EC Number   |
General Information |
Reference |
|---|
    4.2.1.3 | malfunction |
acnA expression is enhanced in an acnB mutant |
730343 |
| 4.2.1.3 | malfunction |
acnA mutants grow very poorly, have secondary mutations, and are quickly outgrown by pseudorevertants. The acnA gene is stably interrupted in a citrate synthase (gltA) null background, indicating that the intracellular accumulation of citrate may be deleterious for survival. No aconitase activity is detected in this mutant. To uncover a function of AcnA beyond its catalytic role in the tricarboxylic acid cycle pathway, the citrate synthase/aconitase (acnA) double mutant is compared with the citrate synthase single mutant. No differences are found |
704318 |
| 4.2.1.3 | malfunction |
aconitase down-regulation suppresses pink1 mutant phenotypes. In contrast to partial loss of aconitase that rescues mitochondrial defects in pink1 mutants, overexpression of aconitase in transgenic mice causes mitochondrial morphological defects and swelling of mitochondria in dopaminergic neurons |
730672 |
| 4.2.1.3 | malfunction |
cell wall-modifying enzyme peptidoglycan deacetylase, PgdA expression is significantly decreased in an acnB mutant. Mutant strain is more susceptible to lysozyme-mediated killing and is attenuated in its ability to colonize mice |
729936 |
| 4.2.1.3 | malfunction |
in acnB mutants proliferation of pepper plants is significantly impaired. Deletion of acnB leads to reduced hypersensitive response induction in resistant pepper plants and an increased susceptibility to the superoxide generating compound menadione |
730692 |
| 4.2.1.3 | malfunction |
mutant shows severe defects in morphology and physiology, as is unable to form any aerial mycelium, spores or phosphinothricin tripeptide |
729645 |
| 4.2.1.3 | metabolism |
ACO is an enzyme that catalyzes the isomerization of citrate to isocitrate in both the Krebs cycle and the glyoxylate cycle |
-, 715094 |
| 4.2.1.3 | metabolism |
the enzyme is involved in the methylcitric acid cycle |
-, 747131 |
| 4.2.1.3 | physiological function |
a comparative proteomic approach with the wild-type and the AcnA mutant strain under oxidative stress conditions identifies up to 90 differentially expressed proteins in both strains. Some of the respective target mRNAs show the presence of iron responsive element motifs. Aconitase controls translation elongation factor Tu expression upon oxidative stress and may be directly involved in regulation upon oxidative stress |
-, 749146 |
| 4.2.1.3 | physiological function |
a zinc hyper-tolerant deletion mutant, which lacks the Pif1 DNA helicase, shows increased iron accumulation, redistribution of the aconitase protein to mitochondria, and also a loss of aconitase activity, despite normal Aco1 protein levels being present. Lack of Aco1 enzymatic activity in mitochondria, citrate accumulation and lack of activity of [Fe-S] enzymes, e.g. succinate dehydrogenase, appear to be direct molecular indicators of increased zinc tolerance |
748566 |
