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:2.3.3.1 (citrate synthase)
4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Azotobacter beijerinckii was grown in ammonia-free glucose/mineral salts media in chemostat culture under oxygen or nitrogen limitation. Selected enzymes of the tricarboxylic acid cycle and poly-beta-hydroxybutyrate metabolism were monitored in relation to oxygen supply for both steady and transition states. Two dissolved oxygen concentrations were used for the nitrogen-limited steady state to investigate the possible effects of respiratory protection of nitrogenase on these enzymes. The levels of NADH oxidase, isocitrate dehydrogenase and 2-oxoglutarate dehydrogenase increased markedly on relaxation of oxygen limitation while pyruvate dehydrogenase and citrate synthase were relatively unaffected. beta-Ketothiolase and acetoacetyl-CoA reductase levels decreased as oxygen limitation was relaxed. Respiratory activity, as measured by the QO2 value, increased with oxygen supply rate. Imposition of oxygen limitation on a nitrogen-limited culture caused an immediate increase in the NADH/NAD ratio but this rapidly readjusted to its previous steady-state value. These changes are discussed in relation to respiratory protection of nitrogenase and poly-beta-hydroxybutyrate metabolism in A. beijerinckii.
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PMID:Regulation of the tricarboxylic acid cycle and poly-beta-hydroxybutyrate metabolism in Azotobacter beijerinckii grown under nitrogen or oxygen limitation. 1 43

The mechanism of the massive extracellular production of citric and isocitric acids by Saccharomycopsis lipolytica grown on n-paraffins has been studied. When growth stops, because of nitrogen limitation, the intracellular concentration of ATP sharply rises whereas that of AMP and ADP decreases to a low level. At the same time production of acids begins. The activity of the NAD-dependent isocitrate dehydrogenase which requires AMP for activity becomes very low and prevents the oxidative function of the citric acid cycle whereas isocitrate lyase is not inhibited. As citrate synthase inhibition by ATP appears to be insufficient to stop n-paraffin degradation, citric and isocitric acids accumulation can take place. Massive excretion of these acids, however, probably still involves other physiological changes brought about by nitrogen limitation, possibly some permeabilization of the cell to these acids.
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PMID:Regulation of the central metabolism in relation to citric acid production in Saccharomycopsis lipolytica. 88 90

The activity of key enzymes of the citrate and glyoxylate cycles was compared in yeast cells during intensive synthesis of citric acids and in its absence in the course of growth of Candida lipolytica on glucose ("glucose" yeast cells) and on hexadecane ("hexadecane" yeast cells). Citrate and isocitrate were found to be formed by the yeast in the tricarboxylic acid cycle. The ability of the yeast for "overproduction" of citrate and isocitrate during its growth on glucose and hexadecane depends on the high activity of the key enzyme of cycle, citrate synthase, as compared with the activity of other enzymes of the tricarboxylic acid cycle. Citrate predominated among excreted acids during growth on glucose in conditions of nitrogen deficiency while isocitrate prevailed during growth on hexadecane. The predominating synthesis of citrate in the first case seems to be related to a lower activity of aconitase in the "glucose" cells as compared with the "hexadecane" cells.
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PMID:[Enzyme activity of citrate, glyoxylate and pentosephosphate cycles during synthesis of citric acids by Candida lipolytica]. 100 46

The propionyl-CoA condensing enzyme which catalyzes the first step in the biosynthesis of 2-methylbutyrate and 2-methylvalerate by Ascaris muscle appears to exist in at least three forms in the mitochondria of this parasitic nematode. Two forms, A and B, were separated by ion exchange chromatography on CM-Sephadex. Chromatography on phosphocellulose resulted in the recovery of one minor peak (I) and two major peaks with activity (II and III). A and B as well as I, II, and III differed in their specific activities. Forms B and III were the most retained by their resins, and were the most active forms of the enzyme in each case. Inhibition studies with metabolites from Ascaris mitochondria indicate that CoASH, a product of the condensation reaction, and acetyl-CoA are effective inhibitors of the condensing and thiolytic activities of the Ascaris enzyme, respectively. Incubation of the active enzyme form B for 2 h with 0.1 mM CoASH at room temperature under nitrogen caused the loss of 92% of the propionyl-CoA condensing activity and 67% of the thiolase activity when assayed in standard mixtures. The propionyl-CoA condensing enzyme exhibited a hyperbolic dependence of the condensation velocity to changes in substrate concentration. However, in the presence of CoASH the Michaelis-Menten kinetics was transformed into a sigmoidal kinetics indicating a deviation from a simple product inhibition. Inactivation of the most active forms of the enzyme with CoASH was accompanied by (a) a change in the chemical reactivity of the protein toward p-chloromurcuribenzoate, (b) a change in the uv-visible spectrum of the protein, and (c) a change in the elution patterns from both CM-Sephadex and phosphocellulose column chromatography, where-upon one, two, or more protein peaks were obtained. The several protein peaks resolved by rechromatography of the [14C]CoASH-inactivated enzyme III on phosphocellulose had different CoASH contents. The elution positions were correlated with the less active forms (I and II) having increased [14C]CoASH activities. Similarly, the two peaks isolated upon rechromatography of the CoASH-partially inactivated enzyme B on CM-Sephadex had different isotope contents and the elution position of enzyme A corresponded to the less active form. The results described indicate that the CoASH modification of Ascaris propionyl-CoA condensing enzyme may be responsible for the existence of several forms of the enzyme and might represent a mode of control by chemically modulating the amount of the active forms of the enzyme.
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PMID:Propionyl-CoA condensing enzyme from Ascaris muscle mitochondria. II. Coenzyme A modulation. 167 27

