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)

The effect of high-intensity trained (6 X 4.5 min at 40 m/min, 15% grade, 2.5-min rest between bouts, 5 days/wk, for 6 wk) on contractile, biochemical, and fatigue properties of the rat diaphragm were examined. The exercise program produced significant elevations in the mitochondrial marker enzyme citrate synthase (mumol X g-1 X min-1) in the soleus (SOL) (27.2 +/- 1.5 vs. 46.7 +/- 2.4; mean +/- SE), deep vastus lateralis (DVL) (40.8 +/- 2.6 vs. 58.3 +/- 2.8), and superficial vastus lateralis (SVL) (8.5 +/- 0.6 vs. 11.4 +/- 0.7). No significant differences were observed in the crural (CRU) (45.9 +/- 2.0 vs. 44.0 +/- 2.3) or ventral costal (VEN) (41.5 +/- 2.0 vs. 45.8 +/- 2.6) diaphragmatic regions. Phosphofructokinase, the rate-limiting enzyme of glycolysis, significantly increased in the SOL (19.0 +/- 0.8 vs. 23.3 +/- 1.3 mumol X g-1 X min-1) and DVL (69.3 +/- 6.0 vs. 86.6 +/- 5.0), but no alterations were seen in the SVL (98.6 +/- 5.7 vs. 106.1 +/- 9.0), CRU (54.4 +/- 2.8 vs. 53.8 +/- 1.5), or VEN (44.7 +/- 2.4 vs. 46.4 +/- 1.4) posttraining. Diaphragm contractile properties, with the exception of an increased rate of fall in twitch tension, remained unchanged after training. Glycogen values were significantly higher in trained diaphragms at rest (6.54 +/- 0.39 vs. 4.86 +/- 0.41 mg/g) and during 1, 5, and 10 min of fatiguing stimulation. During fatigue no differences were observed in force, rate of rise in force, rate of fall in force, muscle lactate, ATP, or creatine phosphate in trained vs. control.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Contractile and biochemical properties of diaphragm: effects of exercise training and fatigue. 294 Feb 18

Concentrations of high-energy phosphates and activities of key enzymes of energy metabolism were assessed in hearts from species with differing levels of cardiac power output. Positive correlations were found between resting power output and the total adenylate pool and between citrate synthase activity and the total adenylate pool. Maximum in vitro activity levels of enzymes from energy metabolism were compared with calculated resting cardiac power output and maximal cardiac power output (as reflected by total oligomycin-insensitive adenosine-triphosphatase activity). Three indexes of carbohydrate metabolism (hexokinase, pyruvate kinase, and L-lactate dehydrogenase) all plateau at relatively low levels of energy demand. In contrast, enzymes required for aerobic fatty acid metabolism, (carnitine palmitoyltransferase and 3-hydroxyacyl-CoA dehydrogenase) and for tricarboxylic acid and electron transport (citrate synthase and cytochrome-c oxidase) show consistent increases as ATP demand is elevated. It appears that as capacity for power development by vertebrate hearts, increases across taxa, the elevated demand for ATP is met by expansion of fatty acid based aerobic metabolism and not carbohydrate metabolism.
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PMID:Matching of vertebrate cardiac energy demand to energy metabolism. 295 61

The muscle enzymatic changes subsequent to 6 months of strength training followed by 3 months of detraining were examined in 21 physically active men. They were assigned either to a heavy-resistance (HR) or an explosive strength (EX) training program. Muscle biopsies were obtained from m. vastus lateralis for the assessment of activities of the enzymes hexokinase (HK), myofibrillar ATPase (ATPase), citrate synthase (CS), phosphofructokinase (PFK), lactate dehydrogenase (LDH), myokinase (MK) and creatine kinase (CK). The activities were measured on freeze-dried tissue samples using fluorometrical assays. Both groups displayed increased (P less than 0.01-0.001) fast-twitch (FT) fiber area consequent to training with no concomitant hypertrophy of slow-twitch (ST) fiber area. Mean fiber area increased by 16% (P less than 0.001) in HR and 9% (NS) in EX. Following detraining, mean fiber area returned to pretraining value only in EX. HK decreased in both groups (P less than 0.01-0.001) and CK decreased in HR (P less than 0.05). When the two groups were treated together, all enzymes, except for LDH, decreased their activity (P less than 0.05-0.001). It is concluded that 6 months of strength training performed either as heavy-resistance or explosive training is not associated with any increased activities of enzymes reflecting phosphagen, glycolytic, or oxidative metabolism. Instead, the present results suggest that exercise-induced hypertrophy is accompanied by attenuation of certain enzyme activities of importance for ATP regeneration.
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PMID:Enzymatic adaptations consequent to long-term strength training. 295 91

