Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The regulation of alpha-ketogluterate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase, and malic enzyme has been studied in Bacillus subitilis. The levels of these enzymes increase rapidly during late exponential phase in a complex medium and are maximal 1 to 2 h after the onset of sporulation. Regulation of enzyme synthesis has been studied in the wild type and different citric acid cycle mutants by adding various metabolites to the growth medium. Alpha-ketoglutarate dehydrogenase is induced by glutamate or alpha-ketoglutarate; succinate dehydrogenase is repressed by malate; and fumarase and malic enzyme are induced by fumarate and malate, respectively. The addition of glucose leads to repression of the citric acid cycle enzymes whereas the level of malic enzyme is unaffected. Studies on the control of enzyme activities in vitro have shown that alpha-ketoglutarate dehydrogenase and succinate dehydrogenase are inhibited by oxalacetate. Enzyme activities are also influenced by the energy level, expressed as the energy charge of the adenylate pool. Isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, and malic enzyme are inhibited at high energy charge values, whereas malate dehydrogenase is inhibited at low energy charge. A survey of the regulation of the citric acid cycle in B.subtilis, based on the present work and previously reported results, is presented and discussed.
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PMID:Regulation of the dicarboxylic acid part of the citric acid cycle in Bacillus subtilis. 80 68

Under conditions of experimental myocardium infarction caused in dogs by ligation of the anterior descending branch of the left coronary artery, the activity of alpha-ketoglutarate dehydrogenase and succinate dehydrogenase in mitochondria of the cortex, cerebellum and medulla ablongata lowers most intensively on the first and fifth day after the appearance of acute myocardium infarction. Activation of the most important enzymes of the pentose-phosphate cycle (glucose-6-phosphate dehydrogenase and transketolase) which is clearly pronounced on the fifth day is observed in the mentioned sections. In the authors' opinions the above changes in the activity of the enzymes are due to the brain hypoxia which may be the main reason of disturbance in the function of the central nervous system under this disease.
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PMID:[Activity of enzymes of tricarboxylic and pentose-phosphate cycles in dog brain with myocardial infarction]. 88 27

The activity of the mitochondria internal membrane ensymes alpha-ketoglutarate dehydrogenase and succinate dehydrogenase was studied after rats poisoning with CCl4. It is established that the activity of these enzymes lowers considerably under effect of CCl4, which is more pronounced for alpha-ketoglutarate dehydrogenase. The pretreatment of animals with inducer of microsomal oxidases intensifies the damaging effect of CCl4 on the internal membranes of mitochondria and decreases the LD50 value for CCL4. Administration of actinomycin D simultaneously with polycyclic hydrocarbons prevents intensification of the CCl4 hepatotoxic effect caused by 3-methylcholanthrene and dibenz (a, h) anthracene.
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PMID:[Effect of tetrachloromethane on alpha-ketoglutarate dehydrogenase and succinate dehydrogenase activity in mitochondria of rat liver under conditions of administration of polycyclic hydrocarbons]. 89 14

Two freshwater bacteria, a Pseudomonas sp. and a Spirillum sp., were grown in continuous culture under steady-state conditions in L-lactate-, succinate-, ammonium- or phosphate-limited media. In Pseudomonas sp., NAD-independent and NAD-dependent L-lactate dehydrogenases, aconitase, isocitrate dehydrogenase and glucose 6-phosphate dehydrogenase activities increased up to 10-fold as the dilution rate (D) was decreased from 0.5 to 0.02 h-1, regardless of whether the growth-limiting nutrient was carbon, ammonium or phosphate. In contrast, 2-oxoglutarate dehydrogenase and succinate dehydrogenase activities were not influenced by D, and NADH oxidase activity increased with D. Spirillum sp. gave different results in some respects, but it also exhibited an increase in the activity of several enzymes at low D values. Such increases may emanate from release of catabolite repression, and catabolite repressors for the five enzymes in Pseudomonas sp. showing such increases are probably compounds of carbon, nitrogen and phosphorus. It is likely that increased enzyme syntheses in low D cultures represent the normal physiological state for bacteria in aquatic environments where growth occurs slowly under nutrient limitations. Such increases probably permit a more effective utilization of nutrients present at sub-saturating concentrations.
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PMID:Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture. 95 May 55

Carbon-14 was incorporated into oxalate and CO2 from either citrate-1,5-14C, succinate-1,4-14C, or fumarate-1,4-14C by cultures of Aspergillus niger pregrown on a medium which contained glucose as the sole carbon source and which did not allow citrate accumulation. In cell-free extracts of mycelium forming oxalate and CO2 from added citrate the following enzymes of the tricarboxylic acid (TCA) cycle were identified: citrate synthase CE 4.1.3.7), aconitate hydratase (EC4.2.1.3), NAD and NADP-dependent isocitrate dehydrogenase (EC 1.1.1.41, 1.1.1.42), (alpha-oxoglutarate dehydrogenase (EC 1.2.4.2), succinate dehydrogenase (EC 1.3.99.1), fumarate hydratase (EC 4.2.1.2), and malate dehydrogenase (EC 1.1.1.37). The in vitro activity of aconitate hydratase and of NADP-dependent isocitrate dehydrogenase was shown to be almost identical to the rate of in vivo degradation of citrate or to exceed this rate. The degradation of citrate to oxalate was inhibited completely by 9 mM fluoroacetate. It is concluded that the TCA cycle is involved in the formation of oxalate from citrate.
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PMID:Oxalate accumulation from citrate by Aspergillus niger. II. Involvement of the tricarboxylic acid cyclase. 115

