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 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

Two types of fumarate reductase transducing phages, lambda frdA, carrying the wild-type frdA gene but differing in the orientation of a R.HindIII fragment of bacterial DNA were isolated from populations of recombinant transducing phages by their ability to complement the lesions of frdA mutants of E. coli. In lysogens, the cloned frdA gene was controlled by its own promoter and was fully responsive to normal regulatory stimuli. The lambda frdA phages would not complement the defects of succinate dehydrogenase (sdh) mutants. Genetic studies showed that the R.HindIII fragment contains ampA, the cis-acting regulatory locus for the chromosomal beta-lactamase gene ampC. No evidence for the presence of other markers was detected but the bacterial segment could be extended to produce plaque-forming phage derivatives containing the amp operon and a gene concerned with bacteriophage morphogenesis, groE(mop). A physical map of the 4.9 kb R.HindIII fragment was constructed by restriction analysis and flanking fragments were identified by DNA:DNA hybridization analysis. The frdA region contained a single asymmetric R.EcoRI target 3.33 kb from one end and the orientation of the physical map with respect to the E.coli linkage map was established.
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PMID:Genetic and physical characterization of lambda transducing phages (lambda frdA) containing the fumarate reductase gene of Escherichia coli K12. 644 51

The specific activities, kinetic constants and pH optima for succinate dehydrogenase were determined in mantle, gill and adductor muscle from three bivalves (Anodonta couperiana, Elliptio buckleyi and Mercenaria campechiensis). In general the Km values for succinate and Ki values for fumarate differed in all bivalve tissues whereas the Ki for malonate was consistently low. The ratio of Ki (fumarate) to Km (succinate) was less than one for all tissues studied. This is similar to many facultative anaerobes with fumarate reductase activity.
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PMID:Succinate dehydrogenase in various tissues of Anodonta couperiana, Elliptio buckleyi and Mercenaria campechiensis (Mollusca: Bivalvia). 646 9

Various enzymes of the tricarboxylic acid cycle (TCA) viz., aconitase (E.C. 4.2.1.3), isocitrate dehydrogenase (E.C. 1.1.1.42), succinate dehydrognease (E.C. 1.3.99.1), fumarate reductase (NADH: fumarate oxido-reductase), fumarase (E.C. 4.2.1.2) and maltate dehydrogenase (E.C. 1.1.1.37) were detected in adult Haemonchus contortus (Nematoda: Trichostrongylidae), in vitro. Low activities of aconitase and isocitrate dehydrogenase suggested that the TCA cycle has a minor function and the pathway of CO2 fixation is the major pathway in the energy metabolism of the parasite. In vitro incubation in Tyrode's solution had no significant effect on TCA cycle enzymes and the worm was able to maintain normal metabolism for 12 h. The effects of D L-tetramisole and rafoxanide on various enzymes of the TCA cycle were studied in adult H. contortus. At 50 micrograms ml-1 varying degrees of inhibition of succinate dehydrogenase and fumarate reductase activities were observed. At the same concentration, the activities of other enzymes remained unaltered.
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PMID:The effects of DL-tetramisole and rafoxanide on tricarboxylic acid cycle enzymes of Haemonchus contortus, in vitro. 668 86

The frdB gene, encoding the iron-sulphur protein subunit of fumarate reductase, has been located and its complete nucleotide sequence determined. The identity of the gene was confirmed by protein chemical studies and determination of the NH2-terminal sequence of the FrdB protein. The frdB gene is situated distal to and partially overlapped by frdA which codes for the flavoprotein subunit of the reductase. Its reading frame contains 244 codons and predicts a protein of Mr 27092. In composition, the FrdB protein is strikingly similar to the corresponding subunit of the related flavoenzyme, succinate dehydrogenase. Analysis of the protein's primary structure revealed several features characteristic of iron-sulphur proteins.
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PMID:Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. 675 16

Diethylpyrocarbonate (Et2PC) inhibits the succinate dehydrogenase [succinate:(acceptor) oxidoreductase, EC 1.3.99.1] activity of submitochondrial particles, Complex II (succinate:ubiquinone oxidoreductase), and the soluble, pure succinate dehydrogenase. The reaction order with respect to Et2PC concentration is close to unity, suggesting modification of one essential residue per active unit of the enzyme. The pH profile of Et2PC inhibition, the partial reversal of inhibition by hydroxylamine, and the spectral change of the Et2PC-treated enzyme in the UV region suggest modification of a histidyl residue. Succinate dehydrogenase activity can be protected against Et2PC inhibition by succinate, fumarate, malonate, or oxaloacetate (also by activating anions such as ClO4(-) and Br-), suggesting that the Et2PC-modified essential residue might be at the active site. In both submitochondrial particles and the purified enzyme, succinate dehydrogenase activity is highest and relatively constant at pH greater than or equal to 7.0 and diminishes precipitously at pH less than 7.0. By contrast, fumarate reductase activity is highest at pH less than or equal to 7.0 and diminishes at pH greater than 7.0. These results are consistent with the possible participation of the unprotonated and protonated forms of the imidazole moiety of the putative histidyl residue, respectively, in succinate oxidation and fumarate reduction.
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PMID:Possible occurrence and role of an essential histidyl residue in succinate dehydrogenase. 694 49

The nucleotide sequence of the frdA gene, which encodes the flavoprotein subunit of the fumarate reductase, of Escherichia coli, has been determined. A polypeptide of Mr = 66,052, containing 602 amino acid residues, is predicted. In composition the FrdA protein strongly resembles the flavoprotein subunits of two succinate dehydrogenases. Moreover, a sequence of nine consecutive residues is common to the flavoprotein subunits from fumarate reductase and the beef heart succinate dehydrogenase. This sequence contains a histidyl residue which probably services as the site for attachment of the FAD cofactor to the reductase.
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PMID:Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. 703 4

A broad range of anions was shown to stimulate the maximal velocity of purified fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli, while leaving the Km for fumarate unaffected. Reducing agents potentiate the effects of anions on the activity, but have no effect by themselves. Thermal stability, conformation as monitored by circular dichroism and susceptibility to the thiol reagent 5,5'-dithiobis-(2-nitrobenzoic acid) are also altered by anions. The apparent Km for succinate in the reverse reaction (succinate dehydrogenase activity) varies as a function of anion concentration, but the maximal velocity is not affected. The membrane-bound activity is not stimulated by anions and its properties closely resemble those of the purified enzyme in the presence of anions. Thus it appears that anions alter the physical and chemical properties of fumarate reductase, so that it more closely resembles the membrane-bound form.
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PMID:The effects of anions on fumarate reductase isolated from the cytoplasmic membrane of Escherichia coli. 704 87

Microfilariae of bovine filarial parasite Setaria cervi are equipped with the enzymes of glycolysis, pentose phosphate and PEP-succinate pathways and thus resemble the adult form in its metabolic pattern. Malate dehydrogenase was the most active enzyme in microfilariae followed by lactic dehydrogenase and fumarase, while phosphoglucoisomerase, PEP-carboxykinase and FDP-aldolase were comparatively less active. The very low ratio of PK/PEPCK in S. cervi microfilariae indicates active fixation of CO2 into PEP to produce oxalacetate. Centperazine and diethylcarbamazine significantly inhibited PEP-carboxykinase, fumarate reductase and succinic dehydrogenase, suggesting that these antifilarials probably exert microfilaricidal action by blocking the PEP-succinate pathway.
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PMID:Setaria cervi: enzymes in microfilariae and in vitro action of antifilarials. 715 43


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