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@ARTICLE{Oeggl:858538,
      author       = {Oeggl, Reinhard and Neumann, Timo and Gätgens, Jochem and
                      Romano, Diego and Noack, Stephan and Rother, Dörte},
      title        = {{C}itrate as {C}ost-{E}fficient {NADPH} {R}egenerating
                      {A}gent},
      journal      = {Frontiers in Bioengineering and Biotechnology},
      volume       = {6},
      issn         = {2296-4185},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2018-07409},
      pages        = {196},
      year         = {2018},
      abstract     = {The economically efficient utilization of NADPH or
                      NADH-dependent enzymes requires the regeneration of consumed
                      reduction equivalents. This cofactor regeneration is
                      classically done via an additional substrate, and if
                      necessary enzyme. We now demonstrate an easy-to-apply
                      cofactor regeneration approach, which can especially be used
                      in screening applications. Simply by applying citrate to a
                      buffer or directly using citrate/-phosphate buffer NADPH can
                      be regenerated by native enzymes of the TCA cycle,
                      practically present in all aerobic living organisms. Apart
                      from viable-culturable cells, this regeneration approach can
                      also be applied with lyophilized cells and even crude cell
                      extracts. This is exemplarily shown for the synthesis of 1
                      phenylethanol from acetophenone with several
                      oxidoreductases. The mechanism of NADPH regeneration by TCA
                      cycle enzymes was further investigated by a transient
                      isotopic labeling experiment feeding [1,5-13C]citrate. This
                      revealed that the regeneration mechanism can further be
                      optimized by genetic modification of two competing internal
                      citrate metabolization pathways, the glyoxylate shunt and
                      the glutamate dehydrogenase.},
      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},
      pubmed       = {pmid:30631764},
      UT           = {WOS:000454341200001},
      doi          = {10.3389/fbioe.2018.00196},
      url          = {https://juser.fz-juelich.de/record/858538},
}