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

Repeated injections of rat with 1-thyroxine (50 microgram/kg daily for 5 five-day weeks) retarded the weight gain of the animals and increased the absolute and relative size of the heart, adrenals and interscapular brown adipose tissue. In the myocardium and thigh muscle, thyroxine treatment resulted in elevated activity of oxidative enzymes, succinate dehydrogenase, malate dehydrogenase and citrate synthase, while the activities of glycolytic enzymes remained unchanged. Glycogen content of the heart was decreased following thyroxine regime. In the brown fat, on the other hand, thyroxine injections resulted in a reduction of the activity of oxidative enzymes. This reduction can be accounted for by the decreased protein (enzyme) content of the tissue due to deposition of fat. Furthermore, thyroxine treatment delayed the body cooling of the rats swimming in water at 25 degrees C and enhanced hyperthermic response to injected noradrenaline. All these changes, which were not observable in rats treated with daily alprenolol (20 mg/kg) injections, were as pronounced in rats injected with alprenolol together with thyroxine as in rats injected with thyroxine only. It is concluded that beta blockers do not antagonize the metabolic changes due to hyperthyroidism.
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PMID:Alprenolol fails to antagonize the metabolic changes following repeated thyroxine injections in the rat. 2 61

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.
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PMID:Pyruvate and citrate metabolism in the muscle tissue of Ascaris lumbricoides. 2 88

Citrate synthase of Escherichia coli reacts rapidly with 1 equivalent of Ellman's reagent, 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), per subunit, losing completely its sensitivity to the allosteric inhibitor, NADH. When the enzyme is treated instead with 4,4'-dithiodipyridine (4,4'-PDS), all activity is lost. Certain evidence in this paper is consistent with the belief that the sulfhydryl group modified by DTNB, and that whose modification by 4,4'-PDS inactivates the enzyme, are the same. (i) Both reagents abolish NADH fluorescence enhancement by the enzyme. (ii) Saturating levels of NADH and some other adenylic acid derivatives inhibit the reactions with both reagents. (iii) When the enzyme is modified with one equivalent of DTNB or 4,4'-PDS, subsequent reactivity toward the other reagent is greatly decreased. (iv) Following modifications, the DTNB and 4,4'-PDS derivatives spontaneously lose thionitrobenzoate (TNB) or pyridine-4-thione (PT), respectively, in reactions which are thought to involve displacement of TNB or PT by a second enzyme sulfhydryl group, so that an enzyme disulfide is introduced. The introduction of the disulfide bond, if this is what occurs, does not lead to cross-linking of citrate synthase polypeptide chains, as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis under nonreducing conditions. Certain evidence has also been found, however, that the sites of modification by DTNB and 4,4'-PDS are not the same. (i) DTNB modification desensitizes to NADH but does not inactivate, while 4,4'-PDS inactivates at least 99.9%. (ii) The presumed disulfide from elimination of TNB is also active, while that from PT modification is no more active than the original 4,4'-PDS modified product. (iii) Prior modification of the enzyme with DTNB affords no protection against later inactivation by 4,4'-PDS. The studies therefore indicate a close relationship between the DTNB desensitization and 4,4'-PDS inactivation, but they are unable to identify it exactly. Other properties of the DTNB reaction are also described, and a hypothesis is offered to explain quantitatively the finding that desensitization lags behind modification during the modification of citrate synthase by DTNB.
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PMID:The reactions of Escherichia coli citrate synthase with the sulfhydryl reagents 5,5'-dithiobis-(2-nitrobenzoic acid) and 4,4'-dithiodipyridine. 3 91

Representative enzyme activities of energy supplying metabolism were measured in muscle specimens of brachial biceps, deltoid or anterior tibial muscle of patients with affections of the peripheral nerves. Simultaneously performed measurements of the same enzyme activities in the contralateral normal muscles served as a control. 5 patients suffered from a lesion of the brachial plexus, 7 patients had a paralysis of the axillary nerve, and 8 patients had a peroneal paralysis. In all denervated muscles no electrophysiological signs of reinnervation were present. The activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase were found to be highest in the normal brachial biceps muscle. Lower activities were measured in the normal deltoid and anterior tibial muscle. The oxidative enzymes, 3-hydroxyacyl-CoA dehydrogenase and citrate synthase as well as hexokinase, showed no significant difference from the levels of the control. It is suggested that a probable factor determining the differences of the enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between brachial biceps, deltoid and anterior tibial muscle, might be the pattern of impulse activity in the motor nerves of these muscles. The enzyme activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase, decreased rapidly during the first 2 months after denervation in the brachial biceps, deltoid and anterior tibial muscle, whereas the decrease was slight during the following months. The activities of the oxidative enzymes (3-hydroxyacyl-CoA dehydrogenase and citrate synthase) showed no significant change after denervation. The metabolic difference of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between the three muscles was no longer maintained. The possible causes of the deeply decreased enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation, as well as the causes of the unchanged oxidative enzyme activities and of the increased hexokinase activity after denervation in the human brachial biceps, deltoid and anterior tibial muscle, are discussed.
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PMID:[Representative enzymes of energy supplying metabolism in the normal and denervated human brachial biceps, deltoid and anterior tibial muscles (author's transl)]. 5 9

