SUMMARY: The synthesis of glutamine synthetase in under different conditions was studied. The optimal concentration of ammonium sulphate in the growth medium for the enzyme synthesis was 0.4 mM. When glucose was limiting growth the enzyme synthesis became dependent on oxygen. L-Glutamine repressed synthesis of the enzyme and, to a lesser extent, that of glutamate dehydrogenase. L-Arginine, L-asparagine, D-glutamine, L-methionine and L-tryptophan also decreased synthesis of glutamine synthetase. On the other hand, L-glutamate induced the enzyme synthesis; L-isoleucine, L-leucine and L-valine also increased it. Acetyl-L-glutamine did not affect the enzyme synthesis. D-Glutamine was much less active than L-glutamine as a substrate in the γ-glutamyl transfer reaction. At low concentrations, both aza-L-serine and 6-diazo-5-oxo-L-norleucine increased the specific activity of glutamine synthetase in the bacteria.


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