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:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A histochemical evaluation of the activity of chosen oxido-reductive enzymes of the cardiac muscle connected with the citric acid cycle, glycolysis and pentose shunt in the early experimental alloxan diabetes period in white rats has been carried out. Dehydrogenases: succinate, isocitrate and glucose-6-phosphate indicated a decrease in the enzymatic activity while the lactate dehydrogenase activity did not undergo any change. An increase in the intensity of the histoenzymatic reaction only concerned glutamate dehydrogenase. The presented histoenzymatic evidence of changes in the enzymatic activities may speak for the possibility of an existence of a direct diabetes influence on the cardiac muscle metabolism.
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PMID:Some histochemical observations on the myocardial metabolism in experimental conditions. Part II. 9 52

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
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PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

As part of a detailed analysis of the specific enzyme metabolism in individual hypothalamic nuclei during different endocrinological and behavioral states, quantitative distribution of a group of enzymes representative of major metabolic pathways was examined. Malic dehydrogenase (MDH), representative of the citric acid cycle, lactic dehydrogenase (LDH), of glycolysis, glutamic dehydrogenase (GDH), of glutamate metabolism, and glucoseo-6-phosphate dehydrogenase (G-6-PDH), of the pentose pathway, were measured in 11 hypothalamic nuclei, the cerebral cortex, and the cerebellum of adult female rats neonatally treated with testosterone propionate (TP). Several significant metabolic changes occurred in specific hypothalamic nuclei following neonatal TP (1 mg) treatment. MDH activity was significantly reduced in the suprachiasmatic (11%), supraoptic (13%), and anterior (9%) nuclei. No statistically significant changes occurred in nuclei of the middle or posterior hypothalamus. LDH was significantly elevated only in the lateral preoptic areas (23%). Several significant increases of G-6-PDH activity occurred in the following nuclei of the anterior hypothalamus: medial preoptic (32%), lateral preoptic (33%), supraoptic (13%), and paraventricular (23%). No statistically significant changes occurred in nuclei of the middle or posterior hypothalamus; these results were similar to those for MDH and LDH. GDH activity was generally elevated in all of the hypothalamic nuclei examined, except in the anterior nucleus. Significant increases of enzyme level were found in each of the major divisions of the hypothalamus. In the anterior hypothalamus, GDH activity in the paraventricular nucleus rose significantly (16%); in the middle hypothalamus, lateral ventromedial and arcuate nuclear levels were elevated (14 and 17%), and medial and posterior nuclear levels were higher than control values (32 and 36%) in the posterior hypothalamus.
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PMID:Quantitative histochemical studies of the hypothalamus: dehydrogenase enzymes following androgen sterilization. 41 65

Activities corresponding to the enzymes glucokinase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, malate dehydrogenase, pyridine nucleotide independent malate dehydrogenase, and glutamate dehydrogenase were found in cell free extracts from Neisseria elongata subsp. gkcolytica. Activities corresponding to 6-phosphogluconate dehydrase and 2-keto-3-deoxy-6-phosphogluconate aldolase were not found. Glucose was catabolized only vira the pentose phosphate pathway. The radiorespirometric findings suggest an extensive recycling of the triose and fructose phosphates. There was no evidence for formation of pyruvate from glucose. Glutamate was oxidized via the tricarboxylic acid cycle. Pyruvate and acetate were obviously catabolized by the glyoxylic and tricarboxylic acid cycles, as in N. elongata.
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PMID:The catabolism of glucose, glutamate pyruvate and acetate in Neisseria elongata subsp. glycolytica. 85 8

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49

Selected aspects of the metabolism of Plasmodium falciparum are reviewed, but conclusions based on the study of other species of plasmodia are intentionally not included since these may not be applicable. The parasites increase glucose consumption 50-100 fold as compared to uninfected red cells; most of the glucose is metabolized to lactic acid. The parasite contains a complete set of glycolytic enzymes. Some enzymes such a hexokinase, enolase and pyruvate kinase are vastly increased over corresponding levels in uninfected red cells. However, the pathway for synthesizing 2,3-diphosphoglycerate (2,3-DPG) is absent. Parasitized red cells show a decline in the concentration of 2,3-DPG which may function as an inhibitor for certain essential enzyme pathways. Pentose shunt activity is increased in absolute terms, but as a percent of total glucose consumption, there is a decrease during parasite infection of the red cell. The parasite contains a gene for G6PD and can produce a small quantity of parasite-encoded enzyme. It is not clear if the production of this enzyme can be up-regulated in G6PG deficient host red cells. The NADPH normally produced by the pentose shunt can be obtained from other parasite pathways (such as glutamate dehydrogenase). NADPH may subserve additional needs in the infected red cell such as driving diribonucleotide reductase activity--a rate limiting enzyme in DNA synthesis. The role of NADPH in protecting the parasite-red cell system against oxidative stress (via glutathione reduction) remains controversial. Parasitized red cells contain about 10 times more NAD(H) than uninfected red cells, but the NADP(H) content is unchanged.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Plasmodium falciparum carbohydrate metabolism: a connection between host cell and parasite. 225 22

