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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The metabolic pathways of glucose were studied by histochemical reactions in some species of gastropods living in different habitats. The glycolytic pathway is histochemically indicated by positive results for glucose-6-phosphate isomerase, fructose-1,6-biphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, and D-lactate dehydrogenase. The enzymes of the Krebs cycle gave different responses: isocitrate dehydrogenase and L-malate dehydrogenase were positive, whilst succinate dehydrogenase was constantly negative. Malate synthetase activity was also demonstrated. Despite L-glutamate dehydrogenase is undetectable, the presence of transaminase indicates the gluconeogenetic route. Phosphoglucomutase and glucose-6-phosphate phosphatase appear also positive. The metabolic meaning of our results were discussed.
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PMID:Histochemical research on metabolic pathways of glucose in some species of Mollusca Gastropoda. 311 Nov 50

The authors performed a controlled trial in 18 top athletes (9 weight lifters and 9 rowers, girls) in order to make evident some chronic and acute effects (antioxidant) of selenium. Nonprotein--SH (essential glutathione), lipid peroxides (MDA-malondialdehyde), glucose-6-phosphate dehydrogenases (G-6-PDH) and fructose-1,6-diphosphate aldolase in serum, have been recorded initially on basal conditions, after 3 weeks of treatment (100 micrograms/day selenium or placebo) and again after 3 weeks of treatment, also on basal conditions, when crossing over the groups (between a free interval of 10 days). In another trial we registered these parameters on basal conditions and after two hours of hard training accompanied by a per oral administration of 150 micrograms selenium (respectively placebo). The results show significant changes under selenium treatment of the peroxides, G-6-PDH and light changes, not significant of the nonprotein--SH, changes which could suggest an antioxidant effect of this element.
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PMID:Studies on selenium in top athletes. 314 41

In Saccharomyces cerevisiae, the HGS2-1 allele confers sensitivities to inorganis mercury (Ono and Sakamoto 1985) and to excess fermentable sugars such as glucose (Sakamoto et al. 1985); exogenous tyrosine antagonizes both inorganic mercury and excess glucose. In this study, the inorganic mercury sensitive strain has been shown to have about twice more glucose-1,6-bisphosphate and slightly less pyruvate than the normal strains, suggesting that the inorganic mercury sensitive strain has the reduced aldolase activity. It has been also shown that the growth retarded cells accumulate trehalose, by which the lower level of glucose-6-phosphate in the inorganic mercury sensitive strain is accounted for, and that inorganic mercury, presumably excess glucose also, causes growth inhibition via depletion of cellular tyrosine. The mechanism how cellular tyrosine is depleted by inorganic mercury or excess glucose is accounted for by the facts that (1) the tyrosine uptake activity is decreased with increase of glucose concentration in growth medium, (2) HGS2-1 enhances the effect of glucose on the tyrosine uptake activity, and (3) inorganic mercury inhibits the tyrosine uptake system by binding to its SH-group(s). Thus, it is concluded that the role of tyrosine is not to detoxify inorganic mercury nor excess fermentable sugars but simply to counteract depletion of cellular tyrosine induced by them.
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PMID:Saccharomyces cerevisiae strains sensitive to inorganic mercury. III. Tyrosine uptake. 332 70

In experimental (white rats, rabbits) and clinical (erythrocytes, blood plasma) studies on 29 healthy subjects and patients it has been demonstrated that primary or secondary n-quinone deficiency is accompanied by increased tissue activity of glycolysis enzymes (aldolase, PGmutase) and aerobic pentose phosphate shunt (6 GPDH). Parallel rise in the amount of glycolysis metabolites (pyruvate and lactate) in the blood and the decline in blood plasma glucose level were observed. The changes in glucose-6-phosphate metabolism are, probably, secondary and reflect tissue structure alterations in the development of K and E avitaminosis.
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PMID:[The role of N-quinones in the regulation of glucose-6-phosphate metabolism]. 375 27

Enzymes of the Embden-Meyerhof-Parnas pathway and hexose monophosphate shunt were examined in cytoplasmic extracts of three serovars of Ureaplasma urealyticum. We found no glucose-6-phosphate or 6-phosphogluconate dehydrogenase, hexokinase, phosphoglucose isomerase, aldolase, or lactic dehydrogenase activities. We failed to find cytochrome pigments in extracts and found no significant production of 14CO2 from [U-14C]glucose, nor did we find oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity. Lactic acid was found only at trace levels in spent culture fluids. Ureaplasmas are apparently nonfermentative and are unlike all other mollicutes in that they have no detectable oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity.
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PMID:Metabolic distinctiveness of ureaplasmas. 379 29

Extracts of Pseudomonas aeruginosa (ATCC 7700) cells grown on glucose, gluconate, or glycerol had enzyme activities related to the Entner-Doudoroff pathway. These activities were present in no more than trace amounts when the bacteria were grown on succinate. Fructose-1,6-diphosphate aldolase could not be detected in extracts of the bacteria grown on any of the above carbon sources. Therefore, it appears that P. aeruginosa degrades glucose via an inducible Entner-Doudoroff pathway. The apparent absence of fructose-1,6-diphosphate aldolase in cells growing on succinate suggests that the bacteria can form hexose and pentose phosphates from succinate by an alternate route. d-Glucose-6-phosphate dehydrogenase, a branch-point enzyme of the Entner-Doudoroff pathway, was purified 50-fold from glucose-grown cells. Its molecular weight, estimated by sucrose density gradient centrifugation, was found to be approximately 190,000. The enzyme was strongly inhibited by adenosine triphosphate, guanosine triphosphate, and deoxyguanosine triphosphate, which decreased the apparent binding of glucose-6-phosphate to the enzyme. It is suggested that adenine nucleotide-linked control of glucose-6-phosphate dehydrogenase may regulate the overall catabolism of hexose phosphates and prevent their wasteful degradation under certain conditions requiring gluconeogenesis.
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PMID:Adenosine triphosphate-linked control of Pseudomonas aeruginosa glucose-6-phosphate dehydrogenase. 438 49

