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)

Effects of repeated administration of benthiocarb on the nitrogen metabolism of hepatic and neuronal systems have been studied. Repeated benthiocarb treatment was associated with significant decrease in proteins with a concomitant increase in free amino acids (FAA) and specific activity levels of proteases suggesting impaired protein synthesis or elevated proteolysis. The glycogenic aminotransferases showed a significant elevation in both the tissues indicating high feeding of ketoacids into oxidative pathway for efficient operation of TCA cycle to combat energy crisis during induced benthiocarb stress. However, the activity levels of branched-chain aminotransferases decreased suggesting their reduced contribution of intermediates to TCA cycle. A comparative evaluation of the activity levels of ammonogenic enzymes, AMP deaminase, adenosine deaminase and glutamate dehydrogenase (GDH) indicated that ammonia was mostly contributed by nucleotide deamination rather than by oxidative deamination. GDH exhibited reduced activity due to low availability of glutamate. In accordance with increased levels of urea, the activity levels of arginase, a terminal enzyme of urea cycle was increased suggesting increased urea cycle operation in order to combat the increased ammonia content. As the presence of urea cycle in the brain is rather doubtful, the conversion of ammonia to glutamine for the synthesis of GABA is envisaged in brain whereas in liver, excess ammonia was converted to urea through ornithine-arginine reacting system. The increased glutaminase activity observed during benthiocarb intoxication is accounted for counteracting acidosis or maintenance of metabolic homeostasis. Arginase, a terminal enzyme of ornithine cycle showed increased activity denoting the efficient potentiality of tissues to avert ammonia toxicity. The changes observed in tissues of rat administered with benthiocarb reflects a shift in nitrogen metabolism for efficient mobilization of end products of protein catabolism.
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PMID:Perturbations in nitrogen metabolism of brain and liver of rat following repeated benthiocarb administration. 266 46

The activities of aspartate and alanine transaminase, serine dehydratase, arginase, glutamate dehydrogenase, adenylate deaminase and glutamine synthetase were determined in the stomach and small intestine of developing rats. Despite the common embryonic origin of the intestine and stomach, their enzymes showed quite different activity levels and patterns of development, depending on their roles. Most enzyme activities were low during late intrauterine life and after birth, attaining adult levels with the change of diet at weaning. No arginase activity was found in the stomach and no changes were detected in adenylate deaminase in the stomach or intestine throughout the period studied. Alanine transaminase, serine dehydratase and, to some extent, glutamine synthetase levels, significantly higher in late intrauterine life, decreased after birth, suggesting that the foetal stomach has a transient ability to handle amino acids.
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PMID:Activities of amino acid metabolizing enzymes in the stomach and small intestine of developing rats. 286 86

There was a nil arginase and serine dehydratase activities in interscapular brown adipose tissue, but the activity of adenylate deaminase, glutamine synthetase, glutamate dehydrogenase and the aspartate, alanine and branched chain amino acid transaminases was higher than those of white adipose tissue; the differences were diminished when expressed per unit of protein weight. Brown adipose tissue enzyme activities were in a range between those of liver and muscle. The high amino acid handling capabilities, together with its physiological role, suggest that brown adipose tissue can metabolize significant amounts of amino acids, its enzyme pattern being different both from white adipose tissue, as well as of liver and muscle.
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PMID:Activities of enzymes of amino acid metabolism in rat brown adipose tissue. 287 38

The effect of 24-hr starvation on the amino acid pool composition and its concentration ratios with respect to blood and plasma as well as the activities of alanine, aspartate and branched chain amino acid transaminases, glutamate dehydrogenase, glutamine synthetase and adenylate deaminase have been studied in rat brown adipose tissue. Starvation induced a considerable decrease of pool amino acid concentration. Alanine and taurine were the amino acids in which the decrease was more marked. Small changes were observed in the activities of the enzymes studied, with decreases only in glutamate dehydrogenase and adenylate deaminase. These changes agree with a decrease in amino acid utilization in this tissue induced by starvation.
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PMID:Effect of 24-hour starvation on amino acid pool composition and enzyme activities of rat brown adipose tissue. 288 93

The amino acid pool composition and its concentration ratios with respect to blood and plasma, as well as the activities of alanine, aspartate and branched chain amino acid transaminases, glutamine synthetase, adenylate deaminase and glutamate dehydrogenase have been studied in the interscapular brown adipose tissue of control, 12-h cold-exposed and 15-day cold-acclimated rats. Cold temperature affected the amino acid metabolism and pool composition more intensely after 15 days than after 12-h cold-exposure, even though the patterns of change were very similar in both groups. Cold temperatures induced a decrease in glutamine and an increase in glutamate concentration in the tissue. This probably increased the metabolism of branched chain amino acids and caused a decrease in adenylate deaminase activity. It also seemed to increase alanine utilization. We concluded that amino acid metabolism in brown adipose tissue is enhanced by cold temperature acclimation.
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PMID:Effect of cold-temperature exposure and acclimation on amino acid pool changes and enzyme activities of rat brown adipose tissue. 288 9

