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

The isolation is described of pure cultures of three non-methane-utilizing methylotrophic bacteria which, together with the previously described Bacillus PM6, have a very limited range of growth substrates; these organisms are designated "restricted facultative' methylotrophs. Two of these isolates, W6A and W3A1, grow only on glucose out of 50 non-C1 compounds tested, whereas the third isolate S2A1 and Bacillus PM6 grow on betaine, glucose, gluconate, alanine, glutamate, citrate and nutrient agar, but not on any of a further 56 non-C1 compounds. Crude sonic extracts of trimethylamine-grown and glucose-grown W6A and W3A1 isolates, and of trimethylamine-grown C2A1 (an obligate methylotroph) contain (i) no detectable 2-oxogltarate dehydrogenase activity, (ii) very low or zero specific activities of succinate dehydrogenase and succinyl-CoA synthetase and (iii) NAD+-dependent isocitrate dehydrogenase activity. Extracts of trimethylamine-grown PM6 and S2A1 methylotrophs have (i) very low 2-oxoglutarate dehydrogenase specific activities, (ii) comparatively high specific activities of succinate dehydrogenase, malate dehydrogenase and succinyl-CoA synthetase and (iii) NADP+-dependent isocitrate dehydrogenase activity but no NAD+-dependent isocitrate dehydrogenase activity. The activities of most of these enzymes are increased during growth on glucose, alanine, glutamate or citrate, but only very low 2-oxoglutarate dehydrogenase activities are present under all growth conditions. The restricted facultative methylotrophs grow on certain non-C1 compounds in the absence of 2-oxoglutarate dehydrogenase and, in some cases, of other enzymes of the tricarboxylic acid cycle; these lesions cannot therefore be the sole cause of obligate methylotrophy.
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PMID:Tricarboxylic acid-cycle and related enzymes in restricted facultative methylotrophs. 0 Sep 91

Transitional steady-state investigations during changes in oxygen tension under aerobic and during aerobic-anaerobic transition conditions were carried out with the aim of finding an indicator system which separates the equilibrium from the non-equilibrium state. Of the parameters used i.e. biomass formation, CO2 production, Q02, NADH oxidase, succinate dehydrogenase, phosphofructokinase, glyceraldehyde-3 phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and 2-oxoglutarate dehydrogenase, only the three enzymes requiring NADH or NADP for their function fulfilled the requirements. Biomass production and CO2 formation were useful only during the aerobic-anaerobic transition period. In each case the response was immediate and the indicator systems demonstrated that a new steady state of oxygen was always obtained after 11 h which, at the specific growth rate used, was equivalent to at least two volume replacements of the growth vessel.
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PMID:Transitional steady-state investigations during aerobic-anaerobic transition of glucose utilization by Escherichia coli K-12. 34 39

Lipoic acid (lip) and 2-oxoglutarate dehydrogenase (sucA) mutants of Escherichia coli K12 exhibit a requirement for exogenous succinate during aerobic growth on glucose minimal medium. Reversion studies have shown that this requirement can be suppressed by gal-linked mutations which inactivate succinate dehydrogenase. Biochemical and genetic studies confirmed that the succinate dehydrogenase gene (sdh) is affected and that suppression is mediated by the same intergenic and indirect mechanism that generates succinate independence in partial revertants of lipoamide dehydrogenase mutants (Creaghan & Guest, 1977). A series of isogenic strains containing all combinations of mutations affecting 2-oxoglutarate dehydrogenase (sucA), succinate dehydrogenase (sdh), isocitrate lyase (aceA) and fumarate reductase (frd) in a background lacking succinate semialdehyde dehydrogenase, was constructed to assess the importance of these enzymes as sources of endogenous succinate (succinyl-CoA) during aerobic and anaerobic growth on glucose. Only strains combining a deficiency in 2-oxoglutarate dehydrogenase with the presence of an active succinate dehydrogenase required succinate for aerobic growth. In all mutants, including the triple mutant (frd sucA aceA), the succinate requirement was suppressed by inactivating succinate dehydrogenase. The aerobic growth rates of succinate-independent strains were most affected by lack of isocitrate lyase but only two mutants (sdh sucA aceA and frd sdh sucA aceA) grew faster with added succinate: the growth yields were lowered by deficiencies in isocitrate lyase and also succinate dehydrogenase. It is concluded that very little succinate is needed for biosynthesis during aerobic growth on glucose and the requirement for relatively high concentrations of succinate (2 mM) by mutants lacking 2-oxoglutarate dehydrogenase or related functions stems from the presence of active succinate dehydrogenase. Anaerobically, either isocitrate lyase or fumarate reductase is essential for succinate-independent growth on glucose.
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PMID:Succinate dehydrogenase-dependent nutritional requirement for succinate in mutants of Escherichia coli K12. 36 70

Glutamate induced the synthesis of 2-oxoglutarate dehydrogenase 50-fold during anaerobic growth of Citrobacter freundii and, in the absence of glutamate, this enzyme was even more active in cultures sparged with N2/CO2(95:5, v/v). Enzyme synthesis was partially repressed when the inlet gas was passed through heated copper but totally repressed when the inlet gas was passed through alkaline pyrogallol and reduced benzyl viologen (a treatment which would remove CO2 as well as O2). Fumarate hydratase activity also decreased but alcohol dehydrogenase and the sum of the succinate dehydrogenase and fumarate reductase activities increased when residual O2 was removed from the sparging gas. Soluble cytochromes a1 and c552.5 were detected in rigorously anaerobic cultures. Thus traces of O2 which contaminate commercial compressed N2 are sufficient to induce 2-oxoglutarate dehydrogenase synthesis and to affect significantly the synthesis and incorporation of respiratory chain components into the cytoplasmic membrane.
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PMID:Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate. 54 60

