phosphatidyl(N-acyl)ethanolamine in Dictyostelium discoideum amoebae."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/title"Comparison of the hydrolysis of phosphatidylethanolamine and phosphatidyl(N-acyl)ethanolamine in Dictyostelium discoideum amoebae."xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/volume"796"xsd:string
http://purl.uniprot.org/citations/6498208http://purl.uniprot.org/core/volume"796"xsd:string
http://purl.uniprot.org/citations/6498208http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6498208
http://purl.uniprot.org/citations/6498208http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6498208
http://purl.uniprot.org/citations/6498208http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6498208
http://purl.uniprot.org/citations/6498208http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6498208
http://purl.uniprot.org/uniprot/Q54Z25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6498208
http://purl.uniprot.org/uniprot/Q54WR4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6498208