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 |