RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/8262214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8262214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8262214http://www.w3.org/2000/01/rdf-schema#comment"The aceE-aceF-lpd genes encoding the pyruvate dehydrogenase (PDH) complex of Escherichia coli are preceded by a gene encoding a putative transcriptional regulator, PdhR (formerly designated GenA). Enzymological tests and studies with pdhR-lacZ and aceE-lacZ translational fusions have shown that a constitutive mutation (acec816), which increases PDH complex synthesis to the pyruvate-induced level in the absence of inducer, is recessive to the wild-type pdhR gene in trans. Sequence comparisons further showed that the acec816 mutation affects a single site in the pdhR gene leading to an Arg118 (CGU)-->Cys (UGU) substitution in the PdhR protein. The results support the view that synthesis of the PDH complex is regulated from the pdhR promoter of a pdhR-aceEF-lpd operon."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(93)81605-y"xsd:string
http://purl.uniprot.org/citations/8262214http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(93)81605-y"xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Quail M.A."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Quail M.A."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Guest J.R."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Guest J.R."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Haydon D.J."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/author"Haydon D.J."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/pages"43-47"xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/pages"43-47"xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/title"A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/title"A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene."xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/volume"336"xsd:string
http://purl.uniprot.org/citations/8262214http://purl.uniprot.org/core/volume"336"xsd:string
http://purl.uniprot.org/citations/8262214http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8262214
http://purl.uniprot.org/citations/8262214http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8262214
http://purl.uniprot.org/citations/8262214http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8262214
http://purl.uniprot.org/citations/8262214http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8262214