The activities of alanine, aspartate and branched-chain amino acid transaminases, glutamate dehydrogenase, glutamine synthetase and adenylate deaminase have been studied in liver of male rats exposed [12 hours at 4 degrees C] or acclimated [15 days at 4 degrees C] to cold temperature. Cold temperature induced an increase of the activities of glutamate dehydrogenase and alanine and aspartate transaminases both in cold-exposed and cold-acclimated animals; adenylate deaminase activity diminished after 15-day cold acclimation. There were not significant changes induced by cold temperature in the activities of the other two enzymes studied. These results agree with a possible direct implication of amino acid utilization by the liver in the context of the overall thermogenic response to cold temperature.
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PMID:Influence of cold exposure on liver amino acid metabolism enzymes of the rat. 290 59

Twenty-one enzymes of different metabolic systems were measured in the rabbit fast-twitch tibialis anterior (TA) muscle after electrical stimulation (10 Hz, 24 h/day) for 1 day to 10 wk. Nine analytical methods are either new, (3-oxoacid CoA-transferase, branched-chain-amino-acid aminotransferase, carnitine acetyltransferase, thiolase), improved (glutamate dehydrogenase, glycogen synthase, adenylic acid deaminase), or specially adapted (hexokinase, phosphoglucomutase). The activities (based on protein) of 12 mitochondrial or partly mitochondrial enzymes were lower in control TA than in control (slow) soleus (30-84% of soleus level). After 2 wk, 11 of these had surpassed the control soleus level. Maximal increases (3- to 14-fold) occurred after 2-5 wk, and thereafter six of the enzymes declined, whereas the other five maintained or increased their levels. Five glycolytic and two high-energy phosphate transfer enzymes, originally much higher in control TA than in control soleus, decreased gradually to levels at 8-10 wk only 27-123% higher than in soleus. Noncollagen protein concentration dropped 46%, explained largely by a sixfold increase in extracellular (chloride) space and a modest increase in collagen. The data constitute strong evidence for coordinate regulation of (mainly cytosolic) enzymes of glycolysis, glycogenolysis, gluconeogenesis, and high-energy phosphate transfer. Changes in the (mainly mitochondrial) enzymes of oxidative metabolism were more divergent, partly because of a hitherto undescribed secondary phase in the metabolic response. This phase may reflect a lower energy consumption in muscles adapted to continuous activity.
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PMID:Chronic stimulation of mammalian muscle: changes in enzymes of six metabolic pathways. 294 40

Denervated dog gastrocnemius muscle has shown a progressive decrease in total protein content, alanine aminotransferase (AIAT), aspartate aminotransferase (AAT) and glutamate dehydrogenase (GDH) activity levels and elevation in free amino acid, ammonia, urea, glutamine contents and AMP deaminase activity levels during post-neurectemic days. The possible implications of these findings are discussed in relation to denervation atrophy.
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PMID:Skeletal muscle protein metabolism under denervation atrophy in dog, Canis domesticus. 357 Apr 36

1. The activity of several tricarboxylic acid-cycle-associated dehydrogenases, adenine-metabolizing enzymes and glutathione reductase and the content of myoglobin were measured in rat diaphragm muscle after unilateral nerve section. 2. Consistent with morphological disintegration of the mitochondria there was a rapid diminution in activity of NAD- and NADP-linked isocitrate dehydrogenase, malate dehydrogenase and glutamate dehydrogenase. 3. Creatine phosphokinase and adenylate kinase, by contrast, showed little change in activity; adenylate deaminase and glutathione reductase activities increased during the hypertrophic phase. The concentration of myoglobin at first declined, then increased again. 4. The distribution of enzymes between the left and right hemidiaphragms was found not to be uniform. 5. Activities of adenine-metabolizing enzymes in the diaphragm were as great as in white muscle. It is suggested that their reputedly lower activities in red muscle properly refer to muscle containing a high proportion of intermediate fibres, which is not the case with diaphragm. 6. The possible causes of the transient hypertrophy after nerve section are discussed.
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PMID:Effects of denervation on the activities of some tricarboxylic acid-cycle-associated dehydrogenases and adenine-metabolizing enzymes in rat diaphragm muscle. 440 65

Aspartate transaminase, alanine transaminase, glutamate dehydrogenase, arginase, serine dehydratase, tyrosine transaminase, glutamine synthetase, glutaminase and adenylate deaminase activities were measured in crude homogenates of 12, 19 and 21-day rat placentae. There is a considerable quantitative importance in enzymes able to produce free ammonia, such as adenylate deaminase and glutamate dehydrogenase, activity that progressively decrease with the age of placenta. The glutamine synthetase and tyrosine transaminase activities increase with age, while serine dehydratase decreases considerably and aspartate and alanine transaminase do not change practically. Arginase shows a maximum at 19, with lower 12 and 21-day activities. No measurable glutaminase activity has been found. The possible implications of the enzymes studied upon the ammonia-producing activity of rat placenta are discussed together with the relative decreasing role of placenta for the overall metabolic activity of the foetus, especially during the last phases of its development.
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PMID:Activities of enzymes involved in amino-acid metabolism in developing rat placenta. 610 12


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