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)

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

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

1. Changes in the activities of acetyl-CoA carboxylase (EC 6.4.1.2), phosphofructokinase (EC 2.7.1.11), aldolase (EC 4.1.2.13), extramitochondrial aconitate hydratase (EC 4.2.1.3) and NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42) have been measured in the livers of developing rats from late foetal life to maturity. 2. The effect of altering the weaning time on some enzymes associated with lipogenesis has been studied. Weaning rats at 15 days of age instead of 21 days results in an immediate increase in the activity of ;malic' enzyme (EC 1.1.1.40) whereas the activities of glucose 6-phosphate dehydrogenase (EC 1.1.1.49) and ATP citrate lyase (EC 4.1.3.8) did not increase until 4-5 days and acetyl-CoA carboxylase 2-3 days after early weaning. Weaning rats on to an artificial-milk diet led to complete repression of the rise in activity of hepatic enzymes associated with lipogenesis normally found on weaning, except for ;malic' enzyme, which increased in activity after 20 days of age. 3. The effect of intraperitoneal injections of glucagon, cortisol, growth hormone and thyroxine on the same hepatic enzymes has been investigated. Only thyroxine had any effect on enzyme activities and caused a 20-fold increase in ;malic' enzyme activity and a twofold increase in ATP citrate lyase activity. 4. The activities of hepatic glucose 6-phosphate dehydrogenase and ;malic' enzyme are higher in adult female than in adult male rats and it has been shown that this sex difference in enzyme activities is due to both male and female sex hormones. 5. Hepatic malate, citrate, pyruvate, glucose 6-phosphate and phosphoenolpyruvate concentrations have been measured throughout development. 6. The results are discussed in relation to the dietary and hormonal control of hepatic enzyme activities during development.
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PMID:Factors involved in changes in hepatic lipogenesis during development of the rat. 424 18

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

By using the continuous culture technique, the transition from aerobiosis to anaerobiosis and its effect on a number of enzymes has been investigated in Escherichia coli K-12. A decrease in the oxygen partial pressure below 28.0 mm of Hg resulted firstly in an increase of the respiratory enzymes (reduced nicotinamide adenine dinucleotide [NADH] oxidase, 2.53-fold; succinic dehydrogenase, 1.4-fold; cytochrome b(1), 3.91-fold; and cytochrome a(2), 2.45-fold) before the electron transport system gradually collapsed as cytochrome a(2), followed by cytochrome b(1), succinic dehydrogenase, and finally NADH oxidase decreased in activity. The change from respiration to fermentation was initiated well before the oxygen tension reached zero by the increase in levels of fructose diphosphate-aldolase, glucose 6-phosphate, and 6-phosphogluconate dehydrogenases and a decrease in 2-oxoglutarate dehydrogenase. Whem the dissolved oxygen tension reached zero, dry weight and CO(2) formation together with isocitrate dehydrogenase decreased, whereas acid production and phosphofructokinase synthesis started to increase. Enzymatic investigations revealed that the kinetics of the enzyme phosphofructokinase from strict aerobic cultures (6.9 ppm oxygen in solution) was adenosine triphosphate (ATP)-insensitive, whereas the same enzyme from anaerobic cultures was ATP-sensitive. A mechanism is proposed for the change from aerobiosis to anaerobiosis together with the occurring change in glucose regulation.
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PMID:Effect of oxygen on several enzymes involved in the aerobic and anaerobic utilization of glucose in Escherichia coli. 434 16

Cells of Azotobacter vinelandii are specifically induced to encyst by beta-hydroxybutyrate (BHB). The process of differentiation, which occurs over a period of 36 h, was characterized by an ordered sequence of biochemical events. Upon initiation of encystment, nitrogen fixation and glucose-6-phosphate dehydrogenase activities decreased immediately to very low levels. This was followed by an increase in the specific activities of BHB dehydrogenase, isocitrate dehydrogenase, isocitrate lyase, and malate synthase first at 3 h and then again at 21 h. The peak activity of fructose 1,6-diphosphate aldolase occurred at 6 h, and the enzyme activity then decreased gradually. Fructose 1,6-diphosphatase had peak activities at 9 and 27 h. Deoxyribonucleic acid synthesis ceased just prior to the final cell division at 4 to 6 h, but ribonucleic acid synthesis continued until the 12th h. From labeling studies and the appearance of new enzyme activities, it appeared that protein synthesis continued throughout encystment.
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PMID:Sequential metabolic events during encystment of Azobacter vinelandii. 434 69

