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http://purl.uniprot.org/citations/3049537http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3049537http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3049537http://www.w3.org/2000/01/rdf-schema#comment"A structural gene for isocitrate lyase was isolated from a cosmid containing an ace locus of the Escherichia coli chromosome. Cloning and expression under control of the tac promoter in a multicopy plasmid showed that a 1.7-kilobase-pair DNA segment was sufficient for complementation of an aceA deletion mutation and overproduction of isocitrate lyase. DNA sequence analysis of the cloned gene and N-terminal protein sequencing of the cloned and wild-type enzymes revealed an entire aceA gene which encodes a 429-amino-acid residue polypeptide whose C-terminus is histidine. The deduced amino acid sequence for the 47.2-kilodalton subunit of E. coli isocitrate lyase could be aligned with that for the 64.8-kilodalton subunit of the castor bean enzyme with 39% identity except for limited N- and C-terminal regions and a 103-residue stretch that was unique for the plant enzyme and started approximately in the middle of that peptide."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.org/dc/terms/identifier"doi:10.1128/jb.170.10.4528-4536.1988"xsd:string
http://purl.uniprot.org/citations/3049537http://purl.org/dc/terms/identifier"doi:10.1128/jb.170.10.4528-4536.1988"xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/author"Matsuoka M."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/author"Matsuoka M."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/author"McFadden B.A."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/author"McFadden B.A."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/pages"4528-4536"xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/pages"4528-4536"xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/title"Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/title"Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/volume"170"xsd:string
http://purl.uniprot.org/citations/3049537http://purl.uniprot.org/core/volume"170"xsd:string
http://purl.uniprot.org/citations/3049537http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3049537
http://purl.uniprot.org/citations/3049537http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3049537
http://purl.uniprot.org/citations/3049537http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3049537
http://purl.uniprot.org/citations/3049537http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3049537
http://purl.uniprot.org/uniprot/P11071http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3049537
http://purl.uniprot.org/uniprot/P0A9G6http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3049537