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)

Some enzyme activities and metabolic features of the black Ma melanotic, brown MI melanotic and Ab amelanotic melanomas of hamster were investigated. The activities of hexokinase and phosphofructokinase were similar in all three melanomas, the activity of NAD-dependent glycerol-3-phosphate dehydrogenase was higher in the amelanotic melanoma and that of pyruvate kinase and lactate dehydrogenase were slightly lower in MI than in the other tumors. The activities of citrate synthase, succinate dehydrogenase and malate dehydrogenase were higher in the Ma and MI melanotic melanomas than in the Ab amelanotic melanoma. The rate of labeled CO2 production from 6-14C-glucose, 1,5-14C-citric acid and U-14C-glutamine was about 2 times higher in melanotic melanomas than in amelanotic one, while no significant differences among the three melanomas were found in respect to 1-14C-glucose and U-14C-glycerol-3-phosphate. The production of 14CO2 was much higher from 1-14C-glucose than from 6-14C-glucose in all the melanomas studied. L-DOPA stimulated the production of 14CO2 from 1-14C-glucose much stronger in the Ma and MI melanomas than in the Ab melanoma. In none of the tumors the incorporation from 6-14C-glucose to CO2 was affected by L-DOPA. It is postulated that oxidation of glucose via the pentose phosphate cycle is involved in melanogenesis.
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PMID:Metabolic characterization of three hamster melanoma variants. 406 92

Crude extracts of both vegetative cells and glycerol-induced microcysts of Myxococcus xanthus contained the following enzyme activities: phosphofructokinase, phosphoglucoisomerase, fructose-1,6-diphosphatase, fructosediphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate carboxylase, citrate synthase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and uridine diphosphate glucose pyrophosphorylase. With the exception of isocitrate dehydrogenase, which was present at a fivefold higher concentration in microcysts, all activities in extracts from both types of cells were essentially equal. Hexokinase and pyruvate kinase could not be detected in extracts from either type of cell. Microcysts metabolized acetate at a lower rate than did vegetative cells. Most of this decrease was reflected in a substantial decrease in ability of microcysts to oxidize acetate to CO(2). In addition, microcysts and vegetative cells showed a different distribution of (14)C-label from incorporated acetate.
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PMID:Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. 430 96

1. The intracellular location and maximal activities of enzymes involved in phosphoenolpyruvate synthesis have been investigated in pigeon liver. Enolase and pyruvate kinase were cytoplasmic, and the activities were 50-60 and 180-210mumoles/min./g. dry wt. at 25 degrees respectively. Phosphoenolpyruvate carboxykinase was present exclusively, and nucleoside diphosphokinase predominantly, in the mitochondria; the particles had to be disrupted to elicit maximal activities, which were 27-33 and 400-600mumoles/min./g. dry wt. at 25 degrees respectively. The activities of all four enzymes did not change significantly during 48hr. of starvation. 2. Conditions for incubation of washed isolated mitochondria were established, to give high rates of synthesis of phosphoenolpyruvate, linear with time and proportional to mitochondrial concentration. Inorganic phosphate and added adenine nucleotides were stimulatory, whereas added Mg(2+) inhibited, partly owing to activation of contaminant pyruvate kinase. Phosphoenolpyruvate formation occurred from oxaloacetate, malate, fumarate, succinate, alpha-oxoglutarate and citrate, in decreasing order of effectiveness. 3. The steady-state ATP/ADP ratio of mitochondrial suspensions was decreased in the presence of added 2.5mm-Mg(2+) (owing to stimulation of adenylate kinase and possibly of an adenosine triphosphatase), 0.5mm-Ca(2+) or 0.4mm-dinitrophenol. In each case the rate of substrate removal and oxygen uptake was increased, whereas phosphoenolpyruvate synthesis was inhibited. Citrate formation was enhanced, owing to de-inhibition of citrate synthase. These effects were not primarily related to changes in the oxaloacetate concentration. 4. Both phosphoenolpyruvate carboxykinase and nucleoside diphosphokinase were active within the atractylosidesensitive barrier to the mitochondrial metabolism of added adenine nucleotides. There was no correlation between the rate of substrate-level phosphorylation associated with the oxidation of alpha-oxoglutarate, and the synthesis of phosphoenolpyruvate. 5. The results suggest that phosphoenolpyruvate formation in pigeon-liver mitochondria is regulated partly by the phosphorylation state of the adenine and guanine nucleotides, and partly by variations in the oxaloacetate concentration, all in the mitochondrial matrix. 6. Phosphoenolpyruvate is assumed to be the metabolite transported from the mitochondria to the cytoplasm during gluconeogenesis from oxaloacetate in pigeon liver.
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PMID:The regulation of phosphoenolpyruvate synthesis in pigeon liver. 496 63

