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)

Transcriptional regulation was demonstrated in Rickettsia prowazekii, an obligate intracytoplasmic bacterium. The level of citrate synthase (gltA) mRNA II, from promoter P2, was greater in the total RNA isolated from heavily infected L929 cells than in moderately infected L929 cells; conversely, the level of ATP/ADP translocase (tlc) mRNA was greater in moderately infected cells. The level of gltA mRNA I, from promoter P1, did not change under these conditions. The chemical half-lives of gltA mRNA II and tlc mRNA under these conditions were very similar.
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PMID:Transcriptional regulation in the obligate intracytoplasmic bacterium Rickettsia prowazekii. 880 50

The objective of this study was to investigate the effects of single and repeated administration of CP-55,940 [(-)-cis-3-[2-hydroxy-4-(1, 1-dimethylheptyl)-phenyl]-trans-4-(3-hydroxypropyl)cyclohexanol)] on behaviour, energy metabolism and biotransformation. Single intraperitoneal administration to male Sprague-Dawley rats of CP-55,940 (0.4 mg/kg), induced a behavioural response characterized by 'splayed hind limbs', antinociception, hypothermia and a decrease in locomotor activity. Brain and liver mitochondria of the CP-55,940-treated rats exhibited an increase in respiration and no changes in ADP/O and citrate synthase specific activity. Repeated intraperitoneal administration of CP-55,940 (0.4 mg/kg, 11 days) induced behavioural tolerance, disappearance of the increase in the mitochondrial oxygen consumption as well as an increase in the monooxygenase activities and the content of liver microsomal cytochrome P450. Some hepatic metabolizing enzymes of the cytosolic glutathione-centre system were also affected. Previous studies had indicated that the tolerance after chronic administration of CP-55,940 could be due to down-regulation of brain cannabinoid receptors. The present findings demonstrate that the behavioural tolerance occurs together with modified biotransformation activities.
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PMID:Chronic cannabinoid, CP-55,940, administration alters biotransformation in the rat. 890 24

1. To examine metabolic correlates of insulin resistance in skeletal muscle, we used 31P magnetic resonance spectroscopy to study glycogenolytic and oxidative ATP synthesis in leg muscle of lean and obese Zucker rats in vivo during 6 min sciatic nerve stimulation at 2 Hz. 2. The water content of resting muscle was reduced by 21 +/- 7% in obese (insulin-resistant) animals compared with lean animals, whereas the lipid content was increased by 140 +/- 70%. These results suggest that intracellular water content was reduced by 17% in obese animals. 3. During exercise, although twitch tensions were not significantly different in the two groups, rates of total ATP synthesis (expressed per litre of intracellular water) were 48 +/- 20% higher in obese animals, suggesting a 50 +/- 8% reduction in intrinsic "metabolic efficiency'. Changes in phosphocreatine and ADP concentration were significantly greater in obese animals than in lean animals, whereas changes in intracellular pH did not differ. 4. These results imply that oxidative ATP synthesis during exercise is activated earlier in obese animals than in lean animals. This difference was not fully accounted for by the greater increase in the concentration of the mitochondrial activating signal ADP. Neither the post-exercise recovery kinetics of phosphocreatine nor the muscle content of the mitochondrial marker enzyme citrate synthase was significantly different in the two groups. The increased oxidative ATP synthesis in exercise must therefore be due to altered kinetics of mitochondrial activation by signals other than ADP. 5. Thus, the insulin-resistant muscle of obese animals may compensate for its decreased efficiency (and consequent increased need for ATP) by increased reliance on oxidative ATP synthesis.
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PMID:Increased oxidative and delayed glycogenolytic ATP synthesis in exercising skeletal muscle of obese (insulin-resistant) Zucker rats. 897 4

Citrate synthase (EC 4.1.3.7) was purified from the acidophilic bacterium Acetobacter europaeus to electrophoretic homogeneity. The specific activity was 228 units/mg of protein during the exponential ethanol-oxidation growth phase. The enzyme has a molecular mass of 280 kDa and is a hexamer with a subunit size of 46 kDa. The apparent K(m) values were 20 microM for oxaloacetate and 51 microM for acetyl-CoA. Unlike citrate synthase from other Gram-negative bacteria, the activity of the enzyme was inhibited by ATP, slightly enhanced by ADP and not effected by NADH. Acetate caused activation of the enzyme. The pH optimum on the citrate synthase activity in vitro was 8.1. The amino-terminal amino acid sequence of the purified enzyme was ENGKSATISLNGKDVALPVL.
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PMID:Purification and properties of citrate synthase from Acetobacter europaeus. 899 6

