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)

Blood and serum from 17 Macaca mulatta were analysed for haptoglobins, transferrins, 6-phosphogluconate dehydrogenase, adenylate kinase, adenosine deaminase, phosphoglucomutase, acid phosphatase, glucose-6-phosphate dehydrogenase and phosphohexose isomerase. Compared to the human pattern, the AcPh and the ADA components of macaques are fast moving; AK, PGM, 6-PGD and G-6-PG have almost uniform and similar electrophoretic mobilities; and the Hp, Tf and PHI show differential mobilities. All these macaques possess similar karyotypes.
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PMID:Genetic variations in primates. Red cell enzymes and serum proteins in Macaca mulatta. 80 45

It has been suggested by some authors that during amphibian development, due to the higher glucose-6-phosphate dehydrogenase (EC 1.1.1.49) activity compared to that of 6-phosphogluconate dehydrogenase (EC 1.1.1.43), 6-phosphogluconate could accumulate in the embryo tissues and regulate the channelling of glucose-6-phosphate into glycolysis. Here, on the base of the specific activities of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glucose-6-phosphate isomerase (EC 5.3.1.9) found in the embryos of Bufo bufo during development, it is discussed whether 6-phosphogluconate can accumulate and play a regulative role on glucose-6-phosphate metabolism in the anuran embryo.
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PMID:Specific activities of 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase and glucose-6-phosphate isomerase during Bufo bufo development. 81 78

Vestigial wing and wild type populations of Drosophila melanogaster were exposed to 5%, 20%, and 60% oxygen at normal atmospheric pressure. Adult mortality rates, larval production, and allele frequency changes in four gene-enzymes were examined in the populations. All flies in 60% oxygen survived as well as controls until day 20 and then died out within the next 10 to 12 d. In 5% oxygen, vestigial wing flies had mortality rates greater than the 20% controls initially, but the rate eventually approached that of the controls. Wild type flies in 5% oxygen survived as well as controls. Larval production and rate of eclosure in 60% oxygen were similar to controls, but reduced in 5% oxygen. Allele frequency shifts to 6-phosphogluconate dehydrogenase and phosphoglucomutase were observed in 5% oxygen, and a shift of alpha-glycerophosphate dehydrogenase allele frequencies occurred in 60% oxygen. There was no evidence of in vivo inactivation of ADH, 6-PGD, alpha-GPD or PGM in 60% oxygen.
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PMID:Survivorship and gene frequencies of Drosophila melanogaster populations in abnormal oxygen atmospheres. 81 44

The stability of various glycolytic enzymes of human erythrocytes has been studied by the mechanical shaking method. The rate of denaturation apparently followed first order kinetics. The t1/2, the shaking time required to denature 50% of the original activity, for glucose-6-phosphate dehydrogenase, phosphofructokinase, and pyruvate kinase was less than 1 min; that for hexokinase, 6-phosphogluconate dehydrogenase, and monophosphoglyceromutase was between 2 and 13 min; that for all the other enzymes was more than 30 min. Since the t1/2 value for each enzyme is highly reproducible if the shaking conditions are kept constant, these parameters may be used as an indicator of protein stability in solution. The mechanical denaturation method may also be used to remove unstable components from a mixture of proteins with different stabilities.
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PMID:Stability of glycolytic enzymes of human erythrocytes. 83 47

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

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.
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PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72

In the presented study the influence of freezing and freeze-drying on enzyme activity is described. Attention is paid to 16 enzymes which can be used for quantitative enzyme histochemical techniques. With the exception of succinate dehydrogenase only, no significant inactivation during freezing and freeze-drying procedures could be demonstrated with lactate dehydrogenase, malate dehydrogenase (NAD+), malate dehydrogenase (decarboxylating) (NADP+), isocitrate dehydrogenase (NADP+), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADH-oxydoreductase, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome c oxidase, phosphoglucomutase, glucosephosphate isomerase, glucose-6-phosphatase, acid phosphatase, beta-glucuronidase and non specific aryl esterase. Therefore, the results supply a sound foundation for those quantitative enzyme histochemical techniques in which tissue specimens are frozen or frozen-dried before enzyme estimations are performed.
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PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61

The influence of fasting and diet composition on the time sequence of changes in hepatic lipogenic enzyme activities in coho salmon was investigated. Young coho salmon fed a high-carbohydrate diet for 3 weeks were then fasted for 2, 6, or 23 days. Liver preparations were assayed for fatty acid synthetase, citrate cleavage enzyme, malic enzyme, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities. Fasting the fish for 2 or 6 days did not influence the activities of these enzymes; however, by the end of the 23-day fast the activities of all these enzymes had decreased. Changing the diet of the fish from high-carbohydrate to high-fat had only a minimal influence on the activities of the hepatic lipogenic enzymes after 7 to 14 days. Longer-term studies demonstrated that high-fat diets did eventually depress lipogenic enzyme activities. The effect of fasting and feeding on the level of lipogenic enzyme activities was observed only after several weeks, in contrast to hours in the rat. This may reflect a difference between poikilothermous and homoiothermous animals.
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PMID:Effects of fasting and feeding various diets on hepatic lipogenic enzyme activities in coho salmon (Oncorhynchus kisutch (Walbaum)). 88 88

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


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