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:1.1.1.49 (glucose-6-phosphate dehydrogenase)
7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This collaborative study on the determination of glucose and fructose in wine was performed by 18 laboratories on 4 matched pairs of commercial wine. The method uses the enzymes hexokinase, glucose-6-phosphate dehydrogenase, and phosphoglucose isomerase and the coenzyme nicotinamide-adenine dinucleotide phosphate. Both glucose and fructose can be determined in the same sample without separation. The method is simple but care is necessary to ensure precise transfer of small volumes. Repeatability and reproducibility standard deviations for glucose ranged from 2.6 to 14.6 mg/L and 4.7 to 16.5 mg/L, respectively. Repeatability and reproducibility values for fructose ranged from 2.4 to 16.1 mg/L and 6.0 to 21.3 mg/L, respectively. The method has been adopted official first action.
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PMID:Enzymatic-ultraviolet determination of glucose and fructose in wine: collaborative study. 405 18

A fluorimetric method to estimate erythrocyte glucose phosphate isomerase is described. Five mul of blood is added to 100 mul of water. Ten mul of the resulting hemolysate is incubated with a reaction mixture (200 mul) containing Tris-HCl buffer pH 8.0, 20 mumoles, MgCl(2) 2 mumoles, nicotinamide adenine dinucleotide phosphate 0.08 mumoles, glucose-6-phosphate dehydrogenase 0.2 EU and fructose-6-phosphate 0.12 mumoles. After ten minutes of 25 degrees C 20 mul of the mixture is added to 2 ml of 0.01 M phosphate buffer pH 7.4 and the nicotinamide adenine dinucleotide phosphate fluorescence determined. Two ml of water was added to the remaining reaction mixture and the hemoglobin concentration determined at 410 nm. The technique is primarily designed for use with small amounts of blood, of widely varying activity, from various animal species.
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PMID:A modified screening method for estimating erythrocyte glucose phosphate isomerase. 414

1. The enzymes of the pentose phosphate pathway were assayed in supernatant fractions from rat muscle, liver and uterus. 2. On incubation of ribose 5-phosphate with uterus and liver supernatants, triose phosphate, sedoheptulose 7-phosphate and hexose monophosphate accumulated. 3. When a muscle supernatant was used, glycerol 3-phosphate instead of triose phosphate appeared and there was a negligible accumulation of hexose monophosphate. 4. Hexose monophosphate production from ribose 5-phosphate was also followed by measuring NADP(+) reduction in the presence of an excess of phosphoglucose isomerase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. 5. With a muscle supernatant, NADPH was reoxidized as rapidly as it was formed owing to the presence of a NADPH-triose phosphate oxidoreductase. 6. A modification of the pentose phosphate pathway in skeletal muscle incorporating this enzyme is proposed.
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PMID:Catalysis of pentose phosphate pathway reactions by cytoplasmic fractions from muscle, uterus and liver of the rat, and the presence of a reduced nicotinamide-adenine dinucleotide phosphate-triose phosphate oxidoreductase in rat muscle. 415 28

Mutants deficient in both glucose-6-phosphate dehydrogenase and phosphoglucose isomerase lysed 4 to 5 h after growth in nutrient medium containing glucose, or after prolonged incubation if the medium contained galactose. The lysis could be prevented by the addition of any other rapidly metabolizable carbon source such as fructose, glucosamine, or glycerol. The glucose-induced lysis was also abolished by introduction of a third mutation lacking phospho-glucose mutase activity but not by a third mutation lacking uridine diphosphate-glucose pyrophosphorylase or teichoic acid glucosyl transferase activity. Galactose-induced lysis was prevented only if the additional mutation abolished the uridine diphosphate-glucose pyrophosphorylase activity. The results showed that lysis was caused by the intracellular accumulation of glucose-1-phosphate, which in turn inhibited at least one of the two enzymes that convert glucosamine-6-phosphate to N-acetyl glucosamine-6-phosphate.
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PMID:Cell lysis of Bacillus subtilis caused by intracellular accumulation of glucose-1-phosphate. 427 11

