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@PHDTHESIS{Sundermeyer:1018222,
      author       = {Sundermeyer, Lea},
      title        = {{A}nalysis of the signal transduction cascade tuning the
                      2-oxoglutarate dehydrogenase activity in {C}orynebacterium
                      glutamicum},
      volume       = {273},
      school       = {Univ. Düsseldorf},
      type         = {Dissertation},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {FZJ-2023-04618},
      isbn         = {978-3-95806-722-6},
      series       = {Schriften des Forschungszentrums Jülich Reihe
                      Schlüsseltechnologien / Key Technologies},
      pages        = {VI, 119},
      year         = {2023},
      note         = {Dissertation, Univ. Düsseldorf, 2022},
      abstract     = {In Corynebacterium glutamicum and many other
                      actinobacteria, the 2-oxoglutarate dehydrogenase complex
                      (ODH), a key enzyme of the tricarboxylic acid cycle, differs
                      from wellknown representatives by an unusual E1 subunit
                      (OdhA), which is fused with the succinyltransferase domain
                      usually present in a separate E2o subunit. Therefore, OdhA
                      requires the lipoyl groups of the E2p protein (AceF) of the
                      pyruvate dehydrogenase complex (PDH) for transferring the
                      succinyl group to coenzyme A. As a consequence, ODH forms a
                      hybrid complex with PDH, composed of the four proteins OdhA,
                      AceE (E1p), AceF, and Lpd (E3). Another unusual feature of
                      ODH in C. glutamicum and other actinobacteria is its
                      regulation by the 15-kDa protein OdhI, which contains a
                      forkhead-associated (FHA) domain known to bind
                      phospho-threonine epitopes. In its unphosphorylated state,
                      OdhI binds to OdhA with nM affinity and inhibits ODH
                      activity. Phosphorylation of OdhI by the soluble
                      serine/threonine protein kinase PknG triggers a
                      conformational change of OdhI that prevents its interaction
                      with OdhA and thereby abolishes the inhibition of ODH
                      activity. Dephosphorylation of phosphorylated OdhI is
                      catalyzed by the phospho-serine/threonine protein
                      phosphatase Ppp. Previous studies suggested that PknG
                      activity is controlled by the periplasmic binding protein
                      GlnH and the transmembrane protein GlnX, whose genes form an
                      operon with pknG....},
      cin          = {IBG-1},
      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)3 / PUB:(DE-HGF)11},
      urn          = {urn:nbn:de:0001-20240124090434709-4196616-1},
      doi          = {10.34734/FZJ-2023-04618},
      url          = {https://juser.fz-juelich.de/record/1018222},
}