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@ARTICLE{Blombach:59689,
      author       = {Blombach, B. and Schreiner, M. E. and Moch, M. and Oldiges,
                      M. and Eikmanns, B. J.},
      title        = {{E}ffect of pyruvate dehydrogenase complex deficiency on
                      {L}-lysine production with {C}orynebacterium glutamicum},
      journal      = {Applied Microbiology and Biotechnology},
      volume       = {76},
      issn         = {0175-7598},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-59689},
      pages        = {615 - 623},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Base Sequence / Biotechnology / Corynebacterium glutamicum:
                      genetics / Corynebacterium glutamicum: growth $\&$
                      development / Corynebacterium glutamicum: metabolism / DNA,
                      Bacterial: genetics / Fermentation / Gene Deletion / Gene
                      Expression / Genes, Bacterial / Kinetics / Lysine:
                      biosynthesis / Pyruvate Dehydrogenase Complex: genetics /
                      Pyruvate Dehydrogenase Complex: metabolism / DNA, Bacterial
                      (NLM Chemicals) / Pyruvate Dehydrogenase Complex (NLM
                      Chemicals) / Lysine (NLM Chemicals) / J (WoSType)},
      cin          = {IBT-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB56},
      pnm          = {Biotechnologie},
      pid          = {G:(DE-Juel1)FUEK410},
      shelfmark    = {Biotechnology $\&$ Applied Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17333167},
      UT           = {WOS:000248893700015},
      doi          = {10.1007/s00253-007-0904-1},
      url          = {https://juser.fz-juelich.de/record/59689},
}