Activation of Acetone and Other Simple Ketones in Anaerobic Bacteria


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HEIDER, Johann, Karola SCHÜHLE, Jasmin FREY, Bernhard SCHINK, 2016. Activation of Acetone and Other Simple Ketones in Anaerobic Bacteria. In: Journal of Molecular Microbiology and Biotechnology. 26(1-3), pp. 152-164. ISSN 1464-1801. eISSN 1660-2412. Available under: doi: 10.1159/000441500

@article{Heider2016-03-10Activ-33891, title={Activation of Acetone and Other Simple Ketones in Anaerobic Bacteria}, year={2016}, doi={10.1159/000441500}, number={1-3}, volume={26}, issn={1464-1801}, journal={Journal of Molecular Microbiology and Biotechnology}, pages={152--164}, author={Heider, Johann and Schühle, Karola and Frey, Jasmin and Schink, Bernhard} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Schühle, Karola</dc:creator> <dcterms:isPartOf rdf:resource=""/> <dc:contributor>Schühle, Karola</dc:contributor> <dc:creator>Schink, Bernhard</dc:creator> <dc:language>eng</dc:language> <dspace:isPartOfCollection rdf:resource=""/> <dc:contributor>Heider, Johann</dc:contributor> <dc:creator>Heider, Johann</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <bibo:uri rdf:resource=""/> <dcterms:available rdf:datatype="">2016-05-12T09:38:14Z</dcterms:available> <dc:creator>Frey, Jasmin</dc:creator> <dcterms:title>Activation of Acetone and Other Simple Ketones in Anaerobic Bacteria</dcterms:title> <dcterms:abstract xml:lang="eng">Acetone and other ketones are activated for subsequent degradation through carboxylation by many nitrate-reducing, phototrophic, and obligately aerobic bacteria. Acetone carboxylation leads to acetoacetate, which is subsequently activated to a thioester and degraded via thiolysis. Two different types of acetone carboxylases have been described, which require either 2 or 4 ATP equivalents as an energy supply for the carboxylation reaction. Both enzymes appear to combine acetone enolphosphate with carbonic phosphate to form acetoacetate. A similar but more complex enzyme is known to carboxylate the aromatic ketone acetophenone, a metabolic intermediate in anaerobic ethylbenzene metabolism in denitrifying bacteria, with simultaneous hydrolysis of 2 ATP to 2 ADP. Obligately anaerobic sulfate-reducing bacteria activate acetone to a four-carbon compound as well, but via a different process than bicarbonate- or CO2-dependent carboxylation. The present evidence indicates that either carbon monoxide or a formyl residue is used as a cosubstrate, and that the overall ATP expenditure of this pathway is substantially lower than in the known acetone carboxylase reactions.</dcterms:abstract> <dc:contributor>Frey, Jasmin</dc:contributor> <dc:contributor>Schink, Bernhard</dc:contributor> <dcterms:issued>2016-03-10</dcterms:issued> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:date rdf:datatype="">2016-05-12T09:38:14Z</dc:date> </rdf:Description> </rdf:RDF>

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