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Query: EC:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A transcript analysis of the citrate synthase and succinate dehydrogenase genes (gltA-sdhCDAB) of Escherichia coli was done by nuclease S1 mapping. Evidence was obtained for two monocistronic gltA transcripts extending anti-clockwise, to a common terminus, from independent promoters with start points 196 bp (major) and 299 bp (minor) upstream of the gltA coding region. Evidence was also obtained for two polycistronic sdh transcripts, sdhCDAB (minor) and sdhDAB (major), extending clockwise, from sites 219 bp upstream of sdhC and 1455 bp upstream of sdhD (i.e. within sdhC), to a common terminus. The synthesis of all of the transcripts was repressed by growth in the presence of glucose, and this is consistent with the well-established fact that both enzymes are subject to catabolite repression. Sequences resembling known binding sites for the cAMP-CRP (cyclic AMP-cyclicAMP receptor protein) complex occur in the vicinity of each promoter suggesting that they are activated by the cAMP-CRP complex.
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PMID:Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12. 330 32

We studied energy metabolism after experimental subarachnoid hemorrhage in rats. Four different cerebral areas were tested: frontal cortex, occipital cortex, hippocampus, and brainstem. Vmax of the following enzymatic activities was evaluated: in the homogenate: hexokinase, phosphofructokinase, and lactate dehydrogenase for the glycolytic pathway, and glucose-6-phosphate dehydrogenase for the hexose monophosphate shunt; in the purified nonsynaptic mitochondria: NAD+-isocitrate dehydrogenase, citrate synthase, and succinate dehydrogenase for the Krebs cycle, and cytochrome oxidase for the electron transfer chain. We also evaluated some parameters related to the respiration of nonsynaptic mitochondria (State 3, State 4, uncoupled state, respiratory control ratio, and ADP:O ratio). Subarachnoid hemorrhage did not significantly affect Vmax of the enzymatic activities related to anaerobic and aerobic metabolism; however, mitochondrial respiration was affected, particularly in the presence of NADH-producing substrates (glutamate + malate).
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PMID:Bioenergetics of different brain areas after experimental subarachnoid hemorrhage in rats. 335 25

Aerobic and anaerobic thresholds determined by different methods in repeated exercise tests were correlated with cardiorespiratory variables and variables of muscle metabolic profile in 33 men aged 20-50 years. Aerobic threshold was determined from blood lactate, ventilation, and respiratory gas exchange by two methods (AerT1 and AerT2) and anaerobic threshold from venous lactate (AnTLa), from ventilation and gas exchange (AnTr) and by using the criterion of 4 mmol.1(-1) of venous lactate (AnT4mmol). In addition to ordinary correlative analyses, applications of LISREL models were used. The 8 explanatory variables chosen for the regression analyses were height, relative heart volume, relative diffusing capacity of the lung, muscle fiber composition, citrate synthase (CS) and succinate dehydrogenase activities, the lactate dehydrogenase--CS ratio, and age. They explained 58% of the variation in AerT1, 73.5% that of AerT2, 71% that of AnTr, 74.5% that of AnTLa, and 67.5% that of AnT4mmol.AerT and AnT alone explained 77% of the variation in each other. Both AerT and AnT were determined mainly by a muscle metabolic profile, with the CS activity of vastus lateralis as the strongest determinant. The factor 'submaximal endurance' which was measured with AerT and AnT seemed to be slightly more closely connected to 'muscle metabolic profile' than was 'maximal aerobic power' (= VO2max), but both also correlated strongly with each other (r = 0.92).
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PMID:Muscle metabolic profile and oxygen transport capacity as determinants of aerobic and anaerobic thresholds. 341 58

The genes encoding both subunits of the succinyl-CoA synthetase of Escherichia coli have been identified as distal genes of the suc operon, which also encodes the dehydrogenase (Elo; sucA) and succinyltransferase (E2o; sucB) components of the 2-oxoglutarate dehydrogenase complex. The newly defined genes express polypeptides of 41 kDa (sucC) and 31 kDa (sucD), corresponding to the beta and alpha subunits of succinyl-CoA synthetase, respectively. The genes are thus located at 16.8 min in the E. coli linkage map, together with the citrate synthase (gltA) and succinate dehydrogenase (sdh) genes, in a cluster of nine citric acid cycle genes: gltA-sdhCDAB-sucABCD. Four deletion strains lacking all of these citric acid cycle enzymes were characterized. The succinyl-CoA synthetase activities of strains harbouring plasmids containing the sucC and sucD genes were amplified some fourfold. Further enzymological studies indicated that expression of succinyl-CoA synthetase is coordinately regulated with 2-oxoglutarate dehydrogenase.
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PMID:Cloning and expression of the succinyl-CoA synthetase genes of Escherichia coli K12. 354 12

