Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/41757

TitleProteomic analysis of nitrate-dependent acetone degradation by Alicycliphilus denitrificans strain BC
Author(s)Oosterkamp, Margreet J.
Boeren, Sjef
Atashgahi, Siavash
Plugge, Caroline M.
Schaap, Peter J.
Stams, Alfons Johannes Maria
KeywordsAlicycliphilus denitrificans
Acetone
Proteome
Anaerobic
Nitrate
β-hydroxybutyrate
beta-hydroxybutyrate
Issue date2015
PublisherOxford University Press
JournalFEMS Microbiology Letters
CitationOosterkamp, Margreet J.; Boeren, Sjef; Atashgahi, Siavash; Plugge, Caroline M.; Schaap, Peter J.; Stams, A. J. M., Proteomic analysis of nitrate-dependent acetone degradation by Alicycliphilus denitrificans strain BC. FEMS Microbiology Letters, 362(11), 1-7, 2015
Abstract(s)Alicycliphilus denitrificans strain BC grows anaerobically on acetone with nitrate as electron acceptor. Comparative proteomics of cultures of A. denitrificans strain BC grown on either acetone or acetate with nitrate was performed to study the enzymes involved in the acetone degradation pathway. In the proposed acetone degradation pathway, an acetone carboxylase converts acetone to acetoacetate, an AMP-dependent synthetase/ligase converts acetoacetate to acetoacetyl-CoA, and an acetyl-CoA acetyltransferase cleaves acetoacetyl-CoA to two acetyl-CoA. We also found a putative aldehyde dehydrogenase associated with acetone degradation. This enzyme functioned as a -hydroxybutyrate dehydrogenase catalyzing the conversion of surplus acetoacetate to -hydroxybutyrate that may be converted to the energy and carbon storage compound, poly--hydroxybutyrate. Accordingly, we confirmed the formation of poly-?-hydroxybutyrate in acetone-grown cells of strain BC. Our findings provide insight in nitrate-dependent acetone degradation that is activated by carboxylation of acetone. This will aid studies of similar pathways found in other microorganisms degrading acetone with nitrate or sulfate as electron acceptor.
TypeArticle
URIhttp://hdl.handle.net/1822/41757
DOI10.1093/femsle/fnv080
ISSN0378-1097
Publisher versionhttp://femsle.oxfordjournals.org/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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