The literature concerning the metabolism of carbon and nitrogen compounds in ectomycorrhizal associations of trees is reviewed. The absorption and translocation of mineral ions by the mycelia require an energy source and a reductant which are both supplied by respiratory catabolism of carbohydrates produced by the host plant. Photosynthates are also required to generate the carbon skeletons for amino acid and carbohydrate syntheses during the growth of the mycelia. Competition for photosynthates occurs between the fungal cells and the various vegetative sinks in the host tree. The nature of carbon compounds involved in these processes, their routes of metabolism, the mechanisms of control and the partitioning of metabolites between the various sites of utilization are only poorly understood. Both ascomycetous and basidiomycetous ectomycorrhizal fungi synthesize and some, if not all, accumulate mannitol, trehalose and triglycerides. The fungal strains employ the Embden--Meyerhof pathway of glucose catabolism and the key enzymes of the pentose phosphate pathway (6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, transaldolase and transketolase). Anaplerotic CO2 fixation, via pyruvate carboxylase and/or phosphoenolpyruvate carboxykinase, provides high pools of amino acids. This process could be important in the recapture and assimilation of respired CO2 in the rhizosphere. The ectomycorrhizas are thought to contain the Embden--Meyerhof pathway, the pentose phosphate pathway and the tricarboxylic acid cycle, which provide the carbon skeletons for the assimilation of ammonia into amino acids. The main route of assimilation of ammonia appears to be through the glutamine synthetase-glutamate synthase cycle in the ectomycorrhizas. Glutamate dehydrogenase plays a minor role in this process. Glutamate dehydrogenase and glutamine synthetase are present in free-living ectomycorrhizal fungi and they participate in the assimilation of ammonia and the synthesis of amino acids through the glutamate dehydrogenase/glutamine synthetase sequence. In both in vitro cultures of fungi and ectomycorrhizas, the assimilated nitrogen accumulates in glutamine. Glutamine, but also ammonia, are thought to be exported from the fungal tissues to the host cells. Studies on the metabolism of ectomycorrhizas and ectomycorrhizal fungi have focused on the metabolic pathways and compounds which accumulate in the symbiotic tissues. Studies on regulation of the overall process, and the control of enzyme activity in particular, are still fragmentary.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Carbon and nitrogen metabolism in ectomycorrhizal fungi and ectomycorrhizas. 312 Jul 92

Effect of naphthoquinone levels on the activity of enzymes involved in glycolysis and pentose phosphate cycles was studied in male rats. Under conditions of primary and secondary K-avitaminosis the enzymatic activity, limiting these cycles, (aldolase of fructose-1,6-diphosphate, glucose phosphate isomerase and glucose-6-phosphate dehydrogenase) was increased, while the mitochondrial glutamate dehydrogenase activity was decreased. As a result of metabolic transformations under conditions of K-avitaminosis (primary and secondary) concentration of DNA in the animal tissues was lowered.
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PMID:[The effect of vitamin K on the activity of glycolysis and pentose phosphate cycle enzymes]. 342 Aug 14

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
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PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

NH+4 produced as a result of the activation of AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) was utilized effectively to form glutamate from 2-oxoglutarate by the action of NADP-glutamate dehydrogenase (L-glutamate:NADP+ oxidoreductase (deaminating), EC 1.4.1.4) under in situ conditions in yeast cells: the decrease in total adenylates stoichiometrically corresponded to the production of NH+4 plus glutamate. Reducing equivalents, NADPH, for the synthesis of glutamate can be supplied by the pentose phosphate pathway. The addition of spermine, an activator of AMP deaminase without changes in glutamate dehydrogenase activity, resulted in an increase in ammonium concentration, which can enhance the formation of glutamate from 2-oxoglutarate. A close correlation of NADP-glutamate dehydrogenase with AMP deaminase activity was observed under various growth conditions. The interaction of the AMP deaminase-ammonium system with glutamate dehydrogenase as an ammonium-assimilating reaction may participate in the control of the cellular NH+4 level, which can correlate with glycolysis.
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PMID:Interaction of the AMP deaminase-ammonium system with glutamate dehydrogenase in yeast. 675 3


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