Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.37 (malate dehydrogenase)
 4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glutamine is utilized at a high rate (fourfold higher than that of glucose) by isolated incubated lymphocytes and produces glutamate, aspartate, lactate and ammonia. The pathway for glutamine metabolism includes the reactions catalysed by glutaminase, aspartate aminotransferase, oxoglutarate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. In fact little if any of the carbon of the glutamine that is used is converted to acetyl-CoA for complete oxidation. For this reason, the oxidation of glutamine is only partial and, in an analogous manner to the terminology used to describe the partial oxidation of glucose to lactate as glycolysis, the term glutaminolysis is used to describe the process of partial glutamine oxidation. The role of glutaminolysis in lymphocytes and perhaps other rapidly dividing cells is to provide both nitrogen and carbon for precursors for synthesis of macromolecules (e.g. purines and pyrimidines for DNA and RNA) and also energy. However, the rate of glutamine utilization by lymphocytes is markedly in excess of the precursor requirements (which are at most 4%) and if glutamine was vitally important in energy production it would be expected that more would be converted to acetyl-CoA for complete oxidation via the Krebs cycle. Indeed most of the energy for lymphocytes may be obtained by the complete oxidation of fatty acids and ketone bodies. Consequently the role of the high rate of glutaminolysis in lymphocytes and other rapidly dividing cells may be identical to that of glycolysis: the high rates provide ideal conditions for the precise and sensitive control of the rate of use of the intermediates of these pathways for biosynthesis when required. High rates of glycolysis and glutaminolysis can be seen as part of a mechanism of control to permit synthesis of macromolecules when required without any need for extracellular signals to make more glucose or glutamine available for these cells. In order to maintain a high rate of glutaminolysis despite fluctuation in the plasma level of glutamine, the flux through the glutaminolytic pathway can be controlled and the key processes in the lymphocyte that may play a role in this process include glutamine transport across the cell and mitochondrial membranes, glutaminase and oxoglutarate dehydrogenase. Changes in the intracellular concentration of Ca2+ may play a role in control of one or more of these reactions.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Glutamine metabolism in lymphocytes: its biochemical, physiological and clinical importance. 390 97

The experiments on (CBA X C57BL/6)F1 mice have shown that regular corazol injections in subliminal doses stimulated seizure susceptibility (pharmacological kindling). Cytophotometric assay of the activity of oxidative metabolism enzymes (glutamate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, alpha-oxoglutarate dehydrogenase, lactate dehydrogenase) and GABA-transaminase in the sensorimotor cortex of kindled mice in post-convulsive period, and 24 hours or 30 days after corazol injections were discontinued, has revealed some specific alterations of the enzymes under study, that suggest the existence of two phases of energy metabolism disturbances. The first phase (24 hours after corazol injections were discontinued) is characterized by intensified succinic acid oxidation, while the second phase (30 days after the last injection) is characterized by anaerobic glycolysis in neuronal and glial cells. Inhibition of GABA-transaminase activity was particularly marked in postconvulsive period. From a molecular point of view these data may be considered as enzyme disturbances during stimulation of seizure susceptability or seizure activity and as a compensation component ensuring anticonvulsive mechanisms and reparative processes (antagonistic principle of molecular mechanism regulation) during activation of antiepileptic system.
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PMID:[Changes in the dehydrogenase and GABA transaminase activity in the cerebral cortex during corazol kindling]. 394 8

The purpose of this study was to assess the relationship between muscle fiber type distribution and enzymatic characteristics in sedentary male and female subjects. Muscle biopsy samples from the vastus lateralis muscle of 38 females and 37 males were analyzed to determine the fiber type composition (I, IIa, and IIb), the fiber size, and maximal activities of enzyme markers of energy metabolic pathways. Significant correlations were found (p less than 0.05) between percent fiber type I area and hexokinase (r = -0.39), phosphofructokinase (r = -0.39), lactate dehydrogenase (r = -0.41), and oxoglutarate dehydrogenase (r = 0.33) activities, whereas such correlations with total phosphorylase (r = -0.02), malate dehydrogenase (r = 0.12), and 3-hydroxyacyl CoA dehydrogenase (r = 0.12) activities were not significant. The results of the present study also suggest the presence of a significant but low covariation of less than 30% between the fiber type distribution and muscle enzyme activities. They confirm the presence of an important metabolic heterogeneity independent of the muscle fiber type distribution in sedentary male and female subjects. Moreover, these results indicate that sedentary males exhibit a lower mean value of percent fiber type I and higher glycolytic enzyme activities than sedentary females.
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PMID:Skeletal muscle histochemical and biochemical characteristics in sedentary male and female subjects. 398 89

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.
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PMID:Intracellular distribution of tricarboxylic acid cycle enzymes in liver of rainbow trout Salmo gairdneri. 405 77