The adaptation of enzyme activities, notably in the oxidative metabolism, and of prerequisites for tissue transport of oxygen in the claudication leg was evaluated by comparing muscle biopsies from the gastrocnemius muscle of the claudication and the symptom-free leg of seven patients with unilateral claudication. The claudication leg had higher activities of a marker enzyme for mitochondrial oxidative capacity, citrate synthase (CS), as well as of the MB and the mitochondrial isoenzyme of creatine kinase (CK), which are considered to be involved in the transfer of high energy phosphate from the mitochondria to the resynthesis of ATP in the cytoplasm. The difference between claudication and healthy leg in activities of these CK isoenzymes were well correlated with the corresponding side difference in CS activity. No significant differences between claudication and healthy leg were found in distribution of muscle fibre types or fibre dimension, capillary density or myoglobin content, nor was there any side difference in phosphofructokinase or lactate dehydrogenase. Side differences tended to be greater in those patients with the most advanced obstructive arterial disease as estimated from non-invasive pressure measurements. It is concluded that in reasonably physically-active patients, the mode of ischaemia to which the claudication leg is subjected leads to a metabolic adaptation characterized by increased activities of enzymes involved in the oxidative metabolism, but no significant adaptation of either the conditions for local oxygen transport, as estimated by myoglobin content, and capillary density, or capacity for anaerobic metabolism.
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PMID:Calf muscle adaptation in intermittent claudication. Side-differences in muscle metabolic characteristics in patients with unilateral arterial disease. 296 71

The purified carbon monoxide dehydrogenase from Clostridium thermoaceticum is the only protein required to catalyze an exchange reaction between carbon monoxide and the carbonyl group of acetyl-CoA. This exchange requires that the CO dehydrogenase bind the methyl, the carbonyl, and the CoA groups of acetyl-CoA, then equilibrate the carbonyl with CO in the solution and re-form acetyl-CoA. CoA is not necessary for the exchange and, in fact, inhibits the reaction. These studies support the view that CO dehydrogenase is the condensing enzyme that forms acetyl-CoA from its component parts. Carbon dioxide also exchanges with the C-1 of acetyl-CoA, but at a much lower rate than does CO. At 50 degrees C and pH 5.3, the optimal pH, the turnover number is 70 mol of CO exchanged per min/mol of enzyme. Low potential electron carriers are stimulatory. The Km app for stimulation by ferredoxin is 50-fold less than the value for flavodoxin. Neither ATP or Pi stimulate the exchange. The EPR spectrum of the CO-reacted enzyme is markedly changed by binding of CoA or acetyl-CoA. Arginine residues of the CO dehydrogenase appear to be involved in the active site, possibly by binding acetyl-CoA. Mersalyl acid, methyl iodide, 5,5-dithiobis-(2-nitrobenzoate), and sodium dithionite inhibit the exchange reaction. A scheme is presented to account for the role of CO dehydrogenase in the exchange reaction and in the synthesis of acetate.
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PMID:Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. 298 90

A rat model was developed in which the adaptive effects of exposing skeletal muscle tissue to a reduced blood flow during muscle contractions could be studied. The common iliac artery was ligated in one hindlimb, using the other as control. This procedure reduced the exercise blood flow to the individual muscles of the lower limb by 76-93%, evaluated with the microsphere technique. Muscle contractions were induced by electrical stimulation of the sciatic nerves in both legs. After intermittent stimulation for 6 days, a significant increase in citrate synthase and cytochrome c oxidase activities was found in the soleus (26%) and extensor digitorum longus (EDL, 20%) muscles of the ligated legs compared with the control legs. Resting metabolite concentrations were also measured, and a reduction of the ATP level (soleus 35%, EDL 14%) and an increased glycogen content (55-71%) were found. These results demonstrate that a reduced blood flow during muscle contractions provokes an adaptive increase of the oxidative enzyme capacity as well as altered resting levels of intracellular metabolites.
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PMID:Metabolic adaptation to reduced muscle blood flow. I. Enzyme and metabolite alterations. 299 Feb 34

The ultrastructure of skeletal muscle and activity of some enzymes of energy metabolism were studied to assess the effect of a deficiency of dietary energy and subsequent nutritional rehabilitation in 24 young, growing, healthy rhesus monkeys. Electron microscopy of muscles on energy-deficient animals showed thinning of myofibrils with widening of interfibrillar space and enlargement and accumulation of mitochondria at subsarcolemmal level. There was an apparent significant reduction in the fiber size. Muscle samples from each animal were analyzed for enzymes representative of glycolysis (phosphofructokinase [PFK] and lactate dehydrogenase [LDH], citric-acid cycle (isocitric dehydrogenase [ICDH] and citrate synthase [CS] and regeneration of ATP (creatine kinase [CK]. PFK and LDH activities were significantly augmented in energy-deficient animals. The increase in LDH activity resulted from a large increase in MU (skeletal muscle) LDH subunit. The activities of CS and ICDH were reduced. No alteration of CK in muscle and serum was observed. The morphological structure and enzyme activities returned to normal after nutritional rehabilitation.
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PMID:Ultrastructure and activity of some enzymes of energy metabolism of skeletal muscle in experimental energy deficiency. 310 25