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52

Chemostat cultures of E. coli K-12 revealed that the metabolic change from respiration to aerobic fermentation can be obtained with increasing specific growth rate at low glucose input concentration (0.1%), or increasing glucose input concentrations at low specific growth rate (0.1 h-1). Both effects do not affect biomass formation. The metabolic change is not related to a pathway switch of glucose utilization. The increase in specific growth rate causes suppression of succinate dehydrogenase, and NADH oxidase, whereas glucose increases cause suppression of succinate dehydrogenase, cytochrome a and 2-ketoglutarate dehydrogenase. Both phenomena are reflected in the specific oxygen uptake rate, specific carbon dioxide production rate and respiratory quotient values. Growth limitation could be related to a maximal glucose uptake rate of the cell and thus constitutes an entirely different effect caused by high glucose input concentration.
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PMID:Effect of specific growth rate and glucose concentration on growth and glucose metabolism of Escherichia coli K-12. 80 Oct 33

The regulation of alpha-ketogluterate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase, and malic enzyme has been studied in Bacillus subitilis. The levels of these enzymes increase rapidly during late exponential phase in a complex medium and are maximal 1 to 2 h after the onset of sporulation. Regulation of enzyme synthesis has been studied in the wild type and different citric acid cycle mutants by adding various metabolites to the growth medium. Alpha-ketoglutarate dehydrogenase is induced by glutamate or alpha-ketoglutarate; succinate dehydrogenase is repressed by malate; and fumarase and malic enzyme are induced by fumarate and malate, respectively. The addition of glucose leads to repression of the citric acid cycle enzymes whereas the level of malic enzyme is unaffected. Studies on the control of enzyme activities in vitro have shown that alpha-ketoglutarate dehydrogenase and succinate dehydrogenase are inhibited by oxalacetate. Enzyme activities are also influenced by the energy level, expressed as the energy charge of the adenylate pool. Isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, and malic enzyme are inhibited at high energy charge values, whereas malate dehydrogenase is inhibited at low energy charge. A survey of the regulation of the citric acid cycle in B.subtilis, based on the present work and previously reported results, is presented and discussed.
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PMID:Regulation of the dicarboxylic acid part of the citric acid cycle in Bacillus subtilis. 80 68

Two freshwater bacteria, a Pseudomonas sp. and a Spirillum sp., were grown in continuous culture under steady-state conditions in L-lactate-, succinate-, ammonium- or phosphate-limited media. In Pseudomonas sp., NAD-independent and NAD-dependent L-lactate dehydrogenases, aconitase, isocitrate dehydrogenase and glucose 6-phosphate dehydrogenase activities increased up to 10-fold as the dilution rate (D) was decreased from 0.5 to 0.02 h-1, regardless of whether the growth-limiting nutrient was carbon, ammonium or phosphate. In contrast, 2-oxoglutarate dehydrogenase and succinate dehydrogenase activities were not influenced by D, and NADH oxidase activity increased with D. Spirillum sp. gave different results in some respects, but it also exhibited an increase in the activity of several enzymes at low D values. Such increases may emanate from release of catabolite repression, and catabolite repressors for the five enzymes in Pseudomonas sp. showing such increases are probably compounds of carbon, nitrogen and phosphorus. It is likely that increased enzyme syntheses in low D cultures represent the normal physiological state for bacteria in aquatic environments where growth occurs slowly under nutrient limitations. Such increases probably permit a more effective utilization of nutrients present at sub-saturating concentrations.
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PMID:Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture. 95 May 55

The primary structure of the succinyl-CoA synthetase of Escherichia coli has been deduced from the nucleotide sequence of a 2451-base-pair segment of DNA containing the corresponding sucC (beta subunit) and sucD (alpha subunit) genes. The genes are located at one end of a gene cluster that encodes several citric acid cycle enzymes: gltA-sdhCDAB-sucABCD; gltA, citrate synthase; sdh, succinate dehydrogenase; sucA and sucB, the dehydrogenase (E1) and succinyltransferase (E2) components of the 2-oxoglutarate dehydrogenase complex. The sucC and sucD genes are separated from the sucA and sucB genes by a 273-base-pair segment containing four palindromic units, but they appear to be expressed from a sucABCD read-through transcript that extends from the suc promoter to a potential rho-independent terminator at the distal end of sucD. The stop codon of the sucC gene overlaps the sucD initiation codon by a single nucleotide, indicating close translational coupling of the sucC and sucD genes. The sucC gene comprises 1161 base pairs (388 codons, excluding the stop codon), and it encodes a polypeptide of Mr 41 390 corresponding to the beta subunit of succinyl-CoA synthetase. The sucD gene comprises 864 base pairs (288 codons, excluding the start and stop codons), and it encodes a product of Mr 29 644, corresponding to the alpha subunit of succinyl-CoA synthetase. The alpha subunit contains a 12-residue amino acid sequence that is identical with the histidine peptide previously isolated from the phosphoenzyme. This sequence forms part of one of the two potential nucleotide binding sites detected in the alpha subunit.
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PMID:Primary structure of the succinyl-CoA synthetase of Escherichia coli. 300 35

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


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