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Cloning, characterization and transcriptional analysis of two phosphate acetyltransferase isoforms from Azotobacter vinelandii

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dc.contributor.author Dimou, M en
dc.contributor.author Venieraki, A en
dc.contributor.author Liakopoulos, G en
dc.contributor.author Katinakis, P en
dc.date.accessioned 2014-06-06T06:51:14Z
dc.date.available 2014-06-06T06:51:14Z
dc.date.issued 2011 en
dc.identifier.issn 03014851 en
dc.identifier.uri http://dx.doi.org/10.1007/s11033-010-0478-3 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/5402
dc.subject Acetate en
dc.subject Azotobacter vinelandii en
dc.subject Phosphate acetyltransferase en
dc.subject RT-qPCR en
dc.subject.other acetic acid en
dc.subject.other acetyl coenzyme A en
dc.subject.other ammonia en
dc.subject.other AvPTA 1 enzyme en
dc.subject.other AvPTA 2 enzyme en
dc.subject.other bacterial enzyme en
dc.subject.other phosphate acetyltransferase en
dc.subject.other unclassified drug en
dc.subject.other article en
dc.subject.other Azotobacter vinelandii en
dc.subject.other bacterial growth en
dc.subject.other bacterial strain en
dc.subject.other binding affinity en
dc.subject.other controlled study en
dc.subject.other down regulation en
dc.subject.other enzyme activity en
dc.subject.other enzyme analysis en
dc.subject.other enzyme kinetics en
dc.subject.other enzyme localization en
dc.subject.other Escherichia coli en
dc.subject.other gene expression regulation en
dc.subject.other gene sequence en
dc.subject.other genetic transcription en
dc.subject.other molecular cloning en
dc.subject.other nonhuman en
dc.subject.other nucleotide sequence en
dc.subject.other protein purification en
dc.subject.other sequence alignment en
dc.subject.other upregulation en
dc.subject.other Acetates en
dc.subject.other Amino Acid Sequence en
dc.subject.other Azotobacter vinelandii en
dc.subject.other Biocatalysis en
dc.subject.other Cloning, Molecular en
dc.subject.other Electrophoresis, Polyacrylamide Gel en
dc.subject.other Gene Expression Regulation, Bacterial en
dc.subject.other Isoenzymes en
dc.subject.other Models, Biological en
dc.subject.other Molecular Sequence Data en
dc.subject.other Phosphate Acetyltransferase en
dc.subject.other Protein Structure, Quaternary en
dc.subject.other Recombinant Proteins en
dc.subject.other Sequence Alignment en
dc.subject.other Transcription, Genetic en
dc.subject.other Azotobacter vinelandii en
dc.subject.other Bacteria (microorganisms) en
dc.title Cloning, characterization and transcriptional analysis of two phosphate acetyltransferase isoforms from Azotobacter vinelandii en
heal.type journalArticle en
heal.identifier.primary 10.1007/s11033-010-0478-3 en
heal.publicationDate 2011 en
heal.abstract Acetate is abundant in soil contributing to a great extent on carbon cycling in nature. Phosphate acetyltransferase (Pta, EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl-P to CoA forming acetyl-CoA and inorganic phosphate, participating to acetate assimilation/dissimilation reactions. In the present study, we demonstrate that Azotobacter vinelandii, a nitrogen-fixing, free-living, soil bacterium, possesses two class II phosphate acetyltransferase isoforms, AvPTA-1 and AvPTA-2, with different kinetic properties. At the acetyl- CoA forming direction, AvPTA-1 has lower affinity for acetyl-P and higher affinity for CoA than AvPTA-2 while at the acetyl-P forming direction; activity was measured only for AvPTA-1. Quantification of their expression patterns by RT-qPCR indicated that both genes are expressed during exponential growth on glucose or acetate and are downregulated in the stationary phase. The ammonium availability during acetate growth resulted in up-regulation of Avpta-2 expression only. Further, the gene expression patterns of other related gene transcripts were also investigated, in order to understand the influence of each pathway in the assimilation/dissimilation of acetate. © Springer Science+Business Media B.V. 2010. en
heal.journalName Molecular Biology Reports en
dc.identifier.issue 6 en
dc.identifier.volume 38 en
dc.identifier.doi 10.1007/s11033-010-0478-3 en
dc.identifier.spage 3653 en
dc.identifier.epage 3663 en


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