Infection of white rats with Francisella tularensis (Pasteurella tularensis) and Salmonella typhimurium and exposure to the endotoxin of S. typhimurium stimulated significant increases in various serum enzymes including aldolase, lactate dehydrogenase, phosphohexose isomerase, isocitrate dehydrogenase, and glutamate-oxalacetate transaminase. The rates of changes in enzymatic activity after infection were directly related to the size of infecting dose and to the type of infective agent employed. Tularemic infection stimulated excessive changes in enzyme activity, whereas salmonellosis and endointoxication elicited less pronounced alterations of relatively short duration. Changes observed in serum enzymes after exposure to these agents reflect the severe liver damage and extensive systemic involvement noted in tularemia as opposed to more localized and less intensive tissue damage occurring during salmonellosis and endointoxication.
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PMID:Influence of bacterial infection on serum enzymes of white rats. 488 56

The regional enzyme activities of glucose metabolism in the rat brain were investigated. Hexokinase (EC 2.7.1.1) and pyruvate dehydrogenase (EC 1.2.4.1), key enzymes for glucose metabolism, showed no changes in activity in all the regions studied of the aging brain as compared with the adult brain. However, the activity of D-3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is low throughout the adult brain and, in contrast with hexokinase and pyruvate dehydrogenase, its activity decreases significantly during aging. Other enzymes that showed significant decreases during aging are aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27), citrate synthase (EC 4.1.3.7), and NAD+-linked isocitrate dehydrogenase (EC 1.1.1.41). The catabolic enzyme in cholinergic metabolism, acetylcholinesterase (EC 3.1.1.7), selected as an example of a non-energy-metabolising enzyme, also showed significant decreases in all regions of the brain in aging, although its highest activity remained in the striatum. These results are discussed with respect to the energy metabolism in various brain regions and their status with aging.
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PMID:Energy-metabolizing enzymes in brain regions of adult and aging rats. 646 Aug 51

The effect of a chronic intake of dietary alcohol upon myocardial enzymes was studied in rats. Alcohol, comprising more than 40% of the dietary calorie content, was administered to rats for 6 or 12 weeks. To assess the metabolic changes in the myocardium, the following enzymes were measured: lactate dehydrogenase (LDH), malate dehydrogenase (MDH), aldolase (ALD), isocitrate dehydrogenase (ICDH), creatine kinase (CK) and glutamate-pyruvate transaminase (GPT). The activity of CK was decreased (4.79 +/- 0.99 U X mg-1 protein) after 6 weeks on alcohol and was significantly different from that of the controls (5.98 +/- 1.44 U X mg-1 protein). After 12 weeks the CK activity of alcoholic rats had recovered to 5.99 +/- 1.08 U X mg protein-1 and approached the value found in the normal myocardium. A pronounced decrease was found in the activity of MDH: 8.26 +/- 0.69 U X mg protein-1 in the controls, and 6.78 +/- 1.07 U X mg protein-1 and 5.79 +/- 0.85 U X mg protein-1 in the alcoholic rats after 6 and 12 weeks, respectively. The LDH activity decreased to a lesser extent, but significantly: 2.45 +/- 0.18 U X mg protein-1 in the controls, and 2.11 +/- 0.07 U X mg protein-1 and 2.06 +/- 0.29 U X mg protein-1 after 6 and 12 weeks on test. Only slight, not significant, changes were observed for the other enzymes investigated (ICDH, ALD, GPT).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme activity changes in rat heart after chronic alcohol ingestion. 668 85

Changes in the activity of 13 enzymes are described in the process of cytodifferentiation of the nerve cells of spinal ganglion, the motor neurons of spinal cord and large nerve cells of the III layer of tectum opticum in 7, 10 and 21 day old chick embryos. Cytophotometry was performed with MZFV-1 (LOMO) by means of plug-method. A relatively high activity of glucose-6-phosphat dehydrogenase, diaphorase, alpha-glycerophosphate dehydrogenase and, partially, acetylcholine esterase was found already in the 7 days old embryo. The activity of monoamine oxidase, aldolase-glyceroaldehyde phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase increased markedly on the 21st day. When studying the reciprocal distribution of two enzymes in separate cells, pairs of enzymes with a high value of correlation coefficient were found. The cytodifferentiation was found to be accompanied by changes in the coefficient of correlation of the same pair of enzymes.
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PMID:[Enzymes in the process of neuronal differentiation of the hen spinal ganglion, spinal cord and tectum opticum. A cytophotometric histochemical study]. 683 47


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