Search results for "Tartrates"

showing 8 items of 18 documents

The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
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l-Carnitine l-tartrate supplementation favorably affects biochemical markers of recovery from physical exertion in middle-aged men and women.

2009

The purpose of this study was to examine the effects of Carnipure tartrate (Lonza, Allendale, NJ) supplementation (total dose of 2 g/d of l-carnitine) on markers of performance and recovery from physical exertion in middle-aged men and women. Normally active and healthy men (n = 9, 45.4 +/- 5.3 years old) and women (n = 9, 51.9 +/- 5.0 years old) volunteered to participate in the investigation. Double-blind, placebo, balanced treatment presentation and crossover design were used with 3 weeks and 3 days of supplementation followed by a 1-week washout period before the other counterbalanced treatment was initiated. After 3 weeks of each supplementation protocol, each participant then performe…

Muscle tissueAdultMalemedicine.medical_specialtyXanthine OxidaseFree RadicalsEndocrinology Diabetes and MetabolismPhysical ExertionPlaceboEndocrinologyDouble-Blind MethodInternal medicineCarnitinemedicineHumansCarnitineExertionLactic AcidLeg pressTartratesCross-Over Studiesbiologybusiness.industryMyoglobinMiddle AgedCrossover studyMiddle agemedicine.anatomical_structureEndocrinologyPurinesDietary Supplementsbiology.proteinCreatine kinaseFemalebusinessBiomarkersmedicine.drugMetabolism: clinical and experimental
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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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Power saturation of ESR signal in ammonium tartrate exposed to 60Co gamma-ray photons, electrons and protons.

2006

Abstract Marrale, M., Brai, M., Triolo, A., Bartolotta, A. and D'Oca, M. C. Power Saturation of ESR Signal in Ammonium Tartrate Exposed to 60Co γ-Ray Photons, Electrons and Protons. Radiat. Res. 166, 802–809 (2006). In this paper we present an investigation of the electron spin resonance (ESR) line shape of ammonium tartrate (AT) dosimeters exposed to radiation with different linear energy transfer (LET). We exposed our dosimeters to γ-ray photons (60Co), 7 MeV and 14 MeV initial energy electrons, and 19.3 MeV initial energy protons. The differences in the power saturation behavior of ESR spectra of AT irradiated with photons, electrons and protons could be correlated to the effective LET o…

PhotonBiophysicsLinear energy transferElectronsElectronRadiationRadiation DosageSensitivity and Specificitylaw.inventionlawRadiology Nuclear Medicine and imagingLinear Energy TransferIrradiationCobalt RadioisotopesElectron paramagnetic resonanceRadiometrySaturation (magnetic)TartratesPhotonsRadiationDosimeterChemistryElectron Spin Resonance SpectroscopyReproducibility of ResultsDose-Response Relationship RadiationAmmonium Tartrate 60Co -Ray Photons Electrons and Protons.Gamma RaysAtomic physicsProtonsAlgorithmsRadiation research
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Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT).

2010

ABSTRACT Escherichia coli K-12 is able to grow under aerobic conditions on d -malate using DctA for d -malate uptake and the d -malate dehydrogenase DmlA (formerly YeaU) for converting d -malate to pyruvate. Induction of dmlA encoding DmlA required an intact dmlR (formerly yeaT ) gene, which encodes DmlR, a LysR-type transcriptional regulator. Induction of dmlA by DmlR required the presence of d -malate or l - or meso -tartrate, but only d -malate supported aerobic growth. The regulator of general C 4 -dicarboxylate metabolism (DcuS-DcuR two-component system) had some effect on dmlA expression. The anaerobic l -tartrate regulator TtdR or the oxygen sensors ArcB-ArcA and FNR did not have a m…

Physiology and MetabolismRegulatorMalatesDehydrogenasemedicine.disease_causeMicrobiologyMalate dehydrogenaseMicrobiologyMalate DehydrogenasemedicineAnaerobiosisMolecular BiologyEscherichia coliTartratesChromatography High Pressure LiquidbiologyEscherichia coli K12Escherichia coli ProteinsMetabolismGene Expression Regulation Bacterialbiology.organism_classificationbeta-GalactosidaseAerobiosisBiochemistryMutationFermentationAnaerobic exerciseBacteriaJournal of bacteriology
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The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli.

