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http://purl.uniprot.org/citations/9683657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9683657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9683657http://www.w3.org/2000/01/rdf-schema#comment"An acyl-coenzyme A carboxylase that carboxylates acetyl-CoA, butyryl-CoA, propionyl-CoA, and succinyl-CoA was purified from Myxococcus xanthus. Since the enzyme showed maximal rates of carboxylation with propionyl-CoA, the enzyme is thought to be propionyl-CoA carboxylase. The apparent Km values for acetyl-CoA, butyryl-CoA, propionyl-CoA, and succinyl-CoA were found to be 0.2, 0. 2, 0.03, and 1.0 mM, respectively. The native enzyme has a molecular mass of 605-615 kDa and is composed of nonidentical subunits (alpha and beta) with molecular masses of 53 and 56 kDa, respectively. The enzyme showed maximal activity at pH 7.0-7.5 and at 25-30 degrees C, and was affected by variation in concentrations of ATP and Mg2+. During development of M. xanthus, the propionyl-CoA carboxylase activity increased gradually, with maximum activity observed during the sporulation stage. Previous work has shown that a propionyl-CoA-carboxylase-deficient mutant of M. xanthus reduces levels of long-chain fatty acids. These results suggest that the propionyl-CoA carboxylase is also responsible for the carboxylation of acetyl-CoA to malonyl-CoA used for the synthesis of long-chain fatty acids during development."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.org/dc/terms/identifier"doi:10.1007/s002030050631"xsd:string
http://purl.uniprot.org/citations/9683657http://purl.org/dc/terms/identifier"doi:10.1007/s002030050631"xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Sato M."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Sato M."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kimura I."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kimura I."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kojyo T."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/author"Kojyo T."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/name"Arch. Microbiol."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/name"Arch. Microbiol."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/pages"179-184"xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/pages"179-184"xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/title"Propionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and function in developing cells."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/title"Propionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and function in developing cells."xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/volume"170"xsd:string
http://purl.uniprot.org/citations/9683657http://purl.uniprot.org/core/volume"170"xsd:string
http://purl.uniprot.org/citations/9683657http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9683657
http://purl.uniprot.org/citations/9683657http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9683657