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Query: EC:1.1.1.41 (
isocitrate dehydrogenase
)
3,101
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
1. The effects of lipoate and asparagusate on animal and plant enzymes of the
TCA
cycle and related metabolic pathways were studied. 2. Lipoate inhibited bovine liver glutamate dehydrogenase [EC 1.4.1.3]. The inhibition may play a role in metabolic regulation. 3. Asparagusate inhibited lipoyl dehydrogenase [EC 1.6.4.3] from asparagus and lettuce competitively with respect to lipoate. Asparagusate had practically no effects on other asparagus enzymes. 4. Asparagusate strongly inhibited lipoyl dehydrogenase, glutamate dehydrogenase, and
isocitrate dehydrogenase
[EC 1.1.1.42] from animal sources, in competition with the corresponding substrate. 5. Asparagusate and lipoate also inhibited yeast glutamate dehydrogenase. 6. Based upon kinetic studies, the mode of these inhibitions is discussed.
...
PMID:Effects of asparagusate and lipoate on enzymes of the tricarboxylic acid cycle and related metabolic pathways. 77 25
Adult mice, Mus booduga were fed orally with bennzenehexachloride (BHC) at a dose of 50 mg/kg body weight every day for 1, 5 and 15 days. Significant decrease in the pyruvate content was observed at all periods of treatment. In support of this increase in lactate content and lactate dehydrogenase (LDH) activity was noticed in all the three tissues. Enzymes of
TCA
cycle namely
isocitrate dehydrogenase
(ICDH), succinate dehydrogenase (SDH) and malate dehydrogenase (MDH) were inhibited suggesting abnormality in mitochondrial oxidative metabolism as a consequence of BHC toxicity.
...
PMID:Changes in the carbohydrate metabolism in the selected tissues of Mus booduga gray after BHC treatment. 172 96
During growth on succinate, Acinetobacter calcoaceticus contains two forms of the enzyme
isocitrate dehydrogenase
. Addition of acetate to a lag-phase culture grown on succinate causes a dramatic increase in activity of form II of
isocitrate dehydrogenase
and in isocitrate lyase. Form II of
isocitrate dehydrogenase
may be responsible for the partition of isocitrate between the
TCA
cycle and the glyoxylate by-pass. This report describes the phosphorylation of the enzyme isocitrate lyase from A. calcoaceticus. This phosphorylation may be a regulatory mechanism for the glyoxylate by-pass.
...
PMID:Phosphorylation of Acinetobacter isocitrate lyase. 173 94
Studies on the tricarboxylic acid cycle (
TCA
cycle) enzymes of Penetrocephalus ganapatii reveal that the
TCA
cycle is only partially operative, as some of the enzymes at the start of the cycle viz. citrate synthase, aconitase and
isocitrate dehydrogenase
are found to be low in their activities. The high activities of malate dehydrogenase and fumarase, showing affinity towards a reverse direction, indicate that the
TCA
cycle operates in the reverse direction resulting in the formation of fumarate. The low succinate dehydrogenase/fumarate reductase ratio suggests that ATP generation may occur at site I of the respiratory chain during the reduction of fumarate into succinate.
...
PMID:Tricarboxylic acid cycle enzymes of a pseudophyllid cestode Penetrocephalus ganapatii. 233 84
Changes in energy metabolism during larval development in Caenorhabditis elegans have been investigated using phosphorus nuclear magnetic resonance (31P NMR). The relative concentrations of ATP, ADP, AMP, sugar phosphates, and other metabolites were observed to change during larval development, producing stage-specific spectra. These spectra are consistent with enzyme assays for
isocitrate dehydrogenase
and isocitrate lyase, indicating that high activity of the glyoxylate pathway during embryonic development decreases during the first larval (L1) stage, and respiration during the L2, L3, and L4 stages occurs preferentially through the
TCA
cycle. Metabolic strategies were further studied using mutants that are predisposed to enter the dauer stage, a developmentally arrested third-stage larva formed under conditions of overcrowding and limited food. After the L1 molt, energy metabolism in animals destined to become dauer larvae diverges from that of animals committed to growth. Relative to the L1, the L2 larvae committed to growth exhibit increased
isocitrate dehydrogenase
activity as well as increases in ATP and other high-energy phosphates, but predauer (L2d) larvae exhibit declining enzyme activities and declining levels of high-energy phosphates. The predominant phosphorus NMR signal in dauer larva extracts corresponds to inorganic phosphate. We conclude that metabolism is regulated during C. elegans larval development, with a major transition apparent after the L1 stage. This transition does not occur in larvae destined to form dauer larvae.
...
PMID:Developmental regulation of energy metabolism in Caenorhabditis elegans. 291 91
The intracellular distribution of enzymes of the
TCA
cycle was investigated in liver of rainbow trout. All enzymes of the cycle apart from succinyl thiokinase were detected. Citrate synthase, alpha-ketoglutarate dehydrogenase and succinate dehydrogenase were wholly mitochondrial. Fumarase, malate dehydrogenase, aconitase and NADP-
isocitrate dehydrogenase
were detected in both cytosol and mitochondria.
...
