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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