Citrate synthase (citrate oxaloacetate-lyase, CoA-acetylating; EC 4.1.3.7, CS) was isolated and purified to homogeneity from a methylotrophic producer of polyhydroxybutyrate (PHB), Methylobacterium extorquens 15. The purification procedure includes streptomycin sulfate treatment of cell-free extract, ammonium sulfate fractionation, two steps of hydrophobic chromatography, and ion-exchange chromatography. The specific activity of the final enzyme preparation was 24 U/mg protein. The enzyme has apparent molecular weight 260 kD and consists of four 66-kD subunits. The enzyme shows a sigmoid saturation curve with CoASA (h = 1.3). Kinetic parameters are: K(m) = 84 microM for CoASA; K(m) = 12 microM for oxaloacetate; Vmax = 29.7 mumoles/min per mg protein. KCl at concentrations up to 80 mM activates the CS. ATP exerts a significant inhibitory effect on the enzyme activity, whereas NAD(P)H, isocitrate, alpha-ketoglutarate, ADP, acetoacetyl-CoA, glyoxylate, and glutamate have no influence. A possible role of the CS in coordinated control of CoASA transformation through the tricarboxylic acid cycle and PHB biosynthesis in this methylotroph is discussed.
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PMID:Purification and characterization of citrate synthase from Methylobacterium extorquens--a methylotrophic producer of polyhydroxybutyrate. 911 33

The influence of muscle oxidative capacity on phosphocreatine (PCr) changes during and after stimulation was examined in the superficial (fast-twitch) section of rat gastrocnemius muscles. Muscle mitochondrial enzymes were increased in one group of rats by 8-10 wk of training on a running wheel (to a final regimen of 50 min/day at 38 m/min, 5 days/wk) and decreased in another group by chemical thyroidectomy [0.025% methimazole (MMI) in drinking water for 8 wk]. After these treatments, muscle citrate synthase activity was 179 and 29%, respectively, of that in corresponding control groups. Muscle PCr and pH were measured by 31P-nuclear magnetic resonance spectroscopy before, during, and after 8 min of isometric twitch stimulation at 0.33 Hz (MMI) or 0.75 Hz (trained) and 2 Hz. There was a significant linear correlation (r = 0.84, P < 0.01) between the rate constant for PCr recovery after submaximal stimulation (0.33 or 0.75 Hz) and citrate synthase activity. Within the control groups, there was a significant correlation (r = 0.72, P < 0.01) between the rate constant for PCr recovery and intracellular pH at the end of stimulation. The results are quantitatively consistent with linear/quasilinear models of respiratory control by the cytoplasmic free energy of ATP hydrolysis but not with respiratory control by cytoplasmic ADP.
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PMID:Linear dependence of muscle phosphocreatine kinetics on oxidative capacity. 912 93

Bladder outlet obstruction induces severe changes in urinary bladder function and metabolism. These changes are characterized by significant reductions in the ability of the in vitro whole bladder to generate pressure and to empty. Metabolically, partial outlet obstruction induces a shift from oxidative to anaerobic metabolism. The decreased oxidative metabolism is mediated in part by significant decreases in mitochondrial substrate metabolism, which in turn is correlated with decreased activity of 2 important mitochondrial enzymes: citrate synthase and malate dehydrogenase. The present study was designed to evaluate mitochondrial function by studying the incorporation of 14C-adenine into high-energy phosphates (ATP, AMP, and ADP). Mild partial outlet obstructions were created by surgically placing silk ligatures loosely around the bladder neck. The results of these studies demonstrate that after 60 min incubation in oxygenated medium containing glucose + 1uCi14C-adenine, 1) There was no significant differences in the total AMP, ADP, and ATP concentrations measured in bladders taken from controls, 7- and 14-day obstructed rabbits; 2) there was no effect of obstruction on either the concentration of 14C-AMP in the tissue or in the ratio of hot to cold AMP; and 3) there was a 50% decrease in the concentration of 14C-ADP and a 70% decrease in the concentration of 14C-ATP in the bladder smooth muscle obtained from obstructed tissue (from both 7- and 14-day obstructions) compared to concentration in the control bladder smooth muscle. These results confirm the previous finding that obstruction did not reduce the rate of incorporation of adenine to AMP within the obstructed bladder smooth muscle and extends these studies to identify a significant reduction in the synthesis of both ADP and ATP. These results support the hypothesis that partial outlet obstruction induce a major dysfunction in mitochondrial function, both in the ability to oxidize substrates and in the ability to generate ATP.
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PMID:Effect of partial outlet obstruction on 14C-adenine incorporation in the rabbit urinary bladder. 913 42

