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http://purl.uniprot.org/citations/18331473http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18331473http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18331473http://www.w3.org/2000/01/rdf-schema#comment"Filamentous fungi metabolize toxic propionyl-CoA via the methylcitrate cycle. Disruption of the methylcitrate synthase gene leads to an accumulation of propionyl-CoA and attenuates virulence of Aspergillus fumigatus. However, addition of acetate, but not ethanol, to propionate-containing medium strongly reduces the accumulation of propionyl-CoA and restores growth of the methylcitrate synthase mutant. Therefore, the existence of a CoA-transferase was postulated, which transfers the CoASH moiety from propionyl-CoA to acetate and, thereby, detoxifying the cell. In this study, we purified the responsible protein from Aspergillus nidulans and characterized its biochemical properties. The enzyme used succinyl-, propionyl- and acetyl-CoA as CoASH donors and the corresponding acids as acceptor molecules. Although the protein displayed high sequence similarity to acetyl-CoA hydrolases this activity was hardly detectable. We additionally identified and deleted the coding DNA sequence of the CoA-transferase. The mutant displayed weak phenotypes in the presence of propionate and behaved like the wild type when no propionate was present. However, when a double-deletion mutant defective in both methylcitrate synthase and CoA-transferase was constructed, the resulting strain was unable to grow on media containing acetate and propionate as sole carbon sources, which confirmed the in vivo activity of the CoA-transferase."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2008.06180.x"xsd:string
http://purl.uniprot.org/citations/18331473http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2008.06180.x"xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/author"Brock M."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/author"Brock M."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/author"Fleck C.B."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/author"Fleck C.B."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/pages"642-656"xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/pages"642-656"xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/title"Characterization of an acyl-CoA: carboxylate CoA-transferase from Aspergillus nidulans involved in propionyl-CoA detoxification."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/title"Characterization of an acyl-CoA: carboxylate CoA-transferase from Aspergillus nidulans involved in propionyl-CoA detoxification."xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/volume"68"xsd:string
http://purl.uniprot.org/citations/18331473http://purl.uniprot.org/core/volume"68"xsd:string
http://purl.uniprot.org/citations/18331473http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18331473
http://purl.uniprot.org/citations/18331473http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18331473
http://purl.uniprot.org/citations/18331473http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18331473
http://purl.uniprot.org/citations/18331473http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18331473
http://purl.uniprot.org/uniprot/Q9TEM3http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18331473
http://purl.uniprot.org/uniprot/A9JPD8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18331473