Viable toadfish hepatocytes were separated into distinct subpopulations by gradient centrifugation. Although 3-5 density subpopulations were obtained for each fish, only two metabolically and enzymatically different subpopulations could be discerned. In all cases, hepatocytes with the lowest density (less than 1.040 g ml-1) were more oxidative in scope, as judged by the activities of mitochondrial enzymes (citrate synthase, aspartate aminotransferase, glutamate dehydrogenase); activities of these enzymes (normalised to cell protein) were on average two- to threefold higher than in subpopulations with higher densities. Lower-density hepatocytes also contained higher levels of the urea cycle enzymes arginase and ornithine carbamoyltransferase. The higher-density subpopulations showed no significant differences from each other in enzymatic activities. Compared with lower-density cells, these hepatocytes had higher activities of two cytosolic enzymes, malate dehydrogenase and glutathione-S-transferase. There was no distinct distribution pattern for alanine aminotransferase and glutamine synthetase. Despite generally lower oxidative enzyme content, higher-density hepatocytes were metabolically more active, with 2.5- to fourfold higher rates of urea synthesis, gluconeogenesis and oxidation of lactate. We conclude that, although the toadfish liver shows distinct enzymatic and metabolic heterogeneity, this heterogeneity is dissimilar to the zonation pattern in the livers of mammals, in that separated toadfish hepatocyte types did not appear to possess exclusive metabolic functions. Notably, all cells were capable of metabolic functions that are strictly localised in mammalian liver. In nitrogen metabolism, glutamine synthetase displays a distribution pattern commensurate with its unique metabolic function in the liver of the ureogenic toadfish. Further, all subpopulations possessed detoxification capabilities as indicated by high levels of glutathione-S-transferase, a 'phase II' conjugation enzyme.
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PMID:Metabolic and enzymatic heterogeneity in the liver of the ureogenic teleost Opsanus beta. 205 Nov 31

The growth and the activity of some enzymes were studied in a Candida lipolytica strain 12a which did not synthesize acids in a medium with glucose under the conditions of nitrogen deficiency. The substrate was not assimilated and cyanide-resistant respiration did not develop in the strain under the conditions of profound nitrogen deficiency. The inability of cells to assimilate glucose at the stationary phase of growth resulted, apparently, from an abrupt decrease of phosphofructokinase and pyruvate dehydrogenase activities in the cells. The activities of pyruvate carboxylase and citrate synthase fell down abruptly at the same time.
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PMID:[Comparative study of Candida lipolytica yeasts with various abilities to produce citrate]. 258 47

1. The effect of dexamethasone (30 micrograms day-1 100 g-1 body wt.) on the metabolism of glucose and glutamine was studied in the small intestine of rats after 9 days of treatment. 2. Dexamethasone treatment resulted in negative nitrogen balance (P less than 0.001), and produced increases in the concentrations of plasma glucose (22%, P less than 0.05), alanine (32%, P less than 0.001) and insulin (127%, P less than 0.001), but a decrease in the plasma concentration of glutamine (20%, P less than 0.05). 3. Portal-drained visceral blood flow increased by approximately 22% (P less than 0.001) in dexamethasone-treated rats, and was accompanied by a decrease in the arterio-venous concentration difference of glucose (43%, P less than 0.001) and an increase in that of lactate (22%, P less than 0.05), glutamine (35%, P less than 0.01), glutamate (33%, P less than 0.01) and alanine (21%, P less than 0.05). 4. Enterocytes isolated from dexamethasone-treated rats showed decreased and increased rates of glucose and glutamine utilization, respectively. 5. The maximal activities of hexokinase, 6-phosphofructokinase, citrate synthase and oxoglutarate dehydrogenase were decreased (30-64%, P less than 0.001) in intestinal mucosal scrapings of dexamethasone-treated rats, whereas the activity of glutaminase was increased (35%, P less than 0.001). 6. It is concluded that glucocorticoid administration decreases the rate of glucose utilization but increases that of glutamine (both in vivo and in vitro) by the epithelial cells of the small intestine. This may be caused by changes in the maximal activities of key enzymes in the pathways of glucose and glutamine metabolism in these cells.
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PMID:Effect of glucocorticoid treatment on glucose and glutamine metabolism by the small intestine of the rat. 340 28

