Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG

  • Christian Schultz
  • Axel Niebisch
  • Lena Gebel
  • Michael BottEmail author
Applied Microbial and Cell Physiology


We recently showed that the activity of the 2-oxoglutarate dehydrogenase complex (ODHC) in Corynebacterium glutamicum is controlled by a novel regulatory mechanism that involves a 15-kDa protein called OdhI and serine/threonine protein kinase G (PknG). In its unphosphorylated state, OdhI binds to the E1 subunit (OdhA) of ODHC and, thereby, inhibits its activity. Inhibition is relieved by phosphorylation of OdhI at threonine-14 by PknG under conditions requiring high ODHC activity. In this work, evidence is provided that the dephosphorylation of phosphorylated OdhI is catalyzed by a phospho-Ser/Thr protein phosphatase encoded by the gene cg0062, designated ppp. As a decreased ODHC activity is important for glutamate synthesis, we investigated the role of OdhI and PknG for glutamate production under biotin limitation and after addition of Tween-40, penicillin, or ethambutol. A ΔodhI mutant formed only 1–13% of the glutamate synthesized by the wild type. Thus, OdhI is essential for efficient glutamate production. The effect of a pknG deletion on glutamate synthesis was dependent on the induction conditions. Under strong biotin limitation and in the presence of ethambutol, the ΔpknG mutant showed significantly increased glutamate production, offering a new way to improve production strains.


Corynebacterium glutamicum Glutamate OdhI 2-Oxoglutarate dehydrogenase Oxoglutarate dehydrogenase inhibitor PknG Serine/threonine protein kinase 



cell dry weight


serine/threonine protein kinase G


2-oxoglutarate dehydrogenase complex


oxoglutarate dehydrogenase inhibitor protein

TCA cycle

tricarboxylic acid cycle


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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Christian Schultz
    • 1
  • Axel Niebisch
    • 1
  • Lena Gebel
    • 1
  • Michael Bott
    • 1
    Email author
  1. 1.Institut für Biotechnologie 1Forschungszentrum JülichJülichGermany

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