Coordinated regulation of ammonium assimilation and carbon catabolism by glyoxylate in Saccharomyces cerevisiae.
The activities of citrate synthase (EC 4.1.3.7) and NADP+-dependent glutamate dehydrogenase (GDH) (EC 1.4.1.4) of Saccharomyces cerevisiae were inhibited in vitro 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 in vivo, 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.
D002244:Carbon / Q000378:metabolism*; D002950:Citrate (si)-Synthase / Q000037:antagonists & inhibitors; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors; D018086:Glutamate Dehydrogenase (NADP+); D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors; D006038:Glyoxylates / Q000378:metabolism* / Q000494:pharmacology; D007656:Ketoglutaric Acids / Q000378:metabolism; D011773:Pyruvates / Q000494:pharmacology; D019289:Pyruvic Acid; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism*
D006038:Glyoxylates; D007656:Ketoglutaric Acids; D011773:Pyruvates; D000644:Quaternary Ammonium Compounds; D002244:Carbon; D019289:Pyruvic Acid; D005969:Glutamate Dehydrogenase; D018086:Glutamate Dehydrogenase (NADP+); D002950:Citrate (si)-Synthase; D005974:Glutamate-Ammonia Ligase; C031150:glyoxylic acid