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:1.1.1.37 (malate dehydrogenase)
4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

With respect to the enzymes of NADPH-forming metabolic pathways in human leukocytes: (a) Glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating) were less active in leukocytes (mostly myeloblasts) from eight patients with acute myeloblastic leukemia (I) than in leukocytes (mostly granulocytes) from 16 normal subjects (II). (b) Of the enzymes of the citrate cleavage pathway, ATP citrate lyase and malate dehydrogenase (decarboxylating) (NADP+) were virtually absent in the cells studied. (c) Isocitrate dehydrogenase (NADP+), aspartate aminotransferase, and alanine aminotransferase, which, together with the much more active malate dehydrogenase, constitute a newly proposed NADPH-forming metabolic cycle, showed a higher activity in I than in II or III, and therefore could compensate, as concerns NADPH-generation, for the low activity of pentose cycle dehydrogenases. We are not sure whether the enzymatic characteristic of I cells is attributable to their immaturity or to their leukemic nature.
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PMID:Enzyme activities of NADPH-forming metabolic pathways in normal and leukemic leukocytes. 23 46

Enzymes of parasite origin were identified by starch-gel electrophoresis. The species of parasite studied were Plasmodium berghei, Plasmodium yoelii nigeriensis, Babesia rodhaini and Anthemosoma garnhami. Lactate dehydrogenase, glucose phosphate isomerase and (NADP) glutamate dehydrogenase were detected in all species; phosphogluconate dehydrogenase was detected in both Plasmodium species but malate dehydrogenase only in P. y. nigeriensis. Glucose-6-phosphate dehydrogenase, alanine aminotransferase and aspartate aminotransferase were not detected in any parasite.
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PMID:Biochemistry of intraerythrocytic parasites. I. Identification of enzymes of parasite origin by starch-gel electrophoresis. 38 67

Three enzymes selected as representative of major metabolic pathways (malic dehydrogenase, of the citric acid cycle, lactic dehydrogenase, of glycolysis and glucose-6-phosphate dehydrogenase, of the pentose pathway) were measured by quantitative histochemical methods in individual hypothalamic nuclei during the 5-day estrous cycle of adult rats. Malic dehydrogenase increases significantly from low proestrous levels to a peak at estrus and then declines during diestrus in the following nuclei and areas of the anterior hypothalamus: medial and lateral preoptic, suprachiasmatic, supraoptic, and anterior. Significant peaks of lactic dehydrogenase occur more often during diestrus-3 in hypothalamic nuclei of the middle and posterior hypothalamus, Glucose-6-phosphate dehydrogenase has a biphasic pattern with peaks usually occurring during the diestrous period.
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PMID:Quantitative histochemical studies of the hypothalamus. Dehydrogenase enzymes during the estrous cycle. 103 42

Enzyme electrophoresis was conducted on 10 Schistosoma mattheei adult worm samples, comprising 270 individuals, collected from cattle in the Eastern Transvaal Lowveld. Glucose-6-phosphate dehydrogenase (G6PDH) was studied in all the samples and phosphoglucomutase (PGM) and malate dehydrogenase (MDH) in five populations each. Only one population was polymorphic for G6PDH. In this population, in addition to the allele found in all the other samples, a second allele occurred with a similar Rf value to S. haematobium. The two alleles were in Hardy-Weinberg equilibrium. MDH-1 exhibited two alleles. However, these alleles were not in equilibrium. In certain populations, heterozygotes occurred together with homozygotes of one of the alleles only. PGM was monomorphic in all the populations studied.
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PMID:Enzyme polymorphism in Schistosoma mattheei from cattle in the Eastern Transvaal Lowveld. 252 8

Adipose tissue growth was studied in two experiments. In the first one, 36 Alpine male kids fed with milk replacer only were slaughtered at 8, 14 or 20 kg (groups A, B and C, respectively). Perirenal adipose tissue developed earlier than omental adipose tissue, but from about 30 days of age, the latter was heavier (allometric coefficients: 2.18 and 1.36 for omental and perirenal adipose tissues, respectively). Even in group C animals, subcutaneous adipose tissue was scarce. When expressed in grams of wet tissue, the lipoprotein lipase (LPL) activity of omental adipose tissue decreased with age. This decline was more marked between groups B and C than between groups A and B (37 and 14%, respectively). Total LPL activity of omental tissue was 3-fold higher in group B than in group A and 3.7-fold higher in group C than in group A. This activity apparently had no relation with the amount of milk intake, daily mean weight gain or omental adipose tissue weight. In the second experiment, 18 male kids were slaughtered unweaned at 6 weeks or 2 or 14 days after weaning (groups A, B and C, respectively). After weaning, the weight of all adipose tissues decreased. Perirenal adipose tissue weight diminished earlier and more intensively than in the other adipose tissues (80% weight drop in 14 days). The weight loss of omental, pericardiac and mesenteric adipose tissue was 65, 49 and 15%, respectively. As with other lipogenic enzymes, the activity of LPL was highest in omental adipose tissue. In perirenal, pericardiac and mesenteric tissues LPL activity was 30, 45 and 60% less than omental activity. In sternal adipose tissue, LPL activity was very low. Acetyl CoA carboxylase (ACX) was active in the internal tissues of unweaned kids, but at a low level, i.e. about one-twentieth of that of LPL. Glucose-6-phosphate dehydrogenase (G6PDH) had a higher activity than NADP-malate dehydrogenase (EM). Soon after weaning, all of these enzyme activities dropped sharply. Two days after weaning, LPL activity declined by about 90% in all tissues, but 14 days after weaning it rose again, especially in perirenal adipose tissue. However, it reached a lower value than in unweaned kids. On the contrary, 14 days after weaning, group C ACX activity returned to a lower value than that of group B.
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PMID:[Weight and metabolism of lipid reserves during the growth of kids]. 285 44

