Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.49 (glucose-6-phosphate dehydrogenase)
 7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activity of the main enzymes of pentose phosphate pathway of carbohydrate metabolism was studied in human mucosa of the stomach. In the mucosa glucose-6-phosphate dehydrogenase in gastric ulcer and 6-phosphogluconate dehydrogenase in normal stomach were shown to be less active as compared with these enzymatic activities in duodenal ulcer. A distinct decrease in the activity of glucose-6-phosphate dehydrogenase was observed in the ulcerous region, independently of the ulcer localization either in corpus ventriculi or in duodenum, as compared with the parts of the mucosa away from the impairment; the lowest enzymatic activity was estimated in the gastric ulcer zone. Activities of 6-phosphogluconate dehydrogenase and transketolase were the same in the ulcerous and normal mucosa and did not depend on the localization of the impairment. Contents of lactic and pyruvic acids were similar in mucosa of the stomach both in gastric and duodenal ulcer.
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PMID:[Characteristics of the pentose phosphate pathway of carbohydrate metabolism in the gastric mucosa of persons with peptic ulcer]. 91 74

Previous studies have shown that transketolase activity is decreased in the brains of thiamin deficient rats. This study assesses the effect of decreased transketolase levels on the activity of the pentose phosphate cycle in murine thiamin deficient cortex and brainstem. Thiamin deficiency was produced in newborn and adult rats by either pyrithiamin administration or by feeding a low thiamin diet. Newborn rats were killed at 22 days of age, and adults were killed at the onset of moderate to severe nurological signs. Cortices and brainstems from thiamin deficient and control rats were analyzed for activity of the two regulatory enzymes of the pentose phosphate cycle, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Flux through the pathway was measured by the differentially labeled glucose technique in the brainstems of deficient and control adult rats. In both the brainstem and cortex of thiamin dificient rats, areas in which transketolase activity was decreased up to 65%, the activities of the two regulatory enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, were unaltered. Further, flux through the pentose phosphate cycle was not decreased as compared to pair-fed control rats. These data do not support the hypothesis that in thiamin dificient rats, a decrease in cerebral transketolase activity leads to a diminished pentose phosphate cycle activity.
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PMID:Thiamin deficiency and the pentose phosphate cycle in rats: intracerebral mechanisms. 93 94

Partial denervation of the liver evoked the dissection of subphrenic vagus nerves and nerves of the hepatogastric duodenal ligament tissue stimulates synthesis of pentoses in the liver due to the oxidative mechanism and inhibits the process of unoxidative formation of pentoses. Three-four weeks after the operation one may observe a 72% increase in the activity of glucose-6-phosphate dehydrogenase in the liver tissue and a 29 and 21% drop in the activity of transketolase and enzymes, respectively, participating in metabolism of ribose-5-phosphate. The content of soluble proteins in the liver with deneravation is unchanged. A correlation is observed between these changes and those in the content of nucleic acids, an opinion is confirmed on the autonomous character of the oxidative and unoxidative phases of the pentose cycle.
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PMID:[Pentosephosphate shunt enzymatic activity in the liver in its disordered innervation]. 96 Feb 38

In soluble fraction of rat liver studies have been made on the activity of glycolytic enzymes and dehydrogenases of the pentose phosphate pathway 3 and 20 hours after the electrical stimulation of the medial (HVM) and lateral (AHL) structures of the medial hypothalamus via chronically implanted electrodes. Electrical stimulation of the HVM within 3 hours decreased total hexokinase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase activities, and to a lower extent -- the activity of glucokinase. This effect was not prevented by the adrenalectomy. During stimulation of the AHL, the decrease of LDH activity was the same, whereas the activity of hexokinase, glucose-6-phosphate dehydrogenase and glucokinase decreased to a lower extent. Electrical stimulation of the medial hypothalamus within 20 hours decreased the response, this effect being presumably associated with the decrease in the content of endogenous noradrenalin in the liver of animals. The role of the hypothalamus and sympathetic nervous system in regulation of the investigated enzymes of energy metabolism in the liver is discussed.
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PMID:[Participation of the hypothalamus in regulating the activity of rat liver energy metabolism enzymes]. 98 65

Three enzymes selected as representative of major metabolic pathways (malic dehydrogenase, of the citric acid cycle, lactic dehydrogenase, of glycolysis and glucose-6-phosphate dehydrogenase, of the pentose pathway) were measured by quantitative histochemical methods in individual hypothalamic nuclei during the 5-day estrous cycle of adult rats. Malic dehydrogenase increases significantly from low proestrous levels to a peak at estrus and then declines during diestrus in the following nuclei and areas of the anterior hypothalamus: medial and lateral preoptic, suprachiasmatic, supraoptic, and anterior. Significant peaks of lactic dehydrogenase occur more often during diestrus-3 in hypothalamic nuclei of the middle and posterior hypothalamus, Glucose-6-phosphate dehydrogenase has a biphasic pattern with peaks usually occurring during the diestrous period.
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PMID:Quantitative histochemical studies of the hypothalamus. Dehydrogenase enzymes during the estrous cycle. 103 42

