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@ARTICLE{Maeda:892288,
      author       = {Maeda, Tomoya and Koch-Koerfges, Abigail and Bott, Michael},
      title        = {{R}elevance of {NADH} {D}ehydrogenase and {A}lternative
                      {T}wo-{E}nzyme {S}ystems for {G}rowth of {C}orynebacterium
                      glutamicum {W}ith {G}lucose, {L}actate, and {A}cetate},
      journal      = {Frontiers in Bioengineering and Biotechnology},
      volume       = {8},
      issn         = {2296-4185},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2021-01997},
      pages        = {621213},
      year         = {2021},
      note         = {Biotechnologie 1},
      abstract     = {The oxidation of NADH with the concomitant reduction of a
                      quinone is a crucial step in the metabolism of respiring
                      cells. In this study, we analyzed the relevance of three
                      different NADH oxidation systems in the actinobacterial
                      model organism Corynebacterium glutamicum by characterizing
                      defined mutants lacking the non-proton-pumping NADH
                      dehydrogenase Ndh (Δndh) and/or one of the alternative
                      NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA
                      (ΔldhA) and malate dehydrogenase Mdh (Δmdh). Together with
                      the menaquinone-dependent L-lactate dehydrogenase LldD and
                      malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo
                      couples can functionally replace Ndh activity. In glucose
                      minimal medium the Δndh mutant, but not the ΔldhA and
                      Δmdh strains, showed reduced growth and a lowered NAD+/NADH
                      ratio, in line with Ndh being the major enzyme for NADH
                      oxidation. Growth of the double mutants ΔndhΔmdh and
                      ΔndhΔldhA, but not of strain ΔmdhΔldhA, in glucose
                      medium was stronger impaired than that of the Δndh mutant,
                      supporting an active role of the alternative Mdh-Mqo and
                      LdhA-LldD systems in NADH oxidation and menaquinone
                      reduction. In L-lactate minimal medium the Δndh mutant grew
                      better than the wild type, probably due to a higher activity
                      of the menaquinone-dependent L-lactate dehydrogenase LldD.
                      The ΔndhΔmdh mutant failed to grow in L-lactate medium and
                      acetate medium. Growth with L-lactate could be restored by
                      additional deletion of sugR, suggesting that ldhA repression
                      by the transcriptional regulator SugR prevented growth on
                      L-lactate medium. Attempts to construct a ΔndhΔmdhΔldhA
                      triple mutant were not successful, suggesting that Ndh, Mdh
                      and LdhA cannot be replaced by other NADH-oxidizing enzymes
                      in C. glutamicum.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33585420},
      UT           = {WOS:000614087900001},
      doi          = {10.3389/fbioe.2020.621213},
      url          = {https://juser.fz-juelich.de/record/892288},
}