Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Citrate synthase activity of Saccharomyces cerevisiae was determined by a radioactive assay procedure and the reaction product, 14C-citric acid, was identified by chromatographic techniques. ATP, d-ATP, GTP and NADH were most inhibitory to the citrate synthase invitro. The activity was inhibited to a lesser extent by ADP, UTP, and NADP whereas, AMP and CTP were much less inhibitory. NADH, like NAD, glutamic acid, glutamine, arginine, ornithine, proline, aspartic acid and alpha-ketoglutarate exhibited no inhibition. These results have been discussed in the light of the role of citrate synthase for the energy metabolism and glutamic acid biosynthesis.
 ...
PMID:Regulation of citrate synthase activity of Saccharomyces cerevisiae. 0

Aconitase and NAD linked isocitrate dehydrogenase were present in Ascaris lumbricoides muscle at only very low activities, whilst there were significant levels of citrate synthase, NADP linked isocitrate dehydrogenase, 2-oxoglutarate dehydrogenase and succinic thiokinase. Pyruvate dehydrogenase was present in A. lumbricoides muscle at levels comparable with mammalian tissues and results suggest that it is modulated via a phosphotransferase/phosphatase system. The tricarboxylic acid cycle intermediates, citrate, isocitrate and 2-oxoglutarate were all detected in freeze clamped muscle, but their steady state levels were considerably lower than those found in mammalian tissues.
 ...
PMID:Pyruvate and citrate metabolism in the muscle tissue of Ascaris lumbricoides. 2 88

The occurrence and levels of activity of various enzymes of carbohydrate catabolism in culture forms (promastigotes) of 4 human species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, and L. tropica) were compared. These organisms possess enzymes of the Embden-Meyerhof pathway but lack lactate dehydrogenase. No evidence could be found for the production of lactic acid by growing cultures and lactic acid could not be detected either in cell-free preparations or after incubation of cell-free extracts with pyruvate and NADH under appropriate conditions. All 4 species possess alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate phosphatase which together could regenerate NAD, thus compensating for the absence of lactate dehydrogenase. The oxidative and nonoxidative reactions of the hexose monophosphate pathway are present in all 4 species. Cell-free extracts have pyruvate dehydrogenase activity which allows the entry of pyruvate into and its subsequent oxidation through the tricarboxylic acid cycle. All enzymes of this cycle, including a thiamine pyrophosphate dependent alpha-ketoglutarate dehydrogenase, are present. Both NAD and NADP-linked malate dehydrogenase activities are present. The isocitrate dehydrogenase is NADP specific. There is an active glutamate dehydrogenase which could compete with alpha-ketoglutarate dehydrogenase for the common substrate (alpha-ketoglutarate). Replenishment of C4 acids is accomplished by heterotrophic CO2 fixation catalyzed by pyruvate carboxylase. All 4 species have high levels of NADH oxidase activity. Several enzymes thus far not found in any species of Leishmania have been demonstrated. These are: phosphoglucose isomerase, triose phosphate isomerase, fructose-1, 6-diphosphatase, 3-phosphoglycerate kinase, enolase, alpha-glycerophosphate dehydrogenase, alpha-glycerophosphate phosphatase, pyruvate dehydrogenase complex, citrate synthase, aconitase, alpha-ketoglutarate dehydrogenase, glutamate dehydrogenase, and NADH oxidase.
 ...
PMID:Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative survey. 100 46

The effects of a 500 mug injection of T3 on the renal handling of citrate by the albino rat was studied by measuring citrate synthase activity, NADP-isocitrate dehydrogenase activity, and plasma, kidney, and urine citrate concentrations 12, 18, 24, 36, and 48 hr after injection. Kidney citrate synthase activity of the T3-injected rats was significantly lower than the controls in the 24- and 36-hr treatment groups, while NADP-IDH activity was significantly lowered only in the 36-hr treatment group. The injection of T3 resulted in hypercitricemia in the 12-, 18-, and 48-hr experimental animals while there was no significant change in citrate between the control values and treated values in the 24- and 36-hr experiments. There was no significant change in renal citrate levels in any of the treatment groups and hypercitrauria was not observed. The results of the present study suggest that T3 can control citrate utilization by increasing the levels of circulating citrate and then increasing the utilization of citrate by the kidney. This is facilitated by a decrease in NADP-IDH activity resulting in a decrease in biosynthesis and a decrease in citrate synthase activity resulting in a decrease in FFA metabolism. It is proposed that this system functions in providing fuel (citrate) for the increased Krebs cycle flux occurring in hyperthyroidism.
 ...
PMID:The effect of 3,3',5-triiodo-L-thyronine on the renal handling of citrate. 115 25

