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@ARTICLE{Lindner:10968,
      author       = {Lindner, S.N. and Niederholtmeyer, H. and Schmitz, K. and
                      Schobert, S. and Wendisch, V. F.},
      title        = {{P}olyphosphate/{ATP}-dependent {NAD} kinase of
                      {C}orynebacterium glutamicum: biochemical properties and
                      impact of ppn{K} overexpression on lysine production},
      journal      = {Applied Microbiology and Biotechnology},
      volume       = {87},
      issn         = {0175-7598},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-10968},
      pages        = {583 - 593},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Nicotinamide adenine dinucleotide phosphate (NADP) is
                      synthesized by phosphorylation of either oxidized or reduced
                      nicotinamide adenine dinucleotide (NAD/NADH). Here, the
                      cg1601/ppnK gene product from Corynebacterium glutamicum
                      genome was purified from recombinant Escherichia coli and
                      enzymatic characterization revealed its activity as a
                      polyphosphate (PolyP)/ATP-dependent NAD kinase (PPNK). PPNK
                      from C. glutamicum was shown to be active as homotetramer
                      accepting PolyP, ATP, and even ADP for phosphorylation of
                      NAD. The catalytic efficiency with ATP as phosphate donor
                      for phosphorylation of NAD was higher than with PolyP. With
                      respect to the chain length of PolyP, PPNK was active with
                      short-chain PolyPs. PPNK activity was independent of
                      bivalent cations when using ATP, but was enhanced by
                      manganese and in particular by magnesium ions. When using
                      PolyP, PPNK required bivalent cations, preferably manganese
                      ions, for activity. PPNK was inhibited by NADP and NADH at
                      concentrations below millimolar. Overexpression of ppnK in
                      C. glutamicum wild type slightly reduced growth and ppnK
                      overexpression in the lysine producing strain DM1729
                      resulted in a lysine product yield on glucose of 0.136 +/-
                      0.006 mol lysine (mol glucose)(-1), which was $12\%$ higher
                      than that of the empty vector control strain.},
      keywords     = {Adenosine Triphosphate: metabolism / Amino Acid Sequence /
                      Bacterial Proteins: chemistry / Bacterial Proteins: genetics
                      / Bacterial Proteins: metabolism / Corynebacterium
                      glutamicum: chemistry / Corynebacterium glutamicum:
                      enzymology / Corynebacterium glutamicum: genetics /
                      Corynebacterium glutamicum: metabolism / Gene Expression /
                      Lysine: biosynthesis / Molecular Sequence Data /
                      Phosphotransferases: chemistry / Phosphotransferases:
                      genetics / Phosphotransferases: metabolism / Polyphosphates:
                      chemistry / Polyphosphates: metabolism / Protein
                      Multimerization / Sequence Homology, Amino Acid / Substrate
                      Specificity / Bacterial Proteins (NLM Chemicals) /
                      Polyphosphates (NLM Chemicals) / Adenosine Triphosphate (NLM
                      Chemicals) / Lysine (NLM Chemicals) / Phosphotransferases
                      (NLM Chemicals) / polyphosphate NAD-kinase (NLM Chemicals) /
                      J (WoSType)},
      cin          = {IBT-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB55},
      pnm          = {Biotechnologie},
      pid          = {G:(DE-Juel1)FUEK410},
      shelfmark    = {Biotechnology $\&$ Applied Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20180116},
      UT           = {WOS:000277959500020},
      doi          = {10.1007/s00253-010-2481-y},
      url          = {https://juser.fz-juelich.de/record/10968},
}