Accumulation of α-ketoglutaric acid in yeast mutants requiring lysine☆

@article{Bhattacharjee1968AccumulationO,
  title={Accumulation of $\alpha$-ketoglutaric acid in yeast mutants requiring lysine☆},
  author={J. K. Bhattacharjee and A. Tucci and M. Strassman},
  journal={Archives of Biochemistry and Biophysics},
  year={1968},
  volume={123},
  pages={235-239}
}
Accumulation of a-ketoglutaric acid in two nonallelic yeast mutants (Ly7 and Ly4) requiring lysine has been demonstrated. In addition to α-ketoglutarate, Ly7 accumulates homocitrate, and Ly4 accumulates both homocitrate and cis-homoaconitate. The cell-free preparations of Ly4 lack homoacunitase activity, but Ly7 has homocitrate synthetase and homoaconitase activities. The mutants that fail to accumulate homoisocitrate have so far been found to accumulate α-ketoglutarate, which is not… Expand
Biosynthesis of lysine in Saccharomyces cervisiae: properties and spectrophotometric determination of homocitrate synthase activity.
TLDR
A rapid assay is described for homocitrate synthase (EC 4.3.1.21) of the lysine biosynthetic pathway of Saccharomyces cerevisiae, where activity was dependent upon time, both substrates, and enzyme. Expand
Effect of Hydroxylysine on the Biosynthesis of Lysine in Saccharomyces
TLDR
Hydroxylysine acts as a growth inhibitor of Saccharomyces for a certain period of time and exerts a significant inhibition in vitro on the homocitric acid-synthesizing activity. Expand
Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus.
TLDR
Surprisingly, HACN does not show any activity when cis-aconitate is substituted for the substrate, even though other enzymes from the alpha-aminoadipate pathway can accept analogous tricarboxylic acid-cycle substrates, which suggests that the in vivo process for conversion of homocitrate into homoisocitrates requires two enzymes. Expand
Accumulation of 2-oxo acids in mutants ofAspergillus niger requiring lysine
TLDR
The accumulation of 2-oxoglutarate and 2- oxoadipate in the fermentation medium indicates that inA. Expand
Isocitrate Dehydrogenase and Glutamate Synthesis in Acetobacter suboxydans
TLDR
It is concluded that A. suboxydans can utilize the conventional tricarboxylic acid cycle enzymes to convert citrate to alpha-ketoglutarate which can then undergo a transamination to glutamate. Expand
Leaky mutation and coordinate regulation of the accumulation of lysine-precursors in Saccharomyces.
  • J. K. Bhattacharjee
  • Biology, Medicine
  • Canadian journal of genetics and cytology. Journal canadien de genetique et de cytologie
  • 1970
One of the lysine auxotrophs (ly12) of Saccharomyces exhibits a residual ability (leakiness) to grow in minimal medium. This mutant accumulates homocitric, cis-homoaconitic and homoisocitric acidsExpand
The fungal α-aminoadipate pathway for lysine biosynthesis requires two enzymes of the aconitase family for the isomerization of homocitrate to homoisocitrate
TLDR
The essential requirement of filamentous fungi for respiration versus the preference of yeasts for fermentation may have directed the evolution of aconitases contributing to energy metabolism and lysine biosynthesis. Expand
The lysine biosynthetic enzyme Lys4 influences iron metabolism, mitochondrial function and virulence in Cryptococcus neoformans.
TLDR
This study identified the ortholog of LYS4 in the human fungal pathogen, Cryptococcus neoformans, and found that LYS2 expression is regulated by iron levels and by the iron-related transcription factors Hap3 and HapX, and revealed that lysine uptake was mediated by two amino acid permeases and influenced by nitrogen catabolite repression. Expand
Relationship among the genes, enzymes, and intermediates of the biosynthetic pathway of lysine in Saccharomyces
SummaryGenetic lesions of 10 of the lysine loci in Saccharomyces have been provisionally correlated with the various enzymatic steps of the homocitric acid pathway for the biosynthesis of lysine. TheExpand
Homocitrate synthase from yeast.
  • A. Tucci, L. Ceci
  • Biology, Medicine
  • Archives of biochemistry and biophysics
  • 1972
TLDR
Homocitrate synthase activity has been partially purified from yeast and was sensitive to inhibition by lysine both in vivo and in vitro only at high concentrations ofLysine. Expand
...
1
2
...

References

SHOWING 1-8 OF 8 REFERENCES
Accumulation of tricarboxylic acids related to lysine biosynthesis in a yeast mutant.
Abstract Accumulation of tricarboxylic acids related to lysine biosynthesis has been demonstrated in a yeast mutant, Ly12, which requires lysine as a growth factor in synthetic medium but canExpand
Homocitric acid accumulation by a lysine-requiring yeast mutant.
TLDR
The excretion of homocitric acid by a lysine-requiring yeast mutant and its conversion into lysin convincingly establish the biosynthesis of lysines in yeast via the previously proposed scheme involving homologues of the citric acid cycle. Expand
Enzymatic formation of cis-homoaconitic acid, an intermediate in lysine biosynthesis in yeast.
TLDR
The enzyme, which has been named cis-homoaconitase, was separated from cis-aconsitase by ammonium sulfate precipitation, has an optimum pH of 8.6 in phosphate buffer, and is inhibited by p-chloromercuribenzoate, α,α'-dipyridyl, and o-phenanthroline. Expand
Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid.
Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis.
  • M. Strassman, L. Ceci
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1964