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)

By using the continuous culture technique, the transition from aerobiosis to anaerobiosis and its effect on a number of enzymes has been investigated in Escherichia coli K-12. A decrease in the oxygen partial pressure below 28.0 mm of Hg resulted firstly in an increase of the respiratory enzymes (reduced nicotinamide adenine dinucleotide [NADH] oxidase, 2.53-fold; succinic dehydrogenase, 1.4-fold; cytochrome b(1), 3.91-fold; and cytochrome a(2), 2.45-fold) before the electron transport system gradually collapsed as cytochrome a(2), followed by cytochrome b(1), succinic dehydrogenase, and finally NADH oxidase decreased in activity. The change from respiration to fermentation was initiated well before the oxygen tension reached zero by the increase in levels of fructose diphosphate-aldolase, glucose 6-phosphate, and 6-phosphogluconate dehydrogenases and a decrease in 2-oxoglutarate dehydrogenase. Whem the dissolved oxygen tension reached zero, dry weight and CO(2) formation together with isocitrate dehydrogenase decreased, whereas acid production and phosphofructokinase synthesis started to increase. Enzymatic investigations revealed that the kinetics of the enzyme phosphofructokinase from strict aerobic cultures (6.9 ppm oxygen in solution) was adenosine triphosphate (ATP)-insensitive, whereas the same enzyme from anaerobic cultures was ATP-sensitive. A mechanism is proposed for the change from aerobiosis to anaerobiosis together with the occurring change in glucose regulation.
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PMID:Effect of oxygen on several enzymes involved in the aerobic and anaerobic utilization of glucose in Escherichia coli. 434 16

A fragment of DNA (3.1 kilobases [kb]) from a ColE1 Escherichia coli DNA hybrid plasmid containing the bacterial citrate synthase gene (gltA) was subcloned in both orientations into phage lambda vectors by in vitro recombination. The resulting phages were able to transduce gltA and, as prophages, complemented the lesion of a gltA mutant, showing that a functional gltA gene is contained in the 3.1-kb fragment. The segment of E. coli DNA cloned in these lambda gltA phages was extended in vivo by prophage integration and aberrant excision in the gltA region. Plaque-forming derivatives, carrying up to three additional tricarboxylic acid cycle genes, succinate dehydrogenase (sdh), 2-oxoglutarate dehydrogenase (sucA), and dihydrolipoamide succinyltransferase (sucB), were isolated and characterized by their transducing and complementing activities with corresponding mutants, and the order of the genes was confirmed as gltA-sdh-sucA-sucB. Physical maps of a variety of the transducing phages showed that the four tricarboxylic acid cycle genes are contained in a 12.8-kb segment of bacterial DNA. The four gene products, plus a possible succinate dehydrogenase small subunit, were identified in postinfection labeling studies, and the polarities of gene expression were defined as counterclockwise for gltA and clockwise for sdh, sucA, and sucB, relative to the E. coli linkage map.
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PMID:Molecular cloning of four tricarboxylic acid cyclic genes of Escherichia coli. 628 1

The nucleotide sequence of a 3614 base-pair segment of DNA containing the sdhA gene, encoding the flavoprotein subunit of succinate dehydrogenase of Escherichia coli, and two genes sdhC and sdhD, encoding small hydrophobic subunits, has been determined. Together with the iron-sulphur protein gene (sdhB) these genes form an operon (sdhCDAB) situated between the citrate synthase gene (gltA) and the 2-oxoglutarate dehydrogenase complex genes (sucAB): gltA-sdhCDAB-sucAB. Transcription of the gltA and sdhCDAB gene appears to diverge from a single intergenic region that contains two pairs of potential promoter sequences and two putative CRP (cyclic AMP receptor protein)-binding sites. The sdhA structural gene comprises 1761 base-pairs (587 codons, excluding the initiation codon, AUG) and it encodes a polypeptide of Mr 64268 that is strikingly homologous with the flavoprotein subunit of fumarate reductase (frdA gene product). The FAD-binding region, including the histidine residue at the FAD-attachment site, has been identified by its homology with other flavoproteins and with the flavopeptide of the bovine heart mitochondrial succinate dehydrogenase. Potential active-site cysteine and histidine residues have also been indicated by the comparisons. The sdhC (384 base-pairs) and sdhD (342 base-pairs) structural genes encode two strongly hydrophobic proteins of Mr 14167 and 12792 respectively. These proteins resemble in size and composition, but not sequence, the membrane anchor proteins of fumarate reductase (the frdC and frdD gene products).
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PMID:Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. 638 59