Pyruvate kinase (EC 2.7.1.40) from Azotobacter vinelandii responds sharply to the adenylate energy charge, with a decrease in activity at high values of charge, as expected for an enzyme of an adenosine triphosphate-regenerating sequence. Glycolytic intermediates, especially glucose 6-phosphate, fructose 6-phosphate, and fructose-1,6-diphosphate, strongly stimulate the reaction and overcome the inhibition caused by high values of energy charge. Thus, the properties of this enzyme depend on interaction between energy charge and the concentrations of hexose phosphates. The properties of pyruvate kinase, together with those of phosphoenolpyruvate carboxylase, aspartokinase, and citrate synthase, seem adapted to provide appropriate partitioning of phosphoenolpyruvate between competing pathways in response to metabolic need.
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PMID:Regulation at the phosphoenolpyruvate branchpoint in Azotobacter vinelandii: pyruvate kinase. 555 41

Burton, Sheril D. (Institute of Marine Science, University of Alaska, College), Richard Y. Morita, and Wayne Miller. Utilization of acetate by Beggiatoa. J. Bacteriol. 91:1192-1200. 1966.-A proposed system which would permit acetate incorporation into four-carbon compounds without the presence of key enzymes of the citric acid cycle or glyoxylate cycle is described. In this system, acetyl-coenzyme A (CoA) is condensed with glyoxylate to form malate, which, in turn, is converted to oxaloacetate. Oxaloacetate then reacts with glutamate to produce alpha-ketoglutarate, which is subsequently converted to isocitrate. Cleavage of isocitrate produces glyoxylate and succinate. Thus, the proposed system is similar to the glyoxylate bypass in that malate is produced from glyoxylate and acetyl-CoA, but differs from both the citric acid cycle and the glyoxylate bypass, since citrate and fumarate are not involved. Fumarase, aconitase, catalase, citritase, pyruvate kinase, enolase, phosphoenolpyruvate carboxylase, lactic dehydrogenase, alpha-ketoglutarate dehydrogenase, and condensing enzyme were not detectable in crude extracts of Beggiatoa. Succinate was oxidized by a soluble enzyme not associated with an electron-transport particle. Isocitrate was identified as the sole compound labeled when C(14)O(2) was added to a reduced nicotinamide adenine dinucleotide, CO(2) generating system (crystalline glucose-6-phosphate dehydrogenase and glucose-6-phosphate) in the presence of alpha-ketoglutarate.
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PMID:Utilization of acetate by Beggiatoa. 592 51

Cells of the aerotolerant anaerobe Giardia lamblia respire in the presence of oxygen. Endogenous respiration is stimulated by glucose but not by other carbohydrates and Krebs cycle intermediates. Endogenous and glucose-stimulated respiration are insensitive to cyanide, malonate, and 2,4-dinitrophenol, but are inhibited by atabrin and iodoacetamide. G. lamblia produces ethanol, acetate and CO2 both aerobically and anaerobically either from endogenous reserves or exogenous glucose. Molecular hydrogen is not produced. The following enzyme activities were detected in homogenates: hexokinase, fructose-biphosphate aldolase, pyruvate kinase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, malate dehydrogenase (decarboxylating), pyruvate synthase, acetyl-CoA synthetase, alcohol dehydrogenase (NADP+), NADH dehydrogenase, NADPH dehydrogenase, NADPH oxidoreductase and superoxide dismutase. The enzymes of energy and carbohydrate metabolism are nonsedimentable (109 000 x g for 30 min). Activities of lactate dehydrogenase, hydrogenase, phosphate acetyltransferase, acetate kinase, citrate synthase, succinate dehydrogenase, fumarate hydratase and catalase were below the limits of detection. The results suggest the occurrence of glycolysis, energy production by substrate level phosphorylation and a flavin, iron-sulfur protein mediated electron transport system as well as the absence of cytochrome mediated oxidative phosphorylation and functional Krebs cycle.
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PMID:Energy metabolism of the anaerobic protozoon Giardia lamblia. 610 7

The present study compares the time courses of the early changes in parvalbumin content, in the properties of the sarcoplasmic reticulum (SR) and in activity and isozyme patterns of metabolic enzymes in chronically (12 h/day) stimulated fast twitch tibialis anterior (TA) muscle of the rabbit. Under the chosen conditions of stimulation, the first significant changes appeared after 6 days. Except for the delayed reduction in pyruvate kinase, the time course of the changes were the same. After 14 days of stimulation, parvalbumin decreased to 37% and Ca2+-ATPase activity of the SR to 29% of normal values. The transformation of the SR was also reflected by a 64% decrease of the 115000-Mr Ca2+-pumping peptide and a 5-fold increase in a 30000-Mr peptide. Following an identical time course, the mitochondrial activities of citrate synthase, 3-hydroxyacyl-CoA dehydrogenase and ketoacid-CoA transferase increased 2.9, 3.0 and 3.7-fold respectively. A similar time course was observed in the M to H-type transition of the lactate dehydrogenase isozymes. The cause of these changes is discussed as it relates to altered transcriptional and/or translational activities. It is suggested that an increase in free intracellular Ca2+ caused by increased contractile activity, which is then perpetuated by the decrease in Ca2+-binding and sequestering capacities, might be the signal for such altered synthetic activities.
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PMID:Relationships between early alterations in parvalbumins, sarcoplasmic reticulum and metabolic enzymes in chronically stimulated fast twitch muscle. 622 11

