Summary: A mutant of lacking aconitase did not grow on minimal medium (MM) and had five- to tenfold less NADP-dependent glutamate dehydrogenase (GDH) activity than the wild-type, although its glutamine synthetase (GS) activity was still inducible. When this mutant was incubated with glutamate as the sole nitrogen source, the 2-oxoglutarate content rose, and the NADP-dependent GDH activity increased. Furthermore, carbon-limited cultures showed a direct relation between NADP-dependent GDH activity and the intracellular 2-oxoglutarate content. We propose that the low NADP-dependent GDH activity found in the mutant was due to the lack of 2-oxoglutarate or some other intermediate of the tricarboxylic acid cycle.


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