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http://purl.uniprot.org/citations/7819205http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7819205http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7819205http://www.w3.org/2000/01/rdf-schema#comment"We have purified the citrate synthase from Azotobacter vinelandii and have determined that the size of the subunit is 48,000 Da and the structure of the holoenzyme is a hexamer. This contrasts with earlier estimates that indicate a 58,000 Da subunit and a tetrameric structure. In addition, the enzyme is allosteric with a Hill coefficient of 1.5 and is inhibited by NADH. The Hill coefficient is changed to about 1 by high ionic strength and AMP. The enzyme is thus similar to the citrate synthases of many other Gram-negative, facultative, anaerobic organisms. In addition, the amino acid sequence of about 100 residues has been determined and found to be highly similar to the sequence of Pseudomonas aeruginosa citrate synthase."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.org/dc/terms/identifier"doi:10.1021/bi00001a031"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.org/dc/terms/identifier"doi:10.1021/bi00001a031"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Moomaw C.R."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Moomaw C.R."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Slaughter C.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Slaughter C.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Srere P.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Srere P.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Atkinson M.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Atkinson M.A."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Rault-Leonardon M."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/author"Rault-Leonardon M."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/pages"257-263"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/pages"257-263"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/title"Azotobacter vinelandii citrate synthase."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/title"Azotobacter vinelandii citrate synthase."xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/volume"34"xsd:string
http://purl.uniprot.org/citations/7819205http://purl.uniprot.org/core/volume"34"xsd:string