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Inactivation of Glutamine Synthetase in Intact E. coli Cells

  • H. Holzer
  • H. Schutt
  • P. C. Heinrich
Conference paper

Abstract

Addition of small amounts of NH4 + (at final concentration 10-4 M, for example) to suspensions of E. coli which have grown in ammonium-free medium leads to a rapid inactivation of glutamine synthetase (1, see figure 1). Pursuit of this observation led to the discovery of an ATP-
Fig. 1.

Time course of the inactivation of glutamine synthetase in E. coli after addition of 10 -4 M NH 4 + at 0° and 37°. Cells were cultivated in glutamate-medium and at zero time ammonium sulfate was added. Samples were withdrawn at various times, sonicated 15 sec, and centrifuged. Symbols o and x denote data from two separate experiments. Taken from ref. 1

and glutamine-dependent, glutamine synthetase-inactivating enzyme (2). Further research by Earl Stadtman’s group in Bethesda and ours in Freiburg (3,4) elucidated a system for the regulation of glutamine synthetase by effector-controlled, enzyme-catalyzed, covalent modification schematized in figure 2. The findings collected in figure 2 are based on studies with extracts of E. coli and with the purified enzymes.

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References

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1972

Authors and Affiliations

  • H. Holzer
    • 1
    • 2
  • H. Schutt
    • 1
    • 2
  • P. C. Heinrich
    • 1
    • 2
  1. 1.Biochemisches Institut der Universität FreiburgFreiburgGermany
  2. 2.Hoffmann-La Roche AGBaselSwitzerland

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