Male 13-lined ground squirrels induced to emerge from hibernation resumed feeding and gained weight. The weight gain was supported by increases in the levels of glucose 6-phosphate dehydrogenase, L-alanine aminotransferase and carnitine acetyltransferase in the liver. Maturation of the testis occurred in a period of about 16 days spanning the time of induced arousal. The testes of hibernating males were characterized by higher levels of L-alanine aminotransferase, glucose 6-phosphate dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase than the testes of aroused males. Hexokinase, carnitine acetyltransferase and citrate synthase levels were similar in the testes of hibernating and aroused males. 3-Hydroxyacyl-CoA dehydrogenase was more active and L-alanine aminotransferase less active in ground squirrel sperm than in rat sperm.
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PMID:Changes in enzyme levels in the testis and liver of the 13-lined ground squirrel (spermophilus tridecemlineatus) at the time of arousal from hibernation. 7 Oct 81

Normal values are given for the activities of pyruvate carboxylase (E.C.6.4.1.1), mitochondrial phosphoenolpyruvate carboxykinase (E.C. 4.1.1.32, PEPCK), and citrate synthase (E.C. 4.1.3.7) in fibroblasts, lymphocytes, and leukocytes. Also given are values for these enzymes in the leukocytes and fibroblasts from a severely mentally and developmentally retarded patient with proximal renal tubular acidosis and hepatic, cerebral, and renal cortical pyruvate carboxylase deficiency. In normals, virtually all of the mitochondrial PEPCK and pyruvate carboxylase activity was present in the mononuclear leukocyte fraction of whole venous blood. Cellular fractionation studies with human lymphocytes and fibroblasts demonstrated that all of the PEPCK activity in these cells is mitochondrial. Normal values for pyruvate carboxylase in leukocytes were 0.092 (0.070--0.208) mU/mg protein (n=5), in lymphocytes 0.154 (0.092--0.262) mU/mg protein (n=5), and in fibroblasts 1.36 (0.778--2.19) mU/mg protein (n=5). The patient with hepatic, renal, and cerebral pyruvate carboxylase deficiency had no detectable activity (less than 0.009 mU/mg protein) in his leukocytes and 0.018 mU/mg protein in his fibroblasts. Data from an assay for pyruvate carboxylase activity in the patient's fibroblasts show that the activity observed is significant but very close to the lower limits of the assay. Values for PEPCK in normal lymphocytes were 1.42 (0.824--1.88) mU/mg protein (n=5), in leukocytes 1.68 (1.64--1.72) mU/mg protein (n=2), and in fibroblasts 5.49 (3.94--6.33) mU/mg protein (n=6).
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PMID:Pyruvate carboxylase and phosphoenolpyruvate carboxykinase activity in leukocytes and fibroblasts from a patient with pyruvate carboxylase deficiency. 10 9

Differences of metabolic qualities and capacities among organs and tissues of perinatal rabbits were investigated. A suitable alternative for the measurement of substrate utilization of single organs seems to be the total amount of certain key enzyme activities calculated for whole organs. The immediate perinatal period is the object of this study with adult animals serving as a reference. We have selected the phosphofructokinase activity to represent the upper segment of glycolytic reactions, 3-hydroxyacyl-CoA dehydrogenase as a key enzyme for beta-oxidation of fatty acids and citrate synthase activity to represent the Krebs cycle activity. In fetal, newborn, and adult rabbits we analyzed liver, kidneys, heart, lung, brain, brown and white adipose tissue, stomach and intestines, skin, a representative sample of skeletal muscles, and of bones. The organ weight distribution, total amount of protein, and DNA was determined for the same ten organs. The share each organ contributes to the total body key enzyme activity shows the importance of each metabolic capacity which is represented by the three enzymes. In perinatal adipose tissue the very high potential for energy production through utilization of Krebs cycle reactions is striking. The same tissue has a high capacity to oxidize fatty acids. The skeletal muscle represents the biggest capacity of glycolytic reactions in all age groups. After birth the metabolic profile of the whole organism shows a marked and steep increase of glycolytic capacity, whereas the capacity to oxidize fatty acids decreases slowly.
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PMID:Perinatal changes of interorgan differences in cell metabolism. 12 90

