Coordinated regulation of ammonium assimilation and carbon catabolism by glyoxylate in Saccharomyces cerevisiae.

@article{Gonzlez1987CoordinatedRO,
  title={Coordinated regulation of ammonium assimilation and carbon catabolism by glyoxylate in Saccharomyces cerevisiae.},
  author={A. Gonz{\'a}lez and Luis Rodr{\'i}guez and Jorge Luis Folch and Mario Sober{\'o}n and H. Olivera},
  journal={Journal of general microbiology},
  year={1987},
  volume={133 9},
  pages={
          2497-501
        }
}
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… 

Figures and Tables from this paper

Enzymes of Ammonia Assimilation in Fungi: An Overview
TLDR
An overall view of the elements present in ammonia assimilation especially in fungi will be carried out along with recent developments and concepts.
The Saccharomyces cerevisiae ICL2 Gene Encodes a Mitochondrial 2-Methylisocitrate Lyase Involved in Propionyl-Coenzyme A Metabolism
TLDR
It is demonstrated that ICL2 encodes a specific 2-methylisocitrate lyase and that the ICL1-encoded isocitrates lyase exhibits a low but significant activity with 2- methylisocite lyase.

References

SHOWING 1-10 OF 16 REFERENCES
Regulation by ammonium of glutamate dehydrogenase (NADP+) from Saccharomyces cerevisiae.
TLDR
The following results suggest that the decrease in NADP-GDH activity in ammonia-accumulating yeast cells is brought about by repression of synthesis.
The participation of the anabolic glutamate dehydrogenase in the nitrogen catabolite repression of arginase in Saccharomyces cerevisiae.
TLDR
It is shown that controversial conclusions can be reached when using different approaches to provoke catabolite derepression, and it becomes possible to show that additional regulatory processes are involved in arginase sythesis.
NADP+-dependent glutamate dehydrogenase activity is impaired in mutants of Saccharomyces cerevisiae that lack aconitase.
A mutant of Saccharomyces cerevisiae 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,
Activities of Tricarboxylic Acid Cycle Enzymes, Glyoxylate Cycle Enzymes, and Fructose Diphosphatase in Bakers' Yeast During Adaptation to Acetate Oxidation
TLDR
Under the various conditions, the only enzyme activity increase consistently related to the rising oxygen uptake rate was that of isocitrate lyase which apparently limited the activity of the cycle.
The regulation of glutamine metabolism in Candida utilis: the role of glutamine in the control of glutamine synthetase.
TLDR
In yeast growing with different sources of nitrogen there was a good inverse correlation between the rate of enzyme synthesis and the size of the cell pool of glutamines: glutamine and not ammonia appeared to act as a co-repressor of the formation of glutamine synthetase.
Neurospora crassa mutant impaired in glutamine regulation
TLDR
It is proposed that the lower repression of glutamine synthetase by glutamine in this mutant could be a necessary condition for sustaining the higher flow of nitrogen for the accumulation of amino acids observed in ammonium excess and that, if glutamine is the nitrogen signal that regulates the arginine accumulation of the vesicle, the glnr mutant has also escaped this control.
Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route.
TLDR
A detailed quantitative study was carried out of the relationship between growth condition and bacterial glutamate dehydrogenase activity of Aerobacter aerogenes and found the intracellular free ammonia concentration was less than 0.005% of the bacterial dry weight.
Nitrogen catabolite repression in a glutamate auxotroph of Saccharomyces cerevisiae
TLDR
In the glutamate auxotroph, asparaginase II biosynthesis exhibited a decreased sensitivity to nitrogen catabolite repression by ammonium ion but normal sensitivity by all amino acids tested, while in the Saccharomyces cerevisiae biosynthesis, this sensitivity was normal.
...
1
2
...