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On the Mechanism of Action and Metabolic Control of the Multifunctional Enzyme Complex that Catalyzes Adenylylation and Deadenylylation of Escherichia coli Glutamine Synthetase

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Book cover Metabolic Interconversion of Enzymes

Abstract

Glutamine metabolism in E. coli is modulated by enzyme catalyzed adenylylation and deadenylylation of glutamine synthetase (GS) in response to fluctuations in the intracellular concentration of glutamine, α-ketoglutarate and various nucleoside tri phosphates. Adenylylation is accompanied by a decrease in catalytic activity (1,2), a change in divalent ion specificity (1), a change in sensitivity to cumulative feedback inhibition by 9 different end products of glutamine metabolism (3,4) and a substantial shift in pH optimum (3).

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Stadtman, E.R. et al. (1972). On the Mechanism of Action and Metabolic Control of the Multifunctional Enzyme Complex that Catalyzes Adenylylation and Deadenylylation of Escherichia coli Glutamine Synthetase. In: Wieland, O., Helmreich, E., Holzer, H. (eds) Metabolic Interconversion of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-37966-0_24

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  • DOI: https://doi.org/10.1007/978-3-662-37966-0_24

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-37241-8

  • Online ISBN: 978-3-662-37966-0

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