2-Methylcitrate was tested in vitro on enzymes which interact with citrate and isocitrate. It was found to inhibit citrate synthase, aconitase, the NAD+- and NADP+-linked isocitrate dehydrogenase. This inhibition was competitive in nature except in the case of aconitase, and the Ki for all the enzymes was in the range of 1.5-7.6 mM. Phosphofructokinase was also inhibited by 2-methylcitrate with 50% inhibition achieved at 1 mM. ATP-citrate lyase and acetyl-CoA carboxylase were not inhibited by this compound. 2-Methylcitrate was not a substrate for ATP-citrate lyase. Acetyl-CoA carboxylase was activated by 2-methylcitrate with a Ka of 2.8 mM. The apparent Km (3.3 mM) for 2-methylcitrate for the mitochondrial citrate transporter was about 10-fold higher than the apparent Km (0.26 mM) for citrate. The tricarboxylase carrier can also be inhibited by low concentrations (0.2 mM) of 2-methylcitrate when the concentration of citrate is close to the apparent Km. Accumulation of 2-methylcitrate inside the mitochondrion, therefore, might lead to inhibition of enzymes in the citric acid cycle and thereby contribute to the ketogenesis and hypoglycemia seen under these conditions.
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PMID:Effect of 2-methylcitrate on citrate metabolism: implications for the management of patients with propionic acidemia and methylmalonic aciduria. 12 73

The metabolic effects on rat cardiac and skeletal muscle of a strenous program of swimming, of cold acclimation and of isoprenaline treatment (0.3 mg/kg daily for 5 five-day weeks) were compared. Exercised and cold-exposed rats gained less body weight than did controls or isoprenaline-treated rats. In all treated groups the heart and the intercapular brown adipose tissue hypertrophied. The size of the adrenals increased only in isoprenaline-treated animals. Cold-acclimation and physical training increased and isoprenaline treatment reduced or did not affect the activities of succinate dehydrogenase, malate dehydrogenase and citrate synthase of cardiac muscle. In the skeletal muscle all treatments resulted in increased activities of these enzymes. Of the anaerobic enzymes analysed, only the activity of hexokinase increased in response to the treatements used. This increase was the same in cardiac as in skeletal muscle, but it was significantly greater with isoprenaline-treatment than with training or with cold-acclimation. The activities of lactate dehydrogenase and phosphofructokinase did not differ significantly. All treatments improved cold resistance, but only swimming exercise and cold acclimation significantly increased tolerance to exercise. It is concluded that prolonged stimulation of adrenergic beta-receptors by catecholamines is responsible for the metabolic changes observed.
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PMID:Comparison of the effects of physical exercise, cold acclimation and repeated injections of isoprenaline on rat muscle enzymes. 12 87

Fast-twitch plantaris muscles of female rats were subjected to unilateral compensatory overload, induced by partial excision of synergistic muscles. One group of rats remained sedentary whereas another was subjected to a supplemental program of treadmill exercise consisting of walking 3 m/min, 65% grade, 2 h/day, 5 days/week. Groups of rats were sacrificed after 1, 2, 4, and 8 weeks and their muscles were weighed and analyzed for protein, citrate synthase, phosphofructokinase (PFK) and myofibril ATPase. Absolute and relative (muscle weight/body weight) muscle weights were much greater in both overloaded groups as compared to contralateral controls. However, treadmill exercise also increased the absolute and relative muscle mass of control plantaris muscles in the exercising group as compared tonormal sedentary contralateral controls. Citrate synthase activity was decreased in overloaded, sedentary muscles as compared to contralateral controls, but after 8 weeks of exercise, it returned to normal levels. PFK was decreased in both sedentary and exercised overloaded muscles throughout the 8 week period. Myofibril ATPase showed a tendency to be reduced in sedentary, overloaded muscles, and was significantly reduced in overloaded, exercising muscles. These results collectively suggest that certain fibers of overloaded fast-patterns take on similar in certain aspects to that normally seen in differentiated slow-twitch muscle fibers.
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PMID:Enzymatic changes in hypertrophied fast-twitch skeletal muscle. 13 54


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