1. The pattern of NADP-linked malic enzyme activity estimated in the whole brain homogenate did not parallel that found in liver of developing rat. 2. Studies on intracellular distribution of malic enzyme in brain showed that the mitochondrial enzyme increased about three-fold between 10th and 40th day of life. Thereafter, a slow gradual increase to the adult level was observed. 3. The extramitochondrial malic enzyme from brain, like the liver enzyme, increased at the time of weaning, although to a lesser extent. At day 5 the brain malic enzyme was equally distributed between mitochondria and cytosol. 4. During the postnatal development, the contribution of the mitochondrial malic enzyme in the total activity was increasing, reaching the value approx. 80% at day 150 after birth. 5. The increase with age of the malic enzyme specific activity was observed in both synaptosomal and non-synaptosomal mitochondria, the changes in the last fraction being more pronounced. 6. The activity of citrate synthase developed markedly between 10-40 postnatal days, increasing about five-fold, while the specific activity of the enzyme did change neither in the synaptosomal nor in non-synaptosomal mitochondria at this period. 7. We conclude that the changes in malic enzyme activity in the developing rat brain are mainly due both to the increase of mitochondrial protein content and to the increase of specific activity of the mitochondrial malic enzyme.
 ...
PMID:Changes of malic enzyme activity in the developing rat brain are due to both the increase of mitochondrial protein content and the increase of specific activity. 173 93

The superficial muscle fibres in the proximal part of the closer muscle in the crab Eriphia can be separated into four fibre groups (I-IV) on the basis of electrophysiological and histochemical characteristics. The activity levels of glyceraldehydephosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH), citrate synthase (CS), NADP-isocitrate dehydrogenase (IDH) and 3-hydroxyacyl-CoA dehydrogenase (HAD), determined in single electrophysiologically identified fibres, differed significantly among the different fibre groups. In addition, fibres belonging to the same group, with similar electrophysiological characteristics, demonstrated variability with regard to metabolic enzyme activities. Nevertheless, comparison of absolute enzyme activities and enzyme activity ratios permitted the discrimination of at least three groups. These groups corresponded with those defined according to electrophysiological and histochemical characteristics. The group I fibres (tonic fibres) are intermediate in oxidative potential and show the lowest values of glycolytic enzymes. The group II and group III fibres can be regarded as fast oxidative fibres. The high ratio between activity levels of enzymes for glycolytic and oxidative metabolism found for group IV fibres (fast fibres) demonstrated that this group depends strongly on anaerobic metabolism.
 ...
PMID:Enzyme activities in single electrophysiologically identified crab muscle fibres. 370 50

The activities of NADP-linked malic enzyme, hexose monophosphate shunt dehydrogenases and NADP-linked isocitrate dehydrogenase were studied during development of skeletal muscle and compared with those in the liver. The variation patterns of malic enzyme activity in the liver and in the skeletal muscle were very similar, however the amplitude of the changes was different. The enzyme activity increased approx 16-fold in the liver and about 2-fold in skeletal muscle at the same stage of development. In skeletal muscle the increase of the malic enzyme activity was only slightly higher than of lactic dehydrogenase and citrate synthase. Studies on the intracellular distribution of malic enzyme in skeletal muscle showed that both mitochondrial and extramitochondrial enzymes increased between 20th and 37th day of life, the increase of the extramitochondrial enzyme being more pronounced. The hexose monophosphate shunt dehydrogenases activity showed an increase in the liver but no change was observed in the skeletal muscle at the weaning time. Changes in the activity of the liver and skeletal muscle isocitrate dehydrogenase were not significant between 10th and 80th day of life. The results suggest that the malic enzyme in the liver is playing a different physiological role than in the skeletal muscle.
 ...
PMID:Changes of the NADP-linked malic enzyme in the developing rat skeletal muscle. 400 45

Four enzyme activities related to glucose metabolism, i.e. those of glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49), lactic dehydrogenase (LDH; EC 1.1.1.27), pyruvate dehydrogenase complex (PDC) and citrate synthase (CS; EC 4.1.3.7) were estimated in posterior root ganglion cells (PRGCs) of the spinal cord in patients suffering from olivopontocerebellar atrophy (OPCA), amyotrophic lateral sclerosis (ALS), and Duchenne muscular dystrophy (DMD) by means of the NAD, NADP and CoA cycling methods. In ALS and DMD, the enzyme activities examined were within normal ranges. In OPCA, PDC activity was significantly reduced and LDH activity tended to be lower than that in controls.
 ...
PMID:Enzymatic analysis of individual posterior root ganglion cells in olivopontocerebellar atrophy, amyotrophic lateral sclerosis and Duchenne muscular dystrophy. 404 97