The activity of glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, pyruvate kinase (PK) and lactate dehydrogenase (LDH) was measured in human adipose tissue (AT) of newborns aged 0-2 and 2-48 h, of 3- to 5-month-old infants and of adults. AT was sampled by means of a special needle from the gluteal region without anesthesia. We observed significantly higher activity of the two pentose phosphate shunt enzymes when calculated on protein content and wet weight basis in newborns as compared to infants and adults. There were no differences for PK and LDH between newborns and adults when the values were calculated for the soluble protein. The protein concentration of the AT decreased significantly during the development.
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PMID:Activity of some enzymes of carbohydrate metabolism in human subcutaneous adipose tissue in newborns, infants and adults. I. Activity of pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase. 114 54

The sub-totally nephrectomized chronically uremic rat has been found to have significantly increased hepatic glucose-6-phosphate dehydrogenase activity and increased lipogenesis and glycoportein synthesis. Increased conversion of 14-C-D-glucose to 14-CO2, and increased plasma free fatty acid levels were also observed. The metabolic significance of these findings has been discussed, particularly with respect to the importance of the pentose shunt in this model. The influence of reduced diet intake, resulting from uremic anorexia, has been considered in light of changes observed. It is concluded that decreased food intake alone is unlikely to be responsible for the altered glucose utilization evident in this model.
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PMID:Carbohydrate metabolism in the chronically uremic rat. 114 18

The activity of the key enzymes of the pentose phosphate pathway (glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, transketolase) was determined in cell-free homogenates of Candida lipolytica 695 and Candida tropicalis 303 growing on different carbon sources. The activity of these enzymes remained almost the same in the course of growth of both cultures. The activity of the enzymes differed only slightly in the cells metabolizing hexadecane and glucose. The activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the cell-free homogenates of C. tropicalis 303 was twice as high as in the cells of C. lipolytica 695. The activity of transketolase was the same in both cultures. The main role of the pentose phosphate pathway is presumed to consist not in catabolism of the carbon source, but in biosynthesis of pentoses and other important intermediates.
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PMID:[Activity of pentose phosphate pathway enzymes in alkane-oxidizing yeast cells]. 116 Jun 34

Polyacrylamide-disc gel electrophoresis and quantitative enzyme assays showed that the pathways of glucose catabolism and secondary metabolism in Penicillium expansum were dependent on the degree of aeration of the cultures. The isoenzyme patterns and specific activities of aldolase and succinate dehydrogenase indicated that glycolysis and the tricarboxylic acid cycle operated under conditions of both limited and efficient aeration (i.e. in cultures grown statically or on an orbital shaker). At high levels of aeration the growth rate was faster and synthesis of extracellular pectolytic enzymes was enhanced, whilst the activities of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase showed that the pentose-phosphate shunt was important in glucose catabolism during the trophophase of growth. In contrast, under conditions of low aeration this latter pathway was virtually undetectable, growth was slower, pectolytic enzyme production low and large concentrations of secondary metabolites (6-methylsalicylic acid, patulin and citrinin) accumulated.
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PMID:The effects of aeration on glucose catabolism in Penicillium expansum. 117 56

Enzyme activities operative in glucose degradation and citrate cleavage pathway were studied in the adipose tissue of twenty-four patients with adult-onset diabetes and normal body weight, aged 59+/-9 years, and twenty-four matched controls. In normal tissue, type II (heat-inactivated) hexokinase moderately predominated over type I (heat-resistant). 6-Phosphofructokinase had an extremely low activity, which was by far the lowest among the ten glycolytic enzyme activities investigated, and which therefore might greatly limit the glycolytic rate. The level of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating) was elevated above that occurring in other tissues. This, especially if considered together with the low 6-phosphofructokinase activity, would suggest a major role of pentose cycle in glucose degradation. Of the citrate cleavage pathway enzymes, ATP citrate-lyase, although having a lower activity than malate dehydrogenase and malate dehydrogenase (decarboxylating) (NADP), was readily measurable, which contrasts with previous data by others. This finding is consistent with the occurrence of lipogenetic capacity in human adipose tissue. In diabetic tissue, there was a decreased activity, both on a protein and on a wet-weight basis, of enzymes concerned with the glucose entry into metabolic pathways, namely hexokinase (both type I and, especially, type II) and pentose cycle dehydrogenases, as well as of pyruvate kinase. This could be connected with the defective glucose utilization by adipose tissue in diabetes. Beside the above-mentioned dehydrogenases, malate dehydrogenase (decarboxylating) (NADP) was also diminished. The reduction of these NADPH-forming enzymes, which supply reducing equivalents for fatty acid synthesis, would suggest a depressed lipogenesis.
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PMID:Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects. 118 27


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