The nucleotide sequence of a 961 base-pair segment of DNA containing the sdhB gene, which encodes the iron-sulphur protein subunit of the E. coli succinate dehydrogenase, has been determined. The sdhB structural gene comprises 711 base pairs (237 codons, excluding the translational initiator and terminator). It is separated by a 15 base-pair intergenic region from the preceding flavoprotein gene (sdhA) and is the distal gene of an operon that also includes genes (sdhC and D) encoding two hydrophobic subunits, sdhCDAB. The distal end of the sdh operon is linked to the 2-oxoglutarate dehydrogenase gene (sucA) by a complex region of dyad symmetry that is homologous with several potential intercistronic regulatory elements or transcriptional attenuators. The sdhB structural gene encodes a polypeptide of Mr26637 that is strikingly homologous with the iron-sulphur protein subunit of fumarate reductase (38% identity, increasing to 58% when conservative changes are included). Both subunits contain 11 cysteine residues, 10 being conserved in three clusters resembling those found in ferredoxins. This work completes the sequence of a 9897 base-pair segment of DNA containing seven tricarboxylic acid cycle genes encoding three enzymes or enzyme complexes, citrate synthase (gltA), succinate dehydrogenase (sdh), and the 2-oxoglutarate dehydrogenase complex (suc), that are organized thus: gltA-sdhCDAB-sucAB.
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PMID:Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. 638 71

Flux through the tricarboxylic acid cycle was calculated from oxygen consumption in hearts perfused near the physiological work load. Activities of citrate synthase, 2-oxoglutarate dehydrogenase and succinate dehydrogenase were measured in the same hearts. Only the activities of 2-oxoglutarate dehydrogenase correlated with calculated fluxes through the cycle.
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PMID:Tricarboxylic acid cycle flux and enzyme activities in the isolated working rat heart. 734 78

Vitamin D3 administration affects the NAD-linked oxidoreductase activities of Krebs cycle from intestinal mucosa of vitamin D-deficient chicks. Vmax values were increased in all of them, while K0.5 for substrate remained unchanged except for 2-oxoglutarate dehydrogenase, which showed lower affinity for oxoglutarate. Addition of Ca2+ to the incubation medium increased the affinity of 2-oxoglutarate dehydrogenase and NAD-isocitrate dehydrogenase for their substrates either in the vitamin D3 treated group or in the control one. The activity of succinate dehydrogenase, a FMN-dependent oxidoreductase, was not modified by vitamin D3 administration. The oxygen consumption of the intestinal mitochondria was not altered by cholecalciferol treatment to vitamin D-deficient chicks. The reason why vitamin D3 selectively affects the NAD-linked oxidoreductase activities of the Krebs cycle remains unknown. The vitamin D hormone, 1,25(OH)2D3, appears to be the mediator of the response.
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PMID:Vitamin D affects Krebs cycle NAD-linked oxidoreductases from chick intestinal mucosa. 754 52

We have identified and sequenced four genes that encode the protein subunits comprising the succinate dehydrogenase enzyme complex (Sdh) of the rickettsia Coxiella burnetii. The Sdh-encoding gene cluster (sdhCDAB) begins 3326 bp upstream from the citrate synthase-encoding gene (gltA) start codon and is read with opposite polarity. An open reading frame encoding the N-terminal 280 amino acids (aa) of 2-oxoglutarate dehydrogenase (SucA) begins 24 bp downstream from the stop codon of the gene specifying the iron-sulfur subunit (sdhB) of Sdh. The deduced aa sequence of Sdh subunits and the N-terminal portion of SucA revealed significant aa identity with the Esherichia coli homologues ranging from a low of 36.6% for SdhD to a high of 61.2% for SdhA and SdhB. Primer extension identified transcription start points (tsp) for sdh and sucA. The region upstream from the sdh tsp, but not the sucA tsp, displayed homology to promoter consensus sequences of E. coli. Further evidence that sucA transcription can occur independent of sdh transcription was provided by demonstrating that a TnphoA insertion disrupting sdhB had no effect on the production of SucA by an E. coli cell-extract-directed in vitro transcription/translation system. The plasmid clone pLPM60, which carries the C. burnetii sdhCDAB coding and upstream regulatory regions, rescued an E. coli sdhA mutant (MOB252), indicating functional expression of the rickettsial locus. A cell extract of MOB252 transformed with pLPM60 showed a sixfold greater level of Sdh enzyme activity over the E. coli wild type. A plasmid clone lacking the sdh upstream regulatory region did not complement nor produce sdh mRNA by dot blot analysis.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization of the succinate dehydrogenase-encoding gene cluster (sdh) from the rickettsia Coxiella burnetii. 769 64

