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http://purl.uniprot.org/citations/16272400http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16272400http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16272400http://www.w3.org/2000/01/rdf-schema#comment"This report shows that Salmonella enterica catabolizes ethanolamine to acetyl-CoA (Ac-CoA), which enters the glyoxylate bypass and tricarboxylic acid cycle for the generation of energy and central metabolites. During growth on ethanolamine, S. enterica excreted acetate, whose recapture depended on Ac-CoA synthetase (Acs) and the housekeeping phosphotransacetylase (Pta) enzyme activities. The Pta enzyme did not play a role in acetate excretion during growth of S. enterica on ethanolamine. It is proposed that during growth on ethanolamine, acetate excretion is necessary to maintain a pool of free CoA. Acetate excretion requires the eut operon-encoded phosphotransacetylase (EutD) and acetate kinase (Ack) enzymes. EutD function was not required for growth on ethanolamine, and an eutD strain showed only a slight reduction in growth rate. The existence of an as-yet-unidentified system that releases acetate was revealed during growth of a strain lacking Acs, the housekeeping phosphotransacetylase (Pta), and EutD. The functions of pyruvate oxidase (PoxB), Ack and STM3118 protein [a homologue of the Saccharomyces cerevisiae Ac-CoA hydrolase (Ach1p) enzyme] were not involved in the release of acetate by the acs pta eutD strain."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.org/dc/terms/identifier"doi:10.1099/mic.0.28156-0"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.org/dc/terms/identifier"doi:10.1099/mic.0.28156-0"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Escalante-Semerena J.C."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Escalante-Semerena J.C."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Garrity J."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Garrity J."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Starai V.J."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/author"Starai V.J."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/name"Microbiology"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/name"Microbiology"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/pages"3793-3801"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/pages"3793-3801"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/title"Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/title"Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities."xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/volume"151"xsd:string
http://purl.uniprot.org/citations/16272400http://purl.uniprot.org/core/volume"151"xsd:string
http://purl.uniprot.org/citations/16272400http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16272400
http://purl.uniprot.org/citations/16272400http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16272400
http://purl.uniprot.org/citations/16272400http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16272400
http://purl.uniprot.org/citations/16272400http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16272400