The effect of severe protein deprivation and subsequent nutritional rehabilitation on the fibre size and mitochondrial enzyme activity of the extensor digitorum longus (EDL) and soleus muscles of the young rat has been examined. Protein deprived rats showed atrophy of type 2 fibres predominantly, reduced histochemical activity of succinic dehydrogenase (SDH) and reduced biochemical activity of citrate synthase. Nutritional rehabilitation indicated by resumption of the original body weight resulted in complete restitution of the weight of the muscles and the size of type 1 and type 2 fibres, but not of the activity of SDH and citrate synthase. The results indicate that regarding size, type 2 fibres tend to be more influenced than type 1 fibres by the nutritional supply. The mitochondrial enzyme activity which is decreased by protein deprivation does not regain the normal levels as quickly as the muscle fibres resume their normal size.
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PMID:Nutritional rehabilitation of skeletal muscle in protein-deprived young rats. 376 Sep 9

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

A technique was developed for the detection, on agar, of mutants of Bacillus subtilis that lacked a functional tricarboxylic acid cycle. Mutants devoid of detectable levels of aconitase, isocitric dehydrogenase, alpha-ketoglutarate dehydrogenase, succinic dehydrogenase, fumarase, and malate dehydrogenase have been isolated and characterized. Several mutants with conditionally expressible lesions, including a mutant with a heat-sensitive citrate synthase, have also been isolated. All of the mutants examined express all the biochemical markers normally absent in early-stage sporulation mutants except elastase, and some of these mutants sporulated nearly as well as the prototroph.
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PMID:Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. 499 41

The growth response of Listeria monocytogenes strains A4413 and 9037-7 to carbohydrates was determined in a defined medium. Neither pyruvate, acetate, citrate, isocitrate, alpha-ketoglutarate, succinate, fumarate, nor malate supported growth. Furthermore, inclusion of any of these carbohydrates in the growth medium with glucose did not increase the growth of Listeria over that observed on glucose alone. Resting cell suspensions of strain A4413 oxidized pyruvate but not acetate, citrate, isocitrate, alpha-ketoglutarate, succinate, fumarate, or malate. Cell-free extracts of strain A4413 contained active citrate synthase, aconitate hydratase, isocitrate dehydrogenase, malate dehydrogenase, fumarate hydratase, fumarate reductase, pyruvate dehydrogenase system, and oxidases for reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate. The alpha-ketoglutarate oxidation system, succinate dehydrogenase, isocitrate lyase, and malate synthase were not detected. Cytochromes were not detected. The data suggest that strain A4413, under these conditions, utilizes a split noncyclic citrate pathway which has an oxidative portion (citrate synthase, aconitate hydratase, and isocitrate dehydrogenase) and a reductive portion (malate dehydrogenase, fumarate hydratase, and fumarate reductase). This pathway is probably important in biosynthesis but not for a net gain in energy.
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PMID:Citrate cycle and related metabolism of Listeria monocytogenes. 499 14

The activities of the eight citric acid-cycle enzymes of rat bone-marrow cells were determined along with several other mitochondrial and non-mitochondrial enzymes. Four of the citric acid-cycle enzymes (aconitase, succinyl-CoA thiokinase, alpha-oxoglutarate dehydrogenase and succinate dehydrogenase) have closely similar low activities; two [isocitrate dehydrogenase (NAD) and citrate synthase] have intermediate activities; the remaining two (malate dehydrogenase and fumarase) have high activities. The other enzymes surveyed also exhibited a spread of three orders of magnitude, the mitochondrial enzymes showing no less variation than the others.
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PMID:The activities of the citric acid-cycle enzymes in rat bone-marrow cells. 566 55


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