Succinate dehydrogenase activity was measured in rat pancreatic islet homogenates incubated in the presence of [1,4-14C]succinate, the reaction velocity being judged through the generation of 14CO2 in the auxiliary reactions catalysed by pig heart fumarase and chicken liver NADP-malate dehydrogenase. In the presence of 1.0 mM succinate, the reaction velocity averaged 5.53 +/- 0.44 pmol min-1 microgram-1 islet protein. The Km for succinate was close to 0.4 mM and the enzymic activity was restricted to mitochondria. These kinetic results indicate that, under the present experimental conditions, the activity of succinate dehydrogenase does not vastly exceed that of either NAD-isocitrate dehydrogenase or the 2-ketoglutarate dehydrogenase complex, at least when the latter enzymes are activated by ADP and/or Ca2+. Nevertheless, the activity of succinate dehydrogenase is sufficient to account for the increase in O2 uptake evoked in intact islets by the monomethyl ester of succinic acid. It could become a rate-limiting step of the Krebs cycle in models of B-cell dysfunction.
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PMID:Hexose metabolism in pancreatic islets: succinate dehydrogenase activity in islet homogenates. 840 29

Activities of the tricarboxylic acid cycle enzymes were measured in subcellular fractions of liver from rats that had been fed clofibrate for 3 weeks. Large changes in these activities per gram tissue were found in the large particle fraction, which also showed an increase in total protein concentration of 76% under clofibrate treatment. The three regulatory enzymes of the cycle, namely citrate synthase, NAD(+)-linked isocitrate dehydrogenase, and 2-oxoglutarate dehydrogenase were significantly enhanced by 24% (P < 0.02), 54% (P < 0.02), and 153% (P < 0.005), respectively. Fumarase and malate dehydrogenase rose by 71% (P < 0.005) and 95% (P < 0.02), whereas succinate dehydrogenase remained unchanged. Enhancement of the citrate synthase, NAD-isocitrate dehydrogenase, and 2-oxoglutarate dehydrogenase may play a role in decreasing intracellular availability of acetyl-CoA for lipid metabolism.
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PMID:Clofibrate elevates enzyme activities of the tricarboxylic acid cycle in rat liver. 846 21

The expression of several mitochondrial and nuclear genes involved in ATP production was examined in cells cultured from muscle biopsies of patients harboring mitochondrial pathologies. The transcript patterns in muscle cells from the patients affected by carnitine palmitoyl transferase II or 2-ketoglutarate dehydrogenase deficiencies were almost similar to control patterns. In the opposite, patterns were strikingly abnormal in all the other cell cultures from patients with defects in enzymatic complexes involved in oxidative phosphorylation: mitochondrial complex II and III deficiencies, two MELAS syndromes (myopathy, encephalopathy, lactic acidosis and stroke like episodes), a case of Kearns-Sayre syndrome and a case of chronic progressive external ophthalmoplegia. In cultured muscle cells from patients with mtDNA mutations, the percentage of mutated mtDNA was low as compared with those determined in the corresponding skeletal muscle biopsy. Moreover, the complex II defect resulting of a nuclear mutation was not expressed in the cell cultures. Thus, an undetermined transcriptional event, transmitted from muscle biopsies to cultured muscle cells, should be involved to account for such abnormal transcript patterns.
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PMID:Expression of oxidative phosphorylation genes in muscle cell cultures from patients with mitochondrial myopathies. 906 96


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