A class of Azotobacter chroococcum mutants induced by Tn1 that were defective in normal aerobic nitrogen fixation when grown on sugars (Fos-) were corrected by provision of alpha-ketoglutarate or glutamate. In a representative mutant, Fos252, rates of evolution of 14CO2 from [14C]acetate or [14C]glucose were 5% of the parental values, although uptake and incorporation were normal for both substrates. The results suggest that a lesion affects the entry of substrates into the tricarboxylic acid cycle. The activity of citrate synthase in Fos252 in vitro was 5% that of the parents. The citrate synthase (gltA) gene from Escherichia coli was cloned into broad-host-range vectors and mobilized into Fos252. The plasmids restored parental citrate synthase activities to Fos252 and complemented the inability to fix N2 in air. The data indicate that a mutation causing an intrinsic limitation in respiratory capacity abolishes normal aerobic N2 fixation, which is consistent with the hypothesis of respiratory protection for nitrogenase in Azotobacter species.
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PMID:Lesions in citrate synthase that affect aerobic nitrogen fixation by Azotobacter chroococcum. 398 12

Burn injury is associated with an elevation in total body oxygen consumption, increased hepatic alanine uptake and conversion to glucose, and a negative nitrogen balance. The primary source of the alanine used for gluconeogenesis by the liver and of the nitrogen lost as urea is believed to be from skeletal muscle. Selected muscle regulatory enzymes and pyruvate and oleate oxidation rates were assayed for maximal activity during the postburn period. Male Sprague-Dawley rats that received 50% total body surface scald burns on the dorsum and abdomen were examined for citrate synthase (CS), phosphofructokinase (PFK), and glutamate-pyruvate transaminase (GPT) activity in uninjured muscle at 3, 7, 13, and 20 days postburn, and the ability of muscle to oxidize pyruvate and oleate was measured at 3 and 13 days after injury. Cs, PFK, and GPT activities increased significantly (p less than 0.05) by 13-20 days after injury in the soleus and diaphragm. The epitrochlearis showed no change in CS, but PFK and GPT were elevated within this time frame. The gastrocnemius muscle showed an elevated oleate oxidation rate at 13 days after injury, but no change at 3 days postburn. Pyruvate oxidation rates were unaltered. The results of this study indicate that during the postburn period several metabolic alterations occur in muscle. These adaptations include: (1) elevated CS activity which may be associated with increased oxidative capacity,, (2) increased PFK activity which implies that more substrate is being shuttled through the glycolytic pathway, (3) increased GPT activity which may reflect increased pyruvate conversion to alanine, and (4) increased oleate oxidation rates which demonstrate that muscle is utilizing more fatty acid substrates during the postburn period.
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PMID:Altered muscle metabolism in rats after thermal injury. 621 91

Intracellular and extracellular concentrations of citrate and the specific activities of ten different enzymes in Candida curvata D were examined in relation to lipid biosynthesis in batch and continuous culture. Citrate was found to accumulate prior to lipid production and declined markedly as lipid accumulated in batch culture. The cells excreted citrate as the culture became nitrogen-limiting after 30 hr of growth, but little more was expelled after 40 hr when lipid accumulation was more marked. In continuous culture, only low levels of citrate were detected at the lower dilution rates and citrate was completely absent from both the cells and medium above a dilution rate of 0.1/hr. The activity of malic enzyme, malate dehydrogenase and ATP:citrate lyase increased in batch culture on lipid accumulated and, in continuous culture, both malic enzyme and ATP:citrate lyase varied in parallel with the specific rate of lipid synthesis which increased with increasing dilution rate. Activity of malate dehydrogenase, citrate synthase and glucose-6-phosphate dehydrogenase decreased with increasing dilution rate. The regulatory significance of these enzymes in lipid accumulation by C. curvata is discussed.
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PMID:Biochemical activities during lipid accumulation in Candida curvata. 663 68


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