2007

ABSTRACT Escherichia coli ferments l -tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for l -tartrate uptake and succinate export and its relation to the general C 4 -dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE ) gene, is required for the uptake of l -tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the l -tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA , ttdB , and ttdT are cotranscribed. Deletion of ttdT abolished growth by l -tartrate and degradation of l -tartrate c…

biologyAntiporterPhysiology and MetabolismSuccinic AcidHeterologousSubstrate (chemistry)Biological TransportTartratebiology.organism_classificationmedicine.disease_causeMicrobiologychemistry.chemical_compoundBiochemistrychemistryBacterial ProteinsDehydrataseFermentationOperonmedicineEscherichia coliFermentationMolecular BiologyEscherichia coliTartratesBacteriaJournal of bacteriology
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A chiral molecular conductor: synthesis, structure, and physical properties of [ET]3[Sb2(L-tart)2].CH3CN (ET = bis(ethylendithio)tetrathiafulvalene; …

2004

The salt [ET](3)[Sb(2)(L-tart)(2)].CH(3)CN (1) has been obtained by electrocrystallization of the organic donor bis(ethylendithio)tetrathiafulvalene (ET or BEDT-TTF) in the presence of the chiral anionic complex [Sb(2)(L-tart)(2)](2-) (L-tart = (2R,3R)-(+)-tartrate). This salt crystallizes in the chiral space group P2(1)2(1)2(1) (a = 11.145(2) angstroms, b = 12.848(2) angstroms, c = 40.159(14) angstroms, V = 5750.4(14) angstroms(3), Z = 4) and is formed by alternating layers of the anions and of the organic radicals in a noncentrosymmetric alpha-type packing. This compound shows a room temperature electrical conductivity of approximately 1 S.cm(-1) and semiconducting behavior with an activa…

chemistry.chemical_classificationAntimonyChemistryStereochemistryRadicalMolecular ConformationTemperatureSalt (chemistry)Activation energyTartrateCrystallography X-RayMagnetic susceptibilityInorganic Chemistrychemistry.chemical_compoundCrystallographyElectrical resistivity and conductivityElectrochemistryOrganometallic CompoundsThermodynamicsPhysical and Theoretical ChemistryElectronic band structureTartratesTetrathiafulvaleneInorganic chemistry
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Spectroscopic and Structural Investigation of the Confinement of D and L Dimethyl Tartrate in Lecithin Reverse Micelles

2009

The confinement of D and L dimethyl tartrate in lecithin reverse micelles dispersed in cyclohexane has been investigated by FT-IR, polarimetry, electronic and vibrational circular dichroism (ECD and VCD), 1H NMR, and small-angle X-ray scattering (SAXS). Measurements have been performed at room temperature as a function of the solubilizate-to-surfactant molar ratio (R) at fixed lecithin concentration. The analysis of experimental data indicates that the dimethyl tartrate molecules are solubilized within reverse micelles in proximity to the surfactant head groups in the same way for the D and L forms. The encapsulation of dimethyl tatrate within lecithin reverse micelles involves changes in i…

lecithin dimethyl tartrate FT-IR polarimetry circular dichroism NMR SAXSfood.ingredientCyclohexanemicellesTartrateLecithinMicellePolyethylene Glycolschemistry.chemical_compoundfoodLecithinsMaterials ChemistryOrganic chemistryPhysical and Theoretical ChemistryTartratesModels StatisticalDose-Response Relationship DrugChemistry PhysicalViscosityChemistrySmall-angle X-ray scatteringTemperaturetechnology industry and agricultureElasticitySurfaces Coatings and FilmslecithinModels ChemicalSpectrophotometryVibrational circular dichroismMicellar solutionsPhosphatidylcholinesProton NMRPhysical chemistrylipids (amino acids peptides and proteins)Rheologydimethyl tartrate
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