PMID:Intracellular distribution of tricarboxylic acid cycle enzymes in liver of rainbow trout Salmo gairdneri. 405 77
Histochemical studies have been made of the
isocitrate dehydrogenase
, succinic dehydrogenase, malate dehydrogenase, glutamate dehydrogenase, DPN diaphorase, TPN diaphorase, delta 5-3 beta-hydroxysteroid dehydrogenase and monoamine oxidase in the caput, corpus and cauda epididymides of normal and alpha chlorohydrin (6.5 mg/kg/9 days) treated rats. Administration of alpha chlorohydrin in a low dose caused a conspicuous decrease in all these enzymes except delta 5-3 beta-HSD, in various cell types of epididymal epithelium and sperms. Biochemical estimations of
isocitrate dehydrogenase
, succinic dehydrogenase, malate dehydrogenase and delta 5-3 beta-HSD have further supported and confirmed these histochemical observations. These changes in enzyme activities after treatment with low dose of alpha chlorohydrin strongly suggest that
TCA
cycle and amino acid metabolism of epididymis become defective, much earlier before any histological damage to the epididymis becomes visible.
...
PMID:Effects of low doses of alpha chlorohydrin on the dehydrogenases and oxidases of rat epididymal epithelium and sperms: a correlative histochemical and biochemical study. 694 44
The effect of DL alpha-lipoic acid on the nephrotoxic potential of gentamicin was examined. Intraperitoneal injection of gentamicin (100 mg/kg/day) to rats resulted in decreased activity of the glycolytic enzymes-hexokinase, phosphoglucoisomerase, aldolase and lactate dehydrogenase. The two gluconeogenic enzymes--glucose-6-phosphatase and fructose-1,6-diphosphatase, the transmembrane enzymes namely the Na+, K(+)-ATPase, Ca(2+)-ATPase, Mg(2+)-ATPase and the brushborder enzyme alkaline phosphatase, also showed decreased activities. This decrease in the activities of ATPases and alkaline phosphatase suggests basolateral and brush border membrane damage. Decreased activity of the
TCA
cycle enzymes
isocitrate dehydrogenase
(ICDH), succinate dehydrogenase (SDH) and malate dehydrogenase (MDH), suggests a loss in mitochondrial integrity. These biochemical disturbances were effectively counteracted by lipoic acid administration. Lipoic acid administration by gastric intubation at two different concentrations (10 mg and 25 mg/kg/day) brought about an increase in the activity of the glycolytic enzymes, ATPases and the
TCA
cycle enzymes. The gluconeogenic enzymes however showed a further decrease in their activities at both the concentrations of lipoic acid administered. These observations shed light on the nephroprotective action of lipoic acid against experimental aminoglycoside toxicity and the protection afforded at 25 mg/kg/day of lipoic acid was noted to be higher than that at 10 mg level.
...
PMID:Role of DL alpha-lipoic acid in gentamicin induced nephrotoxicity. 765 73
Using two-dimensional gel electrophoresis and N-terminal amino acid sequencing analysis, we demonstrate that a mutant of the global regulatory protein ArcA fails to decrease the synthesis of the
TCA
cycle enzymes malate dehydrogenase,
isocitrate dehydrogenase
, lipoamide dehydrogenase E3 and succinate dehydrogenase in response to stasis, while the increased production of the glycolysis enzymes phosphoglycerate mutase and pyruvate kinase is unaffected. Microcalorimetric and respiratory measurements show that the continued production of
TCA
cycle enzymes in the (delta)arcA mutant is manifested as an elevated rate of respiration and total metabolic activity during starvation. The (delta)arcA mutant is severely impaired in surviving prolonged periods of exogenous carbon starvation, a phenotype that can be alleviated by overproducing the superoxide dismutase SodA. In addition, flow cytometry demonstrates that starving (delta)arcA mutant cells, in contrast to wild-type cells, fail to perform reductive division, remain large and contain multiple chromosomal copies. We suggest that the ArcA-dependent reduced production of electron donors and the decreased level and activity of the aerobic respiratory apparatus during growth arrest is an integral part of a defense system aimed at avoiding the damaging effects of oxygen radicals and controlling the rate of utilization of endogenous reserves.
...
PMID:Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. 867 Aug 22
The bradyzoite and tachyzoite forms of Toxoplasma gondii, purified from infected animals, were analysed for their activities of phosphofructokinase, pyruvate kinase, lactate dehydrogenase, NAD(+)- and NADH-linked isocitrate dehydrogenases, and succinic dehydrogenase. Both developmental stages contained high activities of phosphofructokinase (specific for pyrophosphate rather than ATP), pyruvate kinase and lactate dehydrogenase, suggesting that energy metabolism in both forms may centre around a high glycolytic flux linked to lactate production. The markedly higher activity of the latter two enzymes in bradyzoites suggests that lactate production is particularly important in this developmental form. NAD(+)-specific
isocitrate dehydrogenase
was not detectable in either stage of the parasite (and proved useful as a measure of the purity of the bradyzoite preparation), whereas both parasite forms contained low activities of NADP(+)-linked isocitrate dehydrogenase. The results are consistent with the bradyzoites lacking a functional
TCA
cycle and respiratory chain and are suggestive of a lack of susceptibility of this developmental stage to atovaquone.
...
PMID:Enzymes of energy metabolism in the bradyzoites and tachyzoites of Toxoplasma gondii. 893 63
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