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http://purl.uniprot.org/citations/782527http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/782527http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/782527http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/782527http://www.w3.org/2000/01/rdf-schema#comment"A sensitive and quantitative assay for 3-octaprenyl-4-hydroxybenzoate carboxy-lyase has been developed. This enzyme, which catalyses the third reaction in ubiquinone biosynthesis in Escherichia coli, was partially purified and some of its properties determined. It was found that a considerable proportion of the carboxylyase activity could be separated from the membrane fraction in cell extracts prepared using a French press. Gel filtration showed the molecular weight of the enzyme to be about 340 000. For optimal activity the carboxy-lase was shown to require Mn2+, washed membranes or an extract of phospholipids, and an unidentified heat stable factor of molecular weight less than 10 000. The carboxy-lyase reaction was also shown to be strongly stimulated by dithiothreitol and methanol. The properties of the carboxy-lyase are compared with the three other enzymes concerned with ubiquinone biosynthesis in E. coli which have been studied in vitro. The fact that the substrate of the carboxy-lyase is membrane-bound and the enzyme is stimulated by phospholipid suggests that it normally functions in association with the cytoplasmic membrane in vivo."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/782527http://purl.org/dc/terms/identifier"doi:10.1016/0005-2736(76)90407-7"xsd:string
http://purl.uniprot.org/citations/782527http://purl.org/dc/terms/identifier"doi:10.1016/0005-2736(76)90407-7"xsd:string
http://purl.uniprot.org/citations/782527http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/782527
http://purl.uniprot.org/citations/782527http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/782527
http://purl.uniprot.org/citations/782527http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/782527
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Gibson F."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Gibson F."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Young I.G."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Young I.G."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Leppik R.A."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/author"Leppik R.A."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/date"1976"xsd:gYear
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/date"1976"xsd:gYear
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/pages"800-810"xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/pages"800-810"xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/title"Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/title"Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase."xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/volume"436"xsd:string
http://purl.uniprot.org/citations/782527http://purl.uniprot.org/core/volume"436"xsd:string