The content of the Krebs cycle substrates and activity of dehydrogenases corresponding to them were studied in the brain and myocardium tissues of the non-linear male rats adapted to acute hypoxia under conditions of the altered gas medium. The content of malate and succinic acid was studied in the liver and skeletal muscles only. In the brain the total activity of malate dehydrogenase (MDH, EC 1.1.1.37, 1.1.1.39) alpha-ketoglutarate dehydrogenase (KDH, EC 1.2.4.2) pyruvate dehydrogenase (PDH, EC 1.2.4.1) and isocitrate dehydrogenase (ICDH, EC 1.1.1.41-42) is shown to be decreased and kept to be lowered in all the periods of the study. No essential shifts in the activity of these dehydrogenases were found in the myocardium. The activity of succinate dehydrogenase (SDH, EC 1.3.99.1) in both tissues lowers 48 h after the effect of the mentioned factors. Simultaneously the greatest changes in the level of the substrates were observed in the myocardium, in the brain they were less developed. In the liver the content of malate increases without pronounced changes in the amount of succinic acid and in the skeletal muscles the level of malate and succinic acid lowers.
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PMID:[Krebs cycle in tissue of rats subjected to combined effect of hypercapnia, hypoxia and cooling]. 121 51

While laboratory experimental model of coronary heart disease (according to Frol'kis et al.) is developed, activity of succinate dehydrogenase, alpha-ketoglutarate dehydrogenase, Na+, Ka(+)- and Mg2+ ATPase decreases, but activity of lactate dehydrogenase and concentrations of lactic and pyruvic acids in the heart tissue increase. At the same time concentration of glycogene increases more than twice. As far as we can see there is an evidence of a decrease of glycogene utilization due to change in levels of regulatory processes. Despite a decrease of ATP synthesis by the inhibition of tricarboxylic acid cycle the ATP:ADP relation reduces to ATP, as emphatic inhibition of ATPase in the heart tissues takes place in development of the model of the coronary heart disease. The relation between ATP and ADP is considered as a regulator of glycogene utilization. In the liver tissue activity of succinate dehydrogenase, alpha-ketoglutarate dehydrogenase, Na+, K(+)- and Mg2+ ATPase falls, while concentrations of lactic acid grow. No accumulation of glycogen is observed. It is obvious that there are controversial metabolic processes. Experimental data are discussed.
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PMID:[The relation between oxidative processes and the glycogen content in the heart and liver of rabbits with chronic ischemic heart disease]. 148 3

The maximal rate (Vmax) of some mitochondrial enzyme activities related to energy transduction (citrate synthase, alpha-ketoglutarate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, NADH-cytochrome c reductase, cytochrome oxidase) and amino acid metabolism (glutamate dehydrogenase, glutamate-pyruvate transaminase and glutamate-oxaloacetate transaminase) are evaluated in non synaptic ("free") and intrasynaptic mitochondria from brain hippocampus. The different mitochondrial populations were isolated from rat subjected to single i.p. treatment with saline solution, almitrine (30 mg/kg) and delta-yohimbine (10 mg/kg). In control rats, the mitochondrial populations exhibit different enzymatic patterns. Acute treatment with almitrine decreases cytochrome oxidase activity in intra-synaptic mitochondria, while acute treatment with delta-yohimbine decreases succinate dehydrogenase activity in both types of free and intra-synaptic mitochondria. NADH-cytochrome c reductase activity is also decreased by acute treatment with almitrine ("free" and "synaptic" mitochondria) and delta-yohimbine (synaptic mitochondria only).
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PMID:Factors involved in drug interference on enzyme activities of three mitochondrial populations from rat hippocampus. 180 34

The activity of alpha-ketoglutarate dehydrogenase and succinic dehydrogenase in readaptation after 15-day hypokinesia was within normal limits, whereas following 30-day hypokinesia it was enhanced on days 11-15. Pyruvate dehydrogenase exhibited hyperactivity in the end of readaptation week 2 both in 15- and 30-day hypokinesia which resulted in rat liver hyperactivity of glutamate dehydrogenase and transaminases. Normal levels of the latter were recorded on readaptation day 12-19.
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PMID:[Activity of various oxidases and transaminases in the rat liver in the readaptation period after hypokinesia up to 30 days]. 232 62

Continuous exposure of Chinese hamster ovary (CHO) cells to an atmosphere of 98% O2, 2% CO2 (normobaric hyperoxia) leads within a period of several days to cytostasis and clonogenic cell death. Here we report respiratory failure as an important early symptom of oxygen intoxication in CHO cells, resulting in a more than 80% inhibition of oxygen consumption within 3 days of hyperoxic exposure. This inhibition appeared to be correlated with selective inactivation of three mitochondrial key enzymes, NADH dehydrogenase, succinate dehydrogenase, and alpha-ketoglutarate dehydrogenase. The latter enzyme controls the influx of glutamate into the Krebs cycle and is particularly critical for oxidative ATP generation in most cultured cells, which depends on exogenous glutamine rather than glucose as a carbon source. As expected, the inactivation of alpha-ketoglutarate dehydrogenase was correlated with a fall in cellular glutamine utilization, which became apparent from the first day of hyperoxic exposure. Thereafter, glucose utilization and lactate excretion started to increase, up to 3-fold, indicating a cellular response to respiratory failure aimed at increased ATP generation from glycolysis. However, in spite of this response, the cellular ATP level progressively decreased, up to 2.5-fold. Thus, killing of CHO cells by normobaric hyperoxia seems to be due to a severe disturbance of mitochondrial metabolism eventually leading to a depletion of cellular ATP pools.
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PMID:Respiratory failure and stimulation of glycolysis in Chinese hamster ovary cells exposed to normobaric hyperoxia. 235 58


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