Histochemical and biochemical analyses were performed on muscle biopsies obtained after racing from the gluteus muscle of 18 standardbred trotters. Fibre type composition and enzyme activities varied among the horses. The percentage of type IIB fibres showed a positive correlation to the lactate dehydrogenase activity and a negative correlation to the citrate synthase activity. ATP concentrations in whole muscle after racing showed a negative correlation to both lactate and IMP concentrations. Within individual fibres, ATP concentrations varied markedly, with some type II fibres having values as low as 1-5 mmol/kg d.w. and some fibres having values as high as 40-58 mmol/kg d.w., whereas mean ATP concentration for whole muscle was 18.3 +/- 7.7 mmol/kg d.w. Some fibres with low ATP concentrations revealed high IMP concentrations. Blood samples taken after racing showed high values for lactate, ammonia, and uric acid in plasma. Muscle AMP and ADP concentrations after racing were related to the horses placing in a race, with higher concentrations giving a lower placing. The results of this study show that adenine nucleotide breakdown in muscle is of great importance for energy release during racing, and that ATP and IMP concentrations may very markedly among individual fibres. Thus, metabolite analyses on whole muscle must be evaluated with caution, as this only represents a mean value for metabolic responses in different fibres during racing.
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PMID:Metabolic response in skeletal muscle fibres of standardbred trotters after racing. 925 81

Experiments were performed on eight subjects affected by peripheral arterial occlusive disease (PAOD) of the lower limbs. Each patient was submitted to Ecodoppler, angiography and the "Treadmill test". Two bioptic muscle of these patients. A sample was used for the spectrophotometric and spectrophotofluorimetric determinations of: glycogen, pyruvate, lactate, citrate, alpha-ketoglutarate, malate, aspartate, glutamate, AMP, ADP, ATP and creatine phosphate (CP). The other bioptic sample was used to determine the following enzyme activities: hexokinase, phosphofructokinase, pyruvate kinase, lactate dehydrogenase, citrate synthase, succinate dehydrogenase, malate dehydrogenase, total NADH cytochrome c reductase, cytochrome oxidase, aspartate aminotransferase and alanine aminotransferase. Patients showed an increase in lactate dehydrogenase, total NADH cytochrome c reductase and succinate dehydrogenase activities, a decrease in glycogen, ATP and CP concentrations. Telethermographic data showed patient muscle thermic emission quantitatively different from control group. The telethermographic test can be used as an additional diagnostic tool to determine and monitor the efficiency of a muscle undergoing metabolic failure.
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PMID:Instrumental and metabolic evaluation of patients affected by peripheral arterial occlusive disease (PAOD) following surgical revascularization surgery. 928 78

Glucose, the most potent insulin secretagogue, stimulates insulin secretion by aerobic glycolysis, but other secretagogues stimulate insulin release exclusively by mitochondrial metabolism. It is well known that in the intact pancreatic beta-cell, either kind of secretagogue can induce oscillations in metabolism (e.g., glycolysis, ATP/ADP, NAD(P)/NAD(P)H ratios) that occur with a periodicity similar to oscillations in membrane electrical potential and insulin secretion. In this study, pancreatic islet cytosol or mitochondrial fractions were incubated in the presence of physiological concentrations of substrates. Repeated additions of physiological effectors caused oscillations in the activities of the three enzymes studied. Succinate dehydrogenase activity in islet mitochondrial extracts was made to oscillate by adding oxaloacetate (5 micromol/l) to inhibit the enzyme. The enzyme was reactivated by adding acetyl-CoA (3 micromol/l), which combines with oxaloacetate in the citrate synthase reaction and lowers the concentration of oxaloacetate, thus beginning another oscillation. Pyruvate kinase activity was made to oscillate by adding fructose bisphosphate (10 micromol/l). Fructose bisphosphate was degraded to triose phosphates fairly rapidly, and, as it was degraded, there was a parallel decrease in pyruvate kinase activity. The enzyme was reactivated and made to oscillate with subsequent additions of fructose bisphosphate. The mitochondrial glycerol phosphate dehydrogenase was made to oscillate by adding EGTA to chelate calcium, which activates the enzyme. When the concentration of free calcium was raised to >0.1 micromol/l by adding more calcium, the activity of the enzyme increased. Repeated additions of chelator and calcium caused the enzyme activity to oscillate. The results with these three enzymes and physiological concentrations of naturally occurring effectors raise the possibility that the activities of not only these enzymes but of numerous enzymes oscillate in vivo in response to levels of allosteric effectors and substrates. If this is the case, pacemaker activity may result from complex effects distributed across multiple regulatory sites in both the cytosol and mitochondria, rather than from a single enzyme acting as a primary pacemaker.
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PMID:Oscillations in activities of enzymes in pancreatic islet subcellular fractions induced by physiological concentrations of effectors. 939 86


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