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@ARTICLE{Vogt:173011,
      author       = {Vogt, Michael and Krumbach, Karin and Bang, Won-Gi and van
                      Ooyen, Jan and Noack, Stephan and Klein, Bianca and Bott,
                      Michael and Eggeling, Lothar},
      title        = {{T}he contest for precursors: channelling {L}-isoleucin
                      {S}ynthesis in {C}orynebacterium glutamicum without
                      byproduct formation},
      journal      = {Applied microbiology and biotechnology},
      volume       = {99},
      number       = {2},
      issn         = {1432-0614},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {FZJ-2014-06425},
      pages        = {791-800},
      year         = {2015},
      abstract     = {l-Isoleucine is an essential amino acid, which is required
                      as a pharma product and feed additive. Its synthesis shares
                      initial steps with that of l-lysine and l-threonine, and
                      four enzymes of l-isoleucine synthesis have an enlarged
                      substrate specificity involved also in l-valine and
                      l-leucine synthesis. As a consequence, constructing a strain
                      specifically overproducing l-isoleucine without byproduct
                      formation is a challenge. Here, we analyze for consequences
                      of plasmid-encoded genes in Corynebacterium glutamicum
                      MH20-22B on l-isoleucine formation, but still obtain
                      substantial accumulation of byproducts. In a different
                      approach, we introduce point mutations into the genome of
                      MH20-22B to remove the feedback control of homoserine
                      dehydrogenase, hom, and threonine dehydratase, ilvA, and we
                      assay sets of genomic promoter mutations to increase hom and
                      ilvA expression as well as to reduce dapA expression, the
                      latter gene encoding the dihydrodipicolinate synthase. The
                      promoter mutations are mirrored in the resulting
                      differential protein levels determined by a targeted
                      LC-MS/MS approach for the three key enzymes. The best
                      combination of genomic mutations was found in strain K2P55,
                      where 53 mM l-isoleucine could be obtained. Whereas in
                      fed-batch fermentations with the plasmid-based strain, 94 mM
                      l-isoleucine with l-lysine as byproduct was formed; with the
                      plasmid-less strain K2P55, 109 mM l-isoleucine accumulated
                      with no substantial byproduct formation. The specific molar
                      yield with the latter strain was 0.188 mol l-isoleucine (mol
                      glucose)−1 which characterizes it as one of the best
                      l-isoleucine producers available and which does not contain
                      plasmids.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000348770900021},
      doi          = {10.1007/s00253-014-6109-5},
      url          = {https://juser.fz-juelich.de/record/173011},
}