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

Octanoic acid inhibits, in vitro, the bacterial enzymes glucose-6-phosphate dehydrogenase, phosphofructokinase, pyruvate kinase, fumarase, lactate dehydrogenase, and the malic enzyme of Arthrobacter crystallopoietes. The free fatty acid appears to act as an inhibitor of lipogenesis, although it does not affect the rate of gluconeogenesis. To demonstrate that this inhibition may be of physiological significance in vivo, those enzymes not involved in lipogenesis, such as fructose-1, 6-diphosphatase, phosphoglucomutase, phosphohexoisomerase, aconitase, nicotinamide adenine dinucleotide phosphate (NADP) isocitrate dehydrogenase, NADP glutamate dehydrogenase, malate dehydrogenase, and isocitrate lyase, were assayed and found not to be inhibited by the free fatty acid.
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PMID:Selective inhibition of bacterial enzymes by free fatty acids. 430 71

The antigen that causes killing of at least 98% of a human cell population treated with a 1% solution of a specific rabbit antiserum in the presence of complement is a sensitive genetic marker. The rapid loss of human chromosomes in human-Chinese hamster cell hybrids makes possible a convenient test of linkage relationships with this marker. Hybrid clones with and without the lethal antigen were isolated and analyzed. In 76 clones and subclones studied, 41 carried both the lethal antigen and the lactic dehydrogenase-A marker, 35 carried neither, and no clones contained only one of the two markers. In contrast to this clear demonstration of linkage, absence of linkage was found between the lethal antigen and the following markers: Lactic dehydrogenase B, NAD-dependent malic dehydrogenase, NADP-dependent malic dehydrogenase, glucose-6-phosphate dehydrogenase, phosphoglucomutase, glutamate oxaloacetate transaminase, indophenol oxidase, glucose phosphate isomerase, proline, inositol, hypoxanthine B, and glycine A. This lethal antigen appears to be carried on a single human autosome.
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PMID:Genetics of somatic mammalian cells: lethal antigens as genetic markers for study of human linkage groups. 433 8

Mutants of Escherichia coli and Salmonella typhimurium were selected on the basis of their spontaneous leakage of ribonuclease I. The mutants also leaked several other periplasmic enzymes into the medium during active growth but did not leak the intracellular enzymes glucose-6-phosphate dehydrogenase or phosphoglucose isomerase.
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PMID:Leakage of periplasmic enzymes by mutants of Escherichia coli and Salmonella typhimurium: isolation of "periplasmic leaky" mutants. 433 6

1. The activities of six enzymes (hexokinase, phosphoglucose isomerase, phosphofructokinase, aldolase, glucose 6-phosphate dehydrogenase and amylase) in extracts of pea cotyledons were determined. The activities during the first 10 days after germination showed individual and characteristic changes that indicate a specific control of both synthesis and destruction of enzymes. 2. Tissue contents of glucose, inorganic phosphate, glucose 6-phosphate, fructose 6-phosphate, ATP, ADP, AMP, NAD and NADP were also determined, and a correlation is reported between the substrate concentrations at day 1 and the subsequent enzymic activity. 3. The initial NAD(+)/NADH ratio value of 1 changed to about 3 by day 4; the NADP content was lower and changes in the oxidation state were less striking. The ratio of ATP to ADP and AMP remained virtually constant.
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PMID:Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue during germination. 438 39

Spirillum itersonii ATCC 12639 utilized d-fructose but neither d-glucose nor d-gluconate as a sole source of carbon and energy. The substrate saturation kinetics for d-fructose and d-glucose uptake by whole cells indicated the presence of a carrier-mediated transport system for d-fructose but not for d-glucose. The d-fructose uptake activity was induced (10- to 12-fold increase) during growth on d-fructose-Casamino Acids (CA) or d-glucose-CA medium, but not CA alone. d-Fructose uptake activity was stimulated by Na(+) or Li(+), but was inhibited by KCN, NaN(3), 2,4-dinitrophenol, and p-chloromercuribenzoate. High specific activities of glucokinase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydratase, and 2-keto-3-deoxy-6-phosphogluconate aldolase were detected in extracts of cells cultured on d-fructose-CA medium. These enzymatic activities were undetectable in extracts of cells grown in CA or succinate-CA medium. No decrease in the maximally induced specific activities of these enzymes occurred after the addition of succinate to cells during exponential growth on d-fructose-CA. Fructose 1,6-diphosphate aldolase and glucose-6-phosphate isomerase specific activities were approximately the same irrespective of cultural conditions. These results indicated that d-glucose was not utilized by cells of S. itersonii because this bacterium was impermeable to this hexose.
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PMID:Transport and catabolism of D-fructose by Spirillum itersomii. 480 97


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