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

Exposure of foundry workers to mixtures of different heavy metals is a very important toxicological problem. In this paper the estimation of the effects of lead, zinc, and copper on erythrocyte metabolism is presented. Concentrations of copper and zinc at work posts of the group examined did not exceed TLV, while lead concentration was 1.5 to 4 times higher than TLV. Erythrocyte metabolism was measured through activities of such glycolytic pathway enzymes as PFK, PGI, PK, aldolase and G6-PD from the hexose monophosphate pathway. Additionally the free erythrocyte protoporphyrin (FEP) level, D-ALA activity, serum GSH level, 2,3 DPG level in erythrocytes and lactic acid production during a 2-h incubation of red blood cells (RBC) was estimated. The blood-lead level, FEP level, copper concentration in erythrocytes in exposed group were significantly higher than in control group while the zinc level in erythrocytes was significantly lower. Measuring erythrocyte metabolism we showed that the activity of PGI, PFK, aldolase, lactic production and 2,3 DPG levels was significantly higher in the exposed group, probably as a result of anaerobic glycolysis activation.
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PMID:Influence of heavy metal mixtures on erythrocyte metabolism. 234 40

ATPase activity of uterus and ovary was markedly elevated in presence of gossypol and decreased in presence of lactic acid indicating activation and inhibition of energy metabolism by gossypol and lactic acid respectively. The elevated levels of glycogen in uterus indicate inhibition of glycogenolysis as supported by phosphorylase activity. Whereas in ovary the glycogen depletion indicates activation of glycogenolysis supported by phosphorylase activity. The activity levels of aldolase and G-6-PDH decreased in the uterus in presence of gossypol and increased in presence of lactic acid. The same were elevated in ovary indicating the activation of hexose mono and diphosphate pathways. Lactic acid accumulated in presence of both gossypol and lactic acid with a depletion in level of pyruvic acid in both the tissues. This situation in the uterus indicates the condition of anti-implantation in presence of both gossypol and lactic acid. The NAD-LDH activity was inhibited in presence of gossypol and activated in presence of lactic acid in both tissues.
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PMID:In vitro effects of gossypol and lactic acid on rat uterus and ovary during implantation and antiimplantation. 263 59

The incubation of human platelets with methylglyoxal and glucose produces a rapid transformation of the ketoaldehyde to D-lactate by the glyoxalase system and a partial reduction in GSH. Glucose utilization is affected at the level of the glycolytic pathway. No effect of the ketoaldehyde on glycogenolysis and glucose oxidation through the hexose monophosphate shunt was demonstrated. Phosphofructokinase, fructose 1,6 diphosphate (F1, 6DP) aldolase, glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate mutase were mostly inhibited by methylglyoxal. A decrease in lactate and pyruvate formation and an accumulation of some glycolytic intermediates (fructose 1,6 diphosphate, dihydroxyacetone phosphate, 3-phosphoglycerate) was observed. Moreover methylglyoxal induced a fall in the metabolic ATP concentration. Since methylglyoxal is an intermediate of the glycolytic bypass system from dihydroxyacetone phosphate to D-lactate, it may be assumed that ketoaldehyde exerts a regulating effect on triose metabolism.
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PMID:Inhibition of the glycolytic pathway by methylglyoxal in human platelets. 275 37

Changes in carbohydrate metabolism were studied in midgut gland, muscle, and gill tissues of marine prawn Penaeus indicus exposed to a sublethal concentration (0.3 ppm) of phosphamidon. A significant decrease in glycogen and pyruvate and an increase in lactate content were observed in all phosphamidon-exposed prawn tissues after 96 hr. An increase in phosphorylase a and aldolase activity levels suggested the increased formation of triose sugars during phosphamidon toxicity. LDH activity was considerably decreased and an increment in lactate content was observed which indicates reduced mobilization of pyruvate into the citric acid cycle. Glucose-6-phosphate dehydrogenase activity was considerably increased, suggesting the enhanced oxidation of glucose in the hexose monophosphate shunt pathway. Krebs cycle enzymes such as NAD-isocitrate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase were found to be decreased, suggesting the impairment in mitochondrial oxidative metabolism due to the acute toxic impact of phosphamidon. Cytochrome-c oxidase and Mg2+ ATPase activity levels were also decreased considerably, suggesting impaired energy synthesis and breakdown during phosphamidon toxicity, as a result of reduced oxidation of glucose aerobically. The increase in acid and alkaline phosphatase activities indicates the enhanced breakdown of phosphate to release energy in view of inhibiton or impairment in the ATPase system during phosphamidon-induced stress. These results suggest that phosphamidon has a profound effect on the oxidative metabolism of prawn which results in the triggering of compensatory metabolic pathways for survivability.
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PMID:Modulation of carbohydrate metabolism in the selected tissues of marine prawn, Penaeus indicus (H. Milne Edwards), under phosphamidon-induced stress. 337 38

