RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/6780551http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6780551http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6780551http://www.w3.org/2000/01/rdf-schema#comment"Homogeneous beta-ketoadipate succinyl-CoA transferase (EC 2.8.3.6) preparations were obtained from extracts of Acinetobacter calcoaceticus and Pseudomonas putida. Gel filtration indicated that the respective transferases have similar molecular weights of 108,000 and 109,000; each transferase appears to have an alpha 2 beta 2 oligomeric structure formed by association of nonidentical subunits with a molecular weight of about 25,000. The subunits were separated by sodium dodecyl sulfate-gel electrophoresis, and differences in their primary structures were revealed by determination of the NH2-terminal amino acid sequences of the oligomers. The transferases cross-react immunologically and possess similar amino acid compositions. These are remarkably similar to the amino acid compositions of gamma-carboxymuconolactone decarboxylases (EC 4.1.1.44) and beta-ketoadipate enol-lactone hydrolases (EC 3.1.1.24), enzymes that mediate consecutive reactions preceding the transferase step in the beta-ketoadipate pathway."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)69841-8"xsd:string
http://purl.uniprot.org/citations/6780551http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)69841-8"xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/author"Ornston L.N."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/author"Ornston L.N."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/author"Yeh W.-K."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/author"Yeh W.-K."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/date"1981"xsd:gYear
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/date"1981"xsd:gYear
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/pages"1565-1569"xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/pages"1565-1569"xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/title"Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and Pseudomonas putida."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/title"Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and Pseudomonas putida."xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/volume"256"xsd:string
http://purl.uniprot.org/citations/6780551http://purl.uniprot.org/core/volume"256"xsd:string
http://purl.uniprot.org/citations/6780551http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6780551
http://purl.uniprot.org/citations/6780551http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6780551
http://purl.uniprot.org/citations/6780551http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6780551
http://purl.uniprot.org/citations/6780551http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6780551
http://purl.uniprot.org/uniprot/P0A102http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6780551
http://purl.uniprot.org/uniprot/Q01103http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6780551