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

A number of metabolic factors and the activity of a number of enzymes were determined in meal-fed (animals fed a single daily 2 hr meal) and nibbling (ad libitum-fed) rats. The dependency of the observed adaptive changes on the ingestion of carbohydrate was studied by feeding diets high in carbohydrate or fat. Glucose-6-phosphate dehydrogenase and NADP-malic dehydrogenase were more active in adipose tissue from high carbohydrate meal-fed rats than in tissue from ad libitum-fed rats. The activity in adipose tissue of isocitric dehydrogenase, 6-phosphogluconate dehydrogenase, and NAD-malic dehydrogenase did not increase significantly in response to meal-feeding the high carbohydrate diet. No increase in lipogenesis or enzyme activity could be demonstrated in adipose tissue from rats meal-fed a high fat diet. Lipase activity of adipose tissue was increased by high carbohydrate meal-feeding and decreased by feeding a high fat diet. The in vitro uptake of palmitate-1-(14)C by adipose tissue was depressed by a high fat diet and enhanced in rats meal-fed a high carbohydrate diet. Diaphragm or slices of liver from high fat-fed rats oxidized palmitate-1-(14)C more rapidly than did tissue from ad libitum-fed animals. Evidence is presented for the quantitative importance of citrate as a source of extramitochondrial acetyl CoA in adipose tissue of meal-eating and ad libitum-fed rats. The relationship of extramitochondrially formed citrate to the NAD-malic dehydrogenase-malic enzyme system in adipose tissue is discussed.
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PMID:Adaptive changes in enzyme activity and metabolic pathways in adipose tissue from meal-fed rats. 590 Feb 21

In anaerobically glucose-grown yeast isocitrate lyase (EC 4.1.3.1.), and malate dehydrogenase (EC 1.1.1.37.) are repressed by glucose. 24 h cultures still contain 0.3--0.4% glucose in the medium, which is enough to completely repress these activities. Aeration of these cells, in buffer containing acetate, initiates the formation of the three enzymes. Within 16 h, the specific activities of these enzymes increase about 140, 120 and 70-fold, respectively. Glucose-6-phosphate dehydrogenase activity was not altered. When the yeast was grown anaerobically, but with a supplement of an unsaturated fatty acid in the medium, synthesis of the three enzymes was much faster and the specific activities after 16 h of derepression were considerably higher. A relationship exists between the number of double bonds in the unsaturated fatty acid molecule and its capability to stimulate enzyme synthesis: linolenic acid is more effective than linoleic acid, which, in turn, is much more effective than oleic acid. Increasing periods of aeration with glucose of anaerobically grown cells prior to derepression results in an increasing stimulation of enzyme synthesis on subsequent derepression. Anaerobic incubation of yeast in the presence of an unsaturated fatty acid in advance to derepression also increased the velocity of enzyme formation. It is suggested that during the aeration period with glucose and during anaerobic incubation with an unsaturated fatty acid a more active protein synthesizing apparatus was formed.
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PMID:Effect of unsaturated fatty acids on the biosynthesis of glucose-repressed enzymes in yeast. 702 32

Alkali-burnt corneas of the rabbits with 1 N NaOH were studied periodically for enzymatic activities by biochemical methods. There was significant increase of aldolase (ALD) activity both in corneal epithelium and stroma 1, 2, 3 and 4 weeks after alkali burns. Glucose-6-phosphate dehydrogenase (G6PD) activity was significantly decreased in epithelium and was absent in stroma. Thus the breakdown of glucose would be present preferably in the Embden-Meyerhoff pathway instead of the pentose phosphate shunt. Lactate dehydrogenase (LDH) activity of corneal epithelium and stroma was significantly decreased 1, 2, 3, and 4 weeks after alkali burns and the possible pathway of glycolysis might channel to citric acid cycle, in which malate dehydrogenase (MDH) could indicate the important role in this pathway.
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PMID:The enzymatic activities in the alkali-burnt rabbit cornea. 709 40

Glucose-6-phosphate dehydrogenase and NADP-linked malate dehydrogenase were studied in different areas of the brain of three altricial birds during posthatching development. The birds were pigeon and swift, having a posthatching nestling period of 30 days; and sparrow, having a posthatching nestling period of 14 days. The activity of the two enzymes was high during development. G-6-PD activity may be high because of the need for pentoses in the early part of development and the need for reducing equivalents (NADPH2) for synthesis of lipids and other compounds in the later stages of development. Malic enzyme activity also seems to be high because of the need for reducing equivalents. The activity of malic enzyme was found to be higher than that of G-6-PD.
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PMID:Glucose-6-phosphate dehydrogenase and NADP-linked malate dehydrogenase during posthatching development of brain of altricial birds. 721 67


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