SUMMARY: The activities of citrate synthase (EC and NADP-dependent glutamate dehydrogenase (GDH) (EC of were inhibited by glyoxylate. In the presence of glyoxylate, pyruvate and glyoxylate pools increased, suggesting that glyoxylate was efficiently transported and catabolized. Pyruvate accumulation also indicates that citrate synthase was inhibited. A decrease in the glutamate pool was also observed under these conditions. This can be attributed to an increased transamination rate and to the inhibitory effect of glyoxylate on NADP-dependent GDH. Furthermore, the increase in the ammonium pool in the presence of glyoxylate suggests that NADP-dependent GDH was being inhibited , since the activity of glutamine synthetase did not decrease under these conditions. We propose that the inhibition of both citrate synthase and NADP-dependent GDH could form part of a mechanism that regulates the internal 2-oxoglutarate concentration.


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