Search results for "Fumarate reductase"

showing 5 items of 15 documents

A Na+-coupled C4-dicarboxylate transporter (Asuc_0304) and aerobic growth of Actinobacillus succinogenes on C4-dicarboxylates

2014

Actinobacillus succinogenes, which is known to produce large amounts of succinate during fermentation of hexoses, was able to grow on C4-dicarboxylates such as fumarate under aerobic and anaerobic conditions. Anaerobic growth on fumarate was stimulated by glycerol and the major product was succinate, indicating the involvement of fumarate respiration similar to succinate production from glucose. The aerobic growth on C4-dicarboxylates and the transport proteins involved were studied. Fumarate was oxidized to acetate. The genome of A. succinogenes encodes six proteins with similarity to secondary C4-dicarboxylate transporters, including transporters of the Dcu (C4-dicarboxylate uptake), Dcu…

Molecular Sequence Datamedicine.disease_causeModels BiologicalMicrobiologyDivalentBacterial ProteinsFumaratesmedicineDicarboxylic AcidsAmino Acid SequenceAnaerobiosisCarbon RadioisotopesEscherichia coliPhylogenyDicarboxylic Acid Transporterschemistry.chemical_classificationbiologySodiumBiological TransportSuccinatesActinobacillusGene Expression Regulation BacterialFumarate reductasebiology.organism_classificationAerobiosisTransport proteinActinobacillus succinogenesGlucoseBiochemistrychemistrySymporterFermentationCotransporterSequence AlignmentMicrobiology
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Regulation of tartrate metabolism by TtdR and relation to the DcuS–DcuR-regulated C4-dicarboxylate metabolism of Escherichia coli

2009

Escherichia coli catabolizes l-tartrate under anaerobic conditions to oxaloacetate by the use of l-tartrate/succinate antiporter TtdT and l-tartrate dehydratase TtdAB. Subsequently, l-malate is channelled into fumarate respiration and degraded to succinate by the use of fumarase FumB and fumarate reductase FrdABCD. The genes encoding the latter pathway (dcuB, fumB and frdABCD) are transcriptionally activated by the DcuS–DcuR two-component system. Expression of the l-tartrate-specific ttdABT operon encoding TtdAB and TtdT was stimulated by the LysR-type gene regulator TtdR in the presence of l- and meso-tartrate, and repressed by O2 and nitrate. Anaerobic expression required a functional fn…

OperonBiologymedicine.disease_causeMicrobiologyAntiportersSubstrate SpecificityOperonEscherichia colimedicinePromoter Regions GeneticTartratesEscherichia coliPsychological repressionHydro-LyasesRegulator geneNitratesEscherichia coli ProteinsPromoterGene Expression Regulation BacterialFumarate reductaseDNA-Binding ProteinsOxygenGlucoseBiochemistryDehydrataseFumaraseProtein KinasesTranscription FactorsMicrobiology
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Expression of the succinate dehydrogenase genes (sdhCAB) from the facultatively anaerobic paenibacillus macerans during aerobic growth

1998

Paenibacillus (formerly Bacillus) macerans is capable of succinate oxidation under oxic conditions and fumarate reduction under anoxic conditions. The reactions are catalyzed by different enzymes, succinate dehydrogenase (Sdh) and fumarate reductase (Frd). The genes encoding Sdh (sdhCAB) were analyzed. The gene products of sdhA and sdhB were similar to the subunits of known Sdh and Frd enzymes. The hydrophobic subunit SdhC showed close sequence similarity to the class of Sdh/Frd enzymes containing diheme cytochrome b. From the sdhCAB gene cluster two transcripts were produced, one comprising sdhCAB, the other sdhAB. The transcripts were found only during aerobic growth, and the amount was d…

Paenibacillus maceranschemistry.chemical_classificationbiologySDHBSuccinate dehydrogenaseSDHAmacromolecular substancesGeneral MedicineFumarate reductasebiology.organism_classificationBiochemistryMicrobiologyPaenibacillusEnzymeBiochemistrychemistryGene clusterGeneticsbiology.proteinMolecular BiologyArchives of microbiology
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Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase

2001

The membrane fraction of Bacillus subtilis catalyzes the reduction of fumarate to succinate by NADH. The activity is inhibited by low concentrations of 2-(heptyl)-4-hydroxyquinoline-N-oxide (HOQNO), an inhibitor of succinate: quinone reductase. In sdh or aro mutant strains, which lack succinate dehydrogenase or menaquinone, respectively, the activity of fumarate reduction by NADH was missing. In resting cells fumarate reduction required glycerol or glucose as the electron donor, which presumably supply NADH for fumarate reduction. Thus in the bacteria, fumarate reduction by NADH is catalyzed by an electron transport chain consisting of NADH dehydrogenase (NADH:menaquinone reductase), menaqu…

biologyATP synthaseBiochemistryChemistryProtonophoreSuccinate dehydrogenaseNADH dehydrogenasebiology.proteinReductaseFumarate reductaseBiochemistryRedoxElectron transport chainEuropean Journal of Biochemistry
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Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

2006

Sulphate- or sulphur-reducing bacteria with known or draft genome sequences (Desulfovibrio vulgaris, Desulfovibrio desulfuricans G20, Desulfobacterium autotrophicum [draft], Desulfotalea psychrophila and Geobacter sulfurreducens) all contain sdhCAB or frdCAB gene clusters encoding succinate : quinone oxidoreductases. frdD or sdhD genes are missing. The presence and function of succinate dehydrogenase versus fumarate reductase was studied. Desulfovibrio desulfuricans (strain Essex 6) grew by fumarate respiration or by fumarate disproportionation, and contained fumarate reductase activity. Desulfovibrio vulgaris lacked fumarate respiration and contained succinate dehydrogenase activity. Succi…

chemistry.chemical_classificationbiologySulfatesSuccinate dehydrogenaseMolecular Sequence DataSuccinic AcidBacillus subtilisFumarate reductasebiology.organism_classificationMicrobiologySuccinate DehydrogenaseEnzymechemistryBiochemistryFumaratesMultigene Familybiology.proteinDesulfovibrioSDHDAmino Acid SequenceDesulfovibrio vulgarisGeobacter sulfurreducensOxidation-ReductionBacteriaMicrobiology (Reading, England)
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