Fat-cells were prepared from rat and guinea-pig epididymal adipose tissue and compared on the basis of the intracellular distributions and activities of enzymes and with respect to their utilization of various U-(14)C-labelled substrates for lipogenesis. 1. Compared with the rat, guinea-pig extramitochondrial enzyme activities differed in that aconitate hydratase, alanine aminotransferase, ATP-citrate lyase, lactate dehydrogenase, NAD-malate dehydrogenase, NADP-malate dehydrogenase and phosphoenolpyruvate carboxykinase activities were appreciably lower, whereas aspartate aminotransferase, glucose 6-phosphate dehydrogenase, NADP-isocitrate dehydrogenase and 6-phosphogluconate dehydrogenase activities were appreciably higher. Mitochondrial activities of citrate synthase, NADP-isocitrate dehydrogenase and pyruvate carboxylase were appreciably lower, whereas mitochondrial activities of aspartate aminotransferase, glutamate dehydrogenase, NAD-malate dehydrogenase and phosphoenolpyruvate carboxykinase were higher in the guinea pig compared with the rat. 2. In general guinea-pig fat-cells incorporated acetate and lactate into fatty acids more readily than rat fat-cells, whereas rat fat-cells incorporated glucose and pyruvate more readily than guinea-pig fat-cells. 3. Acetate stimulated the incorporation of glucose into fatty acids in rat fat-cells, but had no appreciable effect upon this process in guinea-pig fat-cells. Acetate greatly decreased the incorporation of lactate into fatty acids in cells from both species. 4. Lactate/pyruvate ratios produced by incubation of guinea-pig cells with glucose+insulin were very low compared with those found with rat cells under the same conditions. 5. With glucose (+insulin) or with glucose+acetate (+insulin) as substrates guinea-pig cells produced enough NADPH by the hexose monophosphate pathway to satisfy the NADPH requirements of lipogenesis. In rat fat-cells under the same conditions, hexose monophosphate-pathway NADPH provision was not sufficient to meet the requirements of lipogenesis. 6. These results are discussed, particularly in relationship to the disposition of cytosolic reducing equivalents in the cells.
 ...
PMID:Lipogenesis in rat and guinea-pig isolated epididymal fat-cells. 415 67

1. A method is described for extracting separately mitochondrial and extramitochondrial enzymes from fat-cells prepared by collagenase digestion from rat epididymal fat-pads. The following distribution of enzymes has been observed (with the total activities of the enzymes as units/mg of fat-cell DNA at 25 degrees C given in parenthesis). Exclusively mitochondrial enzymes: glutamate dehydrogenase (1.8), NAD-isocitrate dehydrogenase (0.5), citrate synthase (5.2), pyruvate carboxylase (3.0); exclusively extramitochondrial enzymes: glucose 6-phosphate dehydrogenase (5.8), 6-phosphogluconate dehydrogenase (5.2), NADP-malate dehydrogenase (11.0), ATP-citrate lyase (5.1); enzymes present in both mitochondrial and extramitochondrial compartments: NADP-isocitrate dehydrogenase (3.7), NAD-malate dehydrogenase (330), aconitate hydratase (1.1), carnitine acetyltransferase (0.4), acetyl-CoA synthetase (1.0), aspartate aminotransferase (1.7), alanine aminotransferase (6.1). The mean DNA content of eight preparations of fat-cells was 109mug/g dry weight of cells. 2. Mitochondria showing respiratory control ratios of 3-6 with pyruvate, about 3 with succinate and P/O ratios of approaching 3 and 2 respectively have been isolated from fat-cells. From studies of rates of oxygen uptake and of swelling in iso-osmotic solutions of ammonium salts, it is concluded that fat-cell mitochondria are permeable to the monocarboxylic acids, pyruvate and acetate; that in the presence of phosphate they are permeable to malate and succinate and to a lesser extent oxaloacetate but not fumarate; and that in the presence of both malate and phosphate they are permeable to citrate, isocitrate and 2-oxoglutarate. In addition, isolated fat-cell mitochondria have been found to oxidize acetyl l-carnitine and, slowly, l-glycerol 3-phosphate. 3. It is concluded that the major means of transport of acetyl units into the cytoplasm for fatty acid synthesis is as citrate. Extensive transport as glutamate, 2-oxoglutarate and isocitrate, as acetate and as acetyl l-carnitine appears to be ruled out by the low activities of mitochondrial aconitate hydratase, mitochondrial acetyl-CoA hydrolyase and carnitine acetyltransferase respectively. Pathways whereby oxaloacetate generated in the cytoplasm during fatty acid synthesis by ATP-citrate lyase may be returned to mitochondria for further citrate synthesis are discussed. 4. It is also concluded that fat-cells contain pathways that will allow the excess of reducing power formed in the cytoplasm when adipose tissue is incubated in glucose and insulin to be transferred to mitochondria as l-glycerol 3-phosphate or malate. When adipose tissue is incubated in pyruvate alone, reducing power for fatty acid, l-glycerol 3-phosphate and lactate formation may be transferred to the cytoplasm as citrate and malate.
 ...
PMID:The intracellular localization of enzymes in white-adipose-tissue fat-cells and permeability properties of fat-cell mitochondria. Transfer of acetyl units and reducing power between mitochondria and cytoplasm. 439 82


1 2 3 4 5 Next >>