PUMA publications for /tag/pathway,https://puma.ub.uni-stuttgart.de/tag/pathway,PUMA RSS feed for /tag/pathway,2024-03-29T12:44:00+01:00Comparative 13C metabolic flux analysis of pyruvate dehydrogenase complex-deficient, L-valine-producing Corynebacterium glutamicumhttps://puma.ub.uni-stuttgart.de/bibtex/287adbada4c59b528370d7ee2b0a038d6/bastianbastian2018-02-09T13:18:17+01:00Carbon Complex, Corynebacterium Dehydrogenase Dioxide, Escherichia Glycolysis, Isotopes, NADP Pathway, Pentose Phosphate Proteins, Pyruvate Transhydrogenases Valine, coli coli, glutamicum, myown <span data-person-type="author" class="authorEditorList "><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Tobias Bartek" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/0"><span itemprop="name">T. Bartek</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bastian Blombach" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/1"><span itemprop="name">B. Blombach</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Siegmund Lang" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/2"><span itemprop="name">S. Lang</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bernhard J. Eikmanns" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/3"><span itemprop="name">B. Eikmanns</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Wolfgang Wiechert" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/4"><span itemprop="name">W. Wiechert</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Marco Oldiges" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/5"><span itemprop="name">M. Oldiges</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Katharina Nöh" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/6"><span itemprop="name">K. Nöh</span></a></span>, </span> and <span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Stephan Noack" itemprop="url" href="/person/13db8757c79c2bbc557e709197512559c/author/7"><span itemprop="name">S. Noack</span></a></span></span>. </span><span class="additional-entrytype-information"><span itemtype="http://schema.org/PublicationIssue" itemscope="itemscope" itemprop="isPartOf"><em><span itemprop="journal">Appl. Environ. Microbiol.</span>, </em> <em><span itemtype="http://schema.org/PublicationVolume" itemscope="itemscope" itemprop="isPartOf"><span itemprop="volumeNumber">77 </span></span>(<span itemprop="issueNumber">18</span>):
<span itemprop="pagination">6644--6652</span></em> </span>(<em><span>September 2011<meta content="September 2011" itemprop="datePublished"/></span></em>)</span>Fri Feb 09 13:18:17 CET 2018Appl. Environ. Microbiol.sep186644--6652Comparative 13C metabolic flux analysis of pyruvate dehydrogenase complex-deficient, {L}-valine-producing {Corynebacterium} glutamicum772011Carbon Complex, Corynebacterium Dehydrogenase Dioxide, Escherichia Glycolysis, Isotopes, NADP Pathway, Pentose Phosphate Proteins, Pyruvate Transhydrogenases Valine, coli coli, glutamicum, myown L-Valine can be formed successfully using C. glutamicum strains missing an active pyruvate dehydrogenase enzyme complex (PDHC). Wild-type C. glutamicum and four PDHC-deficient strains were compared by (13)C metabolic flux analysis, especially focusing on the split ratio between glycolysis and the pentose phosphate pathway (PPP). Compared to the wild type, showing a carbon flux of 69\% ± 14\% through the PPP, a strong increase in the PPP flux was observed in PDHC-deficient strains with a maximum of 113\% ± 22\%. The shift in the split ratio can be explained by an increased demand of NADPH for l-valine formation. In accordance, the introduction of the Escherichia coli transhydrogenase PntAB, catalyzing the reversible conversion of NADH to NADPH, into an L-valine-producing C. glutamicum strain caused the PPP flux to decrease to 57\% ± 6\%, which is below the wild-type split ratio. Hence, transhydrogenase activity offers an alternative perspective for sufficient NADPH supply, which is relevant for most amino acid production systems. Moreover, as demonstrated for L-valine, this bypass leads to a significant increase of product yield due to a concurrent reduction in carbon dioxide formation via the PPP.