Three measures of locomotory performance and a series of variables thought to affect performance were measured in the iguanid lizard Ctenosaura similis. Burst speed is mass independent; however, endurance time at 1 km/h (EN-DUR) and maximal distance run (MAX DIS) scale as M0.3. Standard and maximal rates of O2 consumption (VO2max) scale as M0.9; VO2max averages 10-fold greater than standard metabolic rate (SMR). Three of ten enzyme activities measured exhibit significant scaling. After statistically removing the effects of body mass, multiple-regression analysis indicates that 1) 89% of the residual variation in ENDUR is correlated with variation among individuals in thigh muscle mass, VO2max, heart mass, and liver citrate synthase (CS) activity; 2) maximal CO2 consumption (VCO2max) and thigh pyruvate kinase activity statistically explain 64% of the variation in MAX DIS; 3) heart and liver masses together predict 35% of the variation in SMR; 4) thigh and liver CS activity, heart lactate dehydrogenase (LDH) activity, and hematocrit account for 67% of the variation in VO2max;5) 97% of the variation in VCO2max is statistically related to variation in liver CS activity, thigh and heart masses, and heart LDH activity.
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PMID:Physiological correlates of locomotory performance in a lizard: an allometric approach. 623 43

Long-term electrical stimulation (14-28 days) of rabbit fast muscles (tibialis anterior, TA and extensor digitorum longus, EDL) using intermittent high frequency (3 trains per min of 5 s duration at 40 Hz, for 8 h per day) produced changes in enzyme activities similar to those found with continuous stimulation at a frequency occurring in nerves to slow muscles (10 Hz). The activity of citrate synthetase, 3-hydroxyacyl-CoA dehydrogenase and succinate dehydrogenase increased two to 3-fold within 28 days. There was a 4-fold increase in hexokinase whereas phosphofructokinase, pyruvate kinase, lactate dehydrogenase and fructose-1,6-diphosphatase decreased to about 60% of the activity levels in the contralateral unstimulated muscles. Blood flow and oxygen consumption at rest were not changed even after 28 days of stimulation, but were increased during contractions in muscles stimulated at either frequency, the level being twice as high as in control muscles. Glucose uptake was similar to that in control muscles both at rest and during contractions and the output of lactate was similar to that found in control muscles in muscles stimulated at 40 Hz. Muscles stimulated at 10 Hz had smaller lactate output. Thus intermittent stimulation at high frequency (40 Hz) and continuous low frequency (10 Hz) produced similar changes in aerobic metabolism and fuel uptake provided that the total number of stimuli was comparable and that the stimulation was carried out for sufficiently long period.
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PMID:Effects of different patterns of long-term stimulation on blood flow, fuel uptake and enzyme activities in rabbit fast skeletal muscles. 652 41

It is commonly observed that during acclimatization to altitude oxidative enzyme activities increase per g wet weight of tissue. To examine this problem in long-term adapted animals we measured citrate synthase (CS), hydroxyacylCoA dehydrogenase (HOAD), pyruvate kinase (PK), and lactate dehydrogenase (LDH) activities/g of myocardium in two domestic species (llama and alpaca) and a high altitude deer, the taruca. In all these species, we found an upward scaling of oxidative capacity (indicated by absolute activities of CS and HOAD) but a downward scaling of anaerobic/aerobic metabolic potentials of the heart (indicated by low ratios of LDH/CS, and LDH/HOAD, but high ratios of PK/LDH). As the direction and magnitude of these long-term adaptations are the same as in shorter-term acclimatizations, we wondered why a similar pattern at the enzyme level correlates with the right shift of the O2 dissociation curve (ODC) in the latter case, but with a left shifted ODC in the former. We hypothesize that in the long term, increased oxidative enzyme activities allow increased maximum flux capacity of aerobic metabolism. This in turn calls for physiological adjustments in O2 transfer systems; flux limits of the former must be matched by flux limits of the latter. Only then can an acceptably high scope for aerobic activity be achieved despite reduced O2 availability in inspired air. Such long-term match-up invariably calls for a left-shifted ODC plus other well known adjustments in O2 transport. In the short term, right shifting the ODC may increase the total amount of aerobic work possible (by favoring O2 unloading and thus raising tissue O2 concentration), yet maximum flux capacity cannot be changed much because mitochondrial metabolism is designed for maintaining stable rates of ATP synthesis even at widely varying O2 tensions. That is why even in short-term acclimatization, in order to increase flux capacity, the activities of oxidative enzymes also must be increased.
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PMID:Metabolic meaning of elevated levels of oxidative enzymes in high altitude adapted animals: an interpretive hypothesis. 661 4


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