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

Rat liver cytosolic enzyme preparation catalyses the formation of sedoheptulose 1,7-P2 (60% of total heptulose-P formed) from hexose 6-P and triose 3-P (reverse mode of pentose pathway operation). Smaller amounts of sedoheptulose 1,7-P2 are also formed from ribose 5-P during the non-oxidative synthesis of hexose 6-P (forward pentose pathway operation). The apparent absence of erythrose 4-P in biological systems may be explained by its contribution to carbons 4,5,6 and 7 of sedoheptulose 1,7-P2 as well as its pronounced ability to exist in dimeric form. Apart from the aldolase catalyzed formation of sedoheptulose 1,7-P2, 6-phosphofructokinase also catalyses its formation from sedoheptulose 7-P and fructose 1,6-bisphosphatase catalyses its dephosphorylation. These three enzymes may contribute to the regulation of carbon flux through the near equilibrium reactions of the non-oxidative pentose phosphate pathway in vivo. The phosphotransferase enzyme of the L-type pentose pathway is also able to catalyse the interconversion of sedoheptulose mono and bisphosphates via D-glycero D-ido octulose-P.
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PMID:The significance of sedoheptulose 1,7-bisphosphate in the metabolism and regulation of the pentose pathway in liver. 408 20

Rats inoculated with Streptococcus faecalis developed endocarditis and demonstrated a 6- to 30-fold increase in aldolase, isocitric dehydrogenase, phosphohexose isomerase, and lactic dehydrogenase. The animals infected with Bacillus subtilis did not develop overt disease nor significant increases in enzyme activities, but viable organisms were recovered at 2 weeks. Rats inoculated with mixed culture of these organisms showed a 2- to 10-fold increase of enzyme activities without evidence of pathological anatomic changes. Both organisms were recovered at necropsy. The total protein and glycoproteins followed the patterns of enzyme activities. There were major changes in alpha(1), alpha(2), and beta globulins and glycoglobuulins at the early stages of infection. The protein-bound hexose changes coincided with the severity of S. faecalis infection, but were at normal levels after 72 hr of infection of B. subtilis and S. faecalis mixed infections. The results indicate that B. subtilis infection modified the pathogenicity of S. faecalis and by an unknown mechanism affected protein and glycoprotein production in serum of experimental rats.
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PMID:Biochemical changes in serum of pure and mixed Streptococcus faecalis and Bacillus subtilis infections in rats. 418 98

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

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

A new mutation in Escherichia coli, giving inability to grow on gluconic, glucuronic, or galacturonic acids, has been identified as complete deficiency of 2-keto-3-deoxygluconate 6-phosphate (KDGP) aldolase activity. The genetic map position of the locus, eda, is about 35 min. The inability to grow on the uronic acids was expected, because the aldolase is on the sole known pathway of their metabolism. However, inability to grow on gluconate was less expected, because the hexose monophosphate shunt might be used, as happens in mutants blocked in the previous step, edd, of the Entner-Doudoroff pathway. The likely explanation of gluconate negativity is inhibition by accumulated KDGP, because gluconate is inhibitory to growth on other substances, and one type of gluconate revertant is eda(-), edd(-). KDGP is probably the inducer of KDGP aldolase.
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PMID:2-keto-3-deoxygluconate 6-phosphate aldolase mutants of Escherichia coli. 494 94


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