Forty-eight sedentary and 39 quite active or well-trained men participated in this study. Muscle biopsy samples were taken from the vastus lateralis for the determination of fiber type composition (I, IIa, IIb), fiber type area, and assay of the following enzymes: malate dehydrogenase (MDH), 3-hydroxyacyl CoA dehydrogenase (HADH) and oxoglutarate dehydrogenase (OGDH). Maximal oxygen uptake (VO2max) was determined with a progressive cycle ergometer test, while endurance performance or maximal aerobic capacity (MAC) was defined as the total work output during a 90-min cycle ergometer test. Correlation analysis revealed no evidence of association between fiber type composition and VO2max kg-1 or MAC kg-1 in sedentary subjects, while active men exhibited significant correlation between % type I (r = 0.52), % type IIb (r = 0.31) and VO2max kg-1. Enzyme activities were not significantly correlated with MAC kg-1 and VO2max kg-1 in sedentary men while active men exhibited significant correlation for the three enzymes (0.37 less than or equal to r less than or equal to 0.51) with VO2max kg-1. These results show that the contribution of muscle fiber type and enzyme activities to aerobic performance may be inflated from a statistical point of view by the training status heterogeneity of subjects. They also suggest that variation in these muscle characteristics does not account for the individual differences in aerobic performance of subjects who have never trained before. Therefore, the assessment of muscle characteristics is not as useful as originally thought for the detection of individuals with a high potential for endurance performance among untrained subjects.
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PMID:Relationships between skeletal muscle characteristics and aerobic performance in sedentary and active subjects. 408 74

Crude extracts of both vegetative cells and glycerol-induced microcysts of Myxococcus xanthus contained the following enzyme activities: phosphofructokinase, phosphoglucoisomerase, fructose-1,6-diphosphatase, fructosediphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate carboxylase, citrate synthase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and uridine diphosphate glucose pyrophosphorylase. With the exception of isocitrate dehydrogenase, which was present at a fivefold higher concentration in microcysts, all activities in extracts from both types of cells were essentially equal. Hexokinase and pyruvate kinase could not be detected in extracts from either type of cell. Microcysts metabolized acetate at a lower rate than did vegetative cells. Most of this decrease was reflected in a substantial decrease in ability of microcysts to oxidize acetate to CO(2). In addition, microcysts and vegetative cells showed a different distribution of (14)C-label from incorporated acetate.
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PMID:Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. 430 96

The specific activities of isocitric dehydrogenase, alpha-ketoglutaric dehydrogenase, succinic dehydrogenase, malic dehydrogenase, and reduced nicotinamide adenine dinucleotide (NADH) oxidase were determined in extracts of Nitrosomonas europaea and compared with the corresponding values for Anacystis nidulans and autotrophically grown Hydrogenomonas eutropha. In common with other obligate autotrophs and in contrast to facultative autotrophs, Nitrosomonas extracts lacked alpha-ketoglutaric dehydrogenase and KCN-sensitive NADH oxidase activity and had low succinic dehydrogenase activity. The Nitrosomonas NADH oxidase appeared to be of the peroxidase type.
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PMID:Biochemical basis of obligate autotrophy in Nitrosomonas europaea. 430 22

The transport of the tricarboxylic acid cycle C(4)-dicarboxylic acids was studied in both the wild-type strain and tricarboxylic acid cycle mutants of Bacillus subtilis. Active transport of malate, fumarate, and succinate was found to be inducible by these dicarboxylic acids or by precursors to them, whereas glucose or closely related metabolites catabolite-repressed their uptake. l-Malate was found to be the best dicarboxylic acid transport inducer in succinic dehydrogenase, fumarase, and malic dehydrogenase mutants. Succinate and fumarate are accumulated over 100-fold in succinic dehydrogenase and fumarase mutants, respectively, whereas mutants lacking malate dehydrogenase were unable to accumulate significant quantities of the C(4)-dicarboxylic acids. The stereospecificity of this transport system was studied from a comparison of the rates of competitive inhibition of both succinate uptake and efflux in a succinate dehydrogenase mutant by utilizing thirty dicarboxylic acid analogues. The system was specific for the C(4)-dicarboxylic acids of the tricarboxylic acid cycle, neither citrate nor alpha-ketoglutarate were effective competitive inhibitors. Of a wide variety of metabolic inhibitors tested, inhibiors of oxidative phosphorylation and of the formation of proton gradients were the most potent inhibitors of transport. From the kinetics of dicarboxylic acid transport (K(m) approximately 10(-4) M for succinate or fumarate in succinic acid dehydrogenase and fumarase mutants) and from the competitive inhibition studies, it was concluded that an inducible dicarboxylic acid transport system mediates the entry of malate, fumarate, or succinate into B. subtilis. Mutants devoid of alpha-ketoglutarate dehydrogenase were shown to accumulate both alpha-ketoglutarate and glutamate, and these metabolites subsequently inhibited the transport of all the C(4)-dicarboxylic acids, suggesting a regulatory role.
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PMID:Properties of an inducible C 4 -dicarboxylic acid transport system in Bacillus subtilis. 463 50

A technique was developed for the detection, on agar, of mutants of Bacillus subtilis that lacked a functional tricarboxylic acid cycle. Mutants devoid of detectable levels of aconitase, isocitric dehydrogenase, alpha-ketoglutarate dehydrogenase, succinic dehydrogenase, fumarase, and malate dehydrogenase have been isolated and characterized. Several mutants with conditionally expressible lesions, including a mutant with a heat-sensitive citrate synthase, have also been isolated. All of the mutants examined express all the biochemical markers normally absent in early-stage sporulation mutants except elastase, and some of these mutants sporulated nearly as well as the prototroph.
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PMID:Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. 499 41

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate-cytochrome c oxidoreductase and NADH-cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP(+)-linked) and NADPH-cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD(+)- and NADP(+)-linked), alpha-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD(+)-linked), glutamate-oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, alpha-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD(+)- and NADP(+)-linked), glutamate dehydrogenase (NAD(+)-linked), glutamate-oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.
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PMID:The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria. 566 Jun 27


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