The citrate synthase gene from the obligate intracellular rickettsial parasite Coxiella burnetii was cloned and expressed in Escherichia coli. Transduction into E. coli with a C. burnetii gene library constructed in the cosmid vector pHK17 resulted in the functional complementation of the gltA mutation of E. coli MOB154. A GltA+ clone carrying 16.4 kilobase pairs of C. burnetii DNA and designated pJCC959 was isolated and characterized. Southern hybridization analysis confirmed that the pJCC959 cloned insert consists of C. burnetii DNA and that homology exists with the Rickettsia prowazekii citrate synthase gene. Subcloning analysis with the multicopy expression vector pUC8 revealed that citrate synthase expression was under control of a C. burnetti promoter. In vitro transcription-translation of subclones pLPM20 and pLPM30 established a molecular weight of ca. 46,000 for the monomer form of the cloned enzyme. Transposon Tn5 mutagenesis of pLPM30 defined the coding region to approximately 1.2 kilobase pairs of C. burnetii DNA. Maxicell analysis of selected pLPM30::Tn5 insertion derivatives identified the direction of transcription and the relative translational start and stop sites and substantiated the molecular weight value calculated from the in vitro analysis. Inhibition studies showed that citrate synthase activity in crude cell extracts obtained from strain MOB154 transformed with the cloned C. burnetii gene was markedly inhibited by 4 mM ATP, while 4 mM alpha-ketoglutarate had virtually no effect. These data indicate that the C. burnetii enzyme displays regulatory behavior characteristic of the small gram-positive bacterial and eucaryotic enzyme.
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PMID:Cloning and functional expression of the Coxiella burnetii citrate synthase gene in Escherichia coli. 310 7

The effect of hypoxia and post-hypoxic recovery were studied in gastrocnemius muscle of young-adult and mature beagle dogs. Furthermore, the possible interference of pharmacological treatment with nicergoline was evaluated in these conditions. Muscular glycolytic fuels, intermediates and end-products (glycogen, glucose, glucose 6-phosphate, pyruvate, lactate), Kreb's cycle intermediates (citrate, alpha-ketoglutarate, succinate, malate) and related free amino acids (glutamate, alanine), ammonium ion, energy store and mediators (ATP, ADP, AMP and creatine phosphate), and the energy charge potential were evaluated. Furthermore, in the crude extract and/or mitochondrial fraction of another portion of the same gastrocnemius muscle the maximum rate (Vmax) of some muscular enzymes related to the anaerobic glycolytic pathway (hexokinase, lactate dehydrogenase), the Kreb's cycle (citrate synthase, malate dehydrogenase), the aminoacid pool related to the Krebs' cycle (glutamate dehydrogenase and aspartate aminotransferase), the electron transfer chain (cytochrome oxidase) and NAD+/NADH exchanges (total NADH cytochrome c reductase) was evaluated. Some glycolytic metabolites and Krebs' cycle intermediates were modified by acute hypoxia, while free amino acids and energy mediators remained practically unchanged. The pharmacological treatment maintained the glucose and succinate muscular concentrations within the normal range, during hypoxia. The behaviour of muscular metabolites during hypoxia and/or post-hypoxic recovery is an age-related event. In fact, only in young-adult animals did the altered values return to normal in post-hypoxic recovery. In the present experimental conditions, only minor changes were observed as far as muscular enzyme activities are concerned. In any case, some enzyme activities tested showed different Vmax in young-adult dogs in comparison with mature ones.
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PMID:Effect of hypoxia, aging and pharmacological treatment on muscular metabolites and enzyme activities. 322 9

Mitochondrial (mt) biogenesis and mt function were investigated during the cell cycle of leukemic cells. The study shows that the activity of enzymes involved in oxidative phosphorylation increases in the early G1 phase. This increase in activity precedes that of other mt enzymes such as citrate synthase and adenylate kinase. Therefore, the synthesis of mt enzymes, needed for the reduplication of the mt mass in the course of the cell cycle, occurs in a sequential order. The enzymes of the system for oxidative phosphorylation are composed of several subunits. Some of these subunits are encoded on mtDNA and synthesized by mt-specific RNA and protein synthesis. This explains why inhibition of mt protein synthesis during the progression of the cell cycle of G1-enriched cells results in an increasing shortage of ATP. This lack of ATP results first in progression delay and, subsequently, in a cell cycle block in early G1. Furthermore, shortage of ATP impairs the increase in activity of at least one mt matrix enzyme. This study offers new information about a number of aspects of mt biogenesis and mt function during cell cycle progression and elucidates the cytostatic mechanism resulting from prolonged inhibition of mt protein synthesis.
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PMID:Mitochondrial biogenesis and mitochondrial activity during the progression of the cell cycle of human leukemic cells. 340 75


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