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http://purl.uniprot.org/citations/2032623http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2032623http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2032623http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/2032623http://www.w3.org/2000/01/rdf-schema#comment"Apolipoprotein N-acyltransferase, the enzyme catalyzing the conversion of apolipoprotein to mature lipoprotein, was detected by an in vitro assay using [35S]methionine-labeled apolipoprotein as the substrate. Triton X-100 solubilized the enzyme, and was required for its activity. The enzyme showed a broad pH optimum (pH 6.5-7.5). N-Acylation of apolipoprotein with ethanol-washed membranes was dependent on exogenous phospholipids, with phosphatidylethanolamine, phosphatidylglycerol and cardiolipin all showing about 10-to 20-times enhancement of the enzyme activity in the delipidated membranes. Incubation of apolipoprotein with [3H]palmitate-labeled membranes resulted in the incorporation of [3H]palmitate into lipoprotein. The enzyme was found to be enriched in the inner membrane and in the inner membrane/outer membrane mixed fractions of the E. coli cell envelope."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/name"FEMS Microbiol. Lett."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/name"FEMS Microbiol. Lett."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.org/dc/terms/identifier"doi:10.1016/0378-1097(91)90251-5"xsd:string
http://purl.uniprot.org/citations/2032623http://purl.org/dc/terms/identifier"doi:10.1016/0378-1097(91)90251-5"xsd:string
http://purl.uniprot.org/citations/2032623http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2032623
http://purl.uniprot.org/citations/2032623http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2032623
http://purl.uniprot.org/citations/2032623http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2032623
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/author"Wu H.C."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/author"Wu H.C."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/author"Gupta S.D."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/author"Gupta S.D."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/pages"37-41"xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/pages"37-41"xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/title"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/title"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/volume"62"xsd:string
http://purl.uniprot.org/citations/2032623http://purl.uniprot.org/core/volume"62"xsd:string
http://purl.uniprot.org/citations/2032623http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2032623
http://purl.uniprot.org/citations/2032623http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2032623