PUMA publications for /tag/bacterial,%20Dehydrogenase%20complex,https://puma.ub.uni-stuttgart.de/tag/bacterial,%20Dehydrogenase%20complex,PUMA RSS feed for /tag/bacterial,%20Dehydrogenase%20complex,2024-03-28T09:31:47+01:00Effect of pyruvate dehydrogenase complex deficiency on L-lysine production with Corynebacterium glutamicumhttps://puma.ub.uni-stuttgart.de/bibtex/2930ecfe113b73f241ab0452b05337d89/bastianbastian2018-02-09T13:18:17+01:00Bacterial, Base Biotechnology Complex, Corynebacterium DNA, Dehydrogenase Deletion, Expression, Fermentation, Gene Genes, Kinetics, Lysine, Pyruvate Sequence, glutamicum, myown <span data-person-type="author" class="authorEditorList "><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bastian Blombach" itemprop="url" href="/person/197097cd65b8e231a2578efbc7586a5dc/author/0"><span itemprop="name">B. Blombach</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Mark E. Schreiner" itemprop="url" href="/person/197097cd65b8e231a2578efbc7586a5dc/author/1"><span itemprop="name">M. Schreiner</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Matthias Moch" itemprop="url" href="/person/197097cd65b8e231a2578efbc7586a5dc/author/2"><span itemprop="name">M. Moch</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Marco Oldiges" itemprop="url" href="/person/197097cd65b8e231a2578efbc7586a5dc/author/3"><span itemprop="name">M. Oldiges</span></a></span>, </span> and <span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bernhard J. Eikmanns" itemprop="url" href="/person/197097cd65b8e231a2578efbc7586a5dc/author/4"><span itemprop="name">B. Eikmanns</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. Microbiol. Biotechnol.</span>, </em> <em><span itemtype="http://schema.org/PublicationVolume" itemscope="itemscope" itemprop="isPartOf"><span itemprop="volumeNumber">76 </span></span>(<span itemprop="issueNumber">3</span>):
<span itemprop="pagination">615--623</span></em> </span>(<em><span>September 2007<meta content="September 2007" itemprop="datePublished"/></span></em>)</span>Fri Feb 09 13:18:17 CET 2018Appl. Microbiol. Biotechnol.sep3615--623Effect of pyruvate dehydrogenase complex deficiency on {L}-lysine production with {Corynebacterium} glutamicum762007Bacterial, Base Biotechnology Complex, Corynebacterium DNA, Dehydrogenase Deletion, Expression, Fermentation, Gene Genes, Kinetics, Lysine, Pyruvate Sequence, glutamicum, myown Intracellular precursor supply is a critical factor for amino acid productivity of Corynebacterium glutamicum. To test for the effect of improved pyruvate availability on L-lysine production, we deleted the aceE gene encoding the E1p enzyme of the pyruvate dehydrogenase complex (PDHC) in the L-lysine-producer C. glutamicum DM1729 and characterised the resulting strain DM1729-BB1 for growth and L-lysine production. Compared to the host strain, C. glutamicum DM1729-BB1 showed no PDHC activity, was acetate auxotrophic and, after complete consumption of the available carbon sources glucose and acetate, showed a more than 50\% lower substrate-specific biomass yield (0.14 vs 0.33 mol C/mol C), an about fourfold higher biomass-specific L-lysine yield (5.27 vs 1.23 mmol/g cell dry weight) and a more than 40\% higher substrate-specific L-lysine yield (0.13 vs 0.09 mol C/mol C). Overexpression of the pyruvate carboxylase or diaminopimelate dehydrogenase genes in C. glutamicum DM1729-BB1 resulted in a further increase in the biomass-specific L-lysine yield by 6 and 56\%, respectively. In addition to L-lysine, significant amounts of pyruvate, L-alanine and L-valine were produced by C. glutamicum DM1729-BB1 and its derivatives, suggesting a surplus of precursor availability and a further potential to improve L-lysine production by engineering the L-lysine biosynthetic pathway.