The activities of phosphofructokinase, aldolase and pyruvate kinase were diminished in extracts from skeletal muscle of streptozotocin diabetic rats, whereas the activities of glucose phosphate isomerase and phosphoglucomutase were not changed. Treatment of diabetic rats with insulin restored the activity of phosphofructokinase to normal. A kinetic study of the partially purified enzyme from normal and diabetic rats showed identical Michaelis constants for ATP and equal sensitivity to inhibition by excess of this substrate. Extracts of quick frozen muscle from diabetic rats had higher levels of citrate (an inhibitor of phosphofructokinase) and lower levels of D-fructose-1,6-bisphosphate and D-glucose-1,6-bisphosphate (activators of this enzyme). The levels of D-fructose-6-phosphate, D-glucose-6-phosphate, ATP, ADP and AMP were the same for the two groups. Our data suggest that the in vivo decrease of phosphofructokinase activity in skeletal muscle of diabetic rats is due to a decrease in the level of the enzymatically active protein as well as to an unfavorable change in the level of several of its allosteric modulators.
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PMID:Decreased phosphofructokinase activity in skeletal muscle of diabetic rats. 623 37

In order to evaluate properly red cell metabolic data obtained in newborns with congenital hemolytic disorders, the unique metabolic characteristics and normal developmental changes that occur prenatally and postnatally are presented. The age-dependent red cell glycolytic enzymes (hexokinase, aldolase, pyruvate kinase) and glucose-6-phosphate dehydrogenase and most glycolytic intermediates are elevated at birth and at 11 to 12 months of age, consistent with the presence of a young red cell population the entire first year of life. However, certain red cell enzymes are elevated out of proportion to the age of the red cell population [phosphoglucose isomerase. glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase (PGK), and enolase (ENO)] whereas others are decreased [phosphofructokinase (PFK), glutathione peroxidase, carbonic anhydrase, and others]. These metabolic characteristics are felt to be unique and representative of "fetal erythropoiesis." Activities of PGK and ENO decrease the PFK increases toward normal adult values beginning at eight to nine weeks of age. The concentration of glucose-6-phosphate steadily increases after birth and peaks at three to four weeks of age, at a time when PFK activity remains relatively unchanged, suggesting a relative block in glycolysis at the PFK step secondary to an enzyme with both decreased activity and altered kinetic properties (a "fetal" isozyme). Thus, evaluation of red cell enzyme and glycolytic intermediate data obtained in the first year of life should be related to the knowledge that a young red cell population is present and the characteristic unique metabolic red cell alterations described in cord blood persist beyond the immediate neonatal period.
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PMID:Red cell enzymopathies in the newborn. I. Evaluation of red cell metabolism. 628 May 78

Glucose may be converted to 6-phosphogluconate by alternate pathways in Pseudomonas aeruginosa. Glucose is phosphorylated to glucose-6-phosphate, which is oxidized to 6-phosphogluconate during anaerobic growth when nitrate is used as respiratory electron acceptor. Mutant cells lacking glucose-6-phosphate dehydrogenase are unable to catabolize glucose under these conditions. The mutant cells utilize glucose as effectively as do wild-type cells in the presence of oxygen; under these conditions, glucose is utilized via direct oxidation to gluconate, which is converted to 6-phosphogluconate. The membrane-associated glucose dehydrogenase activity was not formed during anaerobic growth with glucose. Gluconate, the product of the enzyme, appeared to be the inducer of the gluconate transport system, gluconokinase, and membrane-associated gluconate dehydrogenase. 6-Phosphogluconate is probably the physiological inducer of glucokinase, glucose-6-phosphate dehydrogenase, and the dehydratase and aldolase of the Entner-Doudoroff pathway. Nitrate-linked respiration is required for the anaerobic uptake of glucose and gluconate by independently regulated transport systems in cells grown under denitrifying conditions.
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PMID:Regulation of alternate peripheral pathways of glucose catabolism during aerobic and anaerobic growth of Pseudomonas aeruginosa. 640 87

Bilipolinum (Adipiodon), iodine contrast medium used in cholangiography, showed an inhibitory effect on the activity of human erythrocyte phosphohexoseisomerase, phosphofructokinase, aldolase and glucose-6-phosphate dehydrogenase. The addition of glucose metabolites (glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-bis-phosphate, pyruvate and lactate) abolished the inhibitory effect of Bilipolinum. In the presence of Bilipolinum purified erythrocyte phosphofructokinase showed a decreased affinity towards substrate, modified allosteric properties and reduced stability at pH below 7.5. Purified erythrocyte glucose-6-phosphate dehydrogenase was also affected by Bilipolinum and its affinity for NADP was decreased. Testing of erythrocyte enzymes in the evaluation of toxicity of iodine contrast media is discussed.
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PMID:The effect of bilipolinum (Adipiodon), an iodine contrast medium on erythrocyte enzymes. 645 4


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