Search results for "Acetyl Coenzyme A"

showing 5 items of 5 documents

Chromatin remodeling regulation by small molecules and metabolites.

2010

The eukaryotic genome is a highly organized nucleoprotein structure comprising of DNA, histones, non-histone proteins, and RNAs, referred to as chromatin. The chromatin exists as a dynamic entity, shuttling between the open and closed forms at specific nuclear regions and loci based on the requirement of the cell. This dynamicity is essential for the various DNA-templated phenomena like transcription, replication, and repair and is achieved through the activity of ATP-dependent chromatin remodeling complexes and covalent modifiers of chromatin. A growing body of data indicates that chromatin enzymatic activities are finely and specifically regulated by a variety of small molecules derived f…

DNA ReplicationS-AdenosylmethionineTranscription GeneticInositol PhosphatesBiophysicsBiochemistryChromatin remodelingchemistry.chemical_compoundAdenosine TriphosphateStructural BiologyAcetyl Coenzyme AGeneticsAnimalsHumansMolecular Biologychromatin small moleculesbiologyGenome HumanDNA replicationDNAChromatin Assembly and DisassemblyNADMi-2/NuRD complexChromatinNucleoproteinChromatinHistoneBiochemistrychemistrybiology.proteinNAD+ kinaseDNABiochimica et biophysica acta
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Significance of pantothenate for glucose fermentation by Oenococcus oeni and for suppression of the erythritol and acetate production.

2001

The heterofermentative lactic acid bacterium Oenococcus oeni requires pantothenic acid for growth. In the presence of sufficient pantothenic acid, glucose was converted by heterolactic fermentation stoichiometrically to lactate, ethanol and CO2. Under pantothenic acid limitation, substantial amounts of erythritol, acetate and glycerol were produced by growing and resting bacteria. Production of erythritol and glycerol was required to compensate for the decreasing ethanol production and to enable the synthesis of acetate. In ribose fermentation, there were no shifts in the fermentation pattern in response to pantothenate supply. In the presence of pantothenate, growing O. oeni contained at l…

ErythritolAcetatesBiochemistryMicrobiologyPantothenic Acidchemistry.chemical_compoundPhosphate AcetyltransferaseAcetyl Coenzyme APantothenic acidGeneticsGlycerolEthanol fuelCoenzyme AMolecular BiologyOenococcus oeniEthanolbiologyGeneral Medicinebiology.organism_classificationAldehyde OxidoreductasesCulture MediaGram-Positive CocciErythritolGlucosechemistryBiochemistryFermentationFermentationBacteriaLeuconostocArchives of microbiology
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Extracellular oxidoreduction potential modifies carbon and electron flow in Escherichia coli.

2000

ABSTRACT Wild-type Escherichia coli K-12 ferments glucose to a mixture of ethanol and acetic, lactic, formic, and succinic acids. In anoxic chemostat culture at four dilution rates and two different oxidoreduction potentials (ORP), this strain generated a spectrum of products which depended on ORP. Whatever the dilution rate tested, in low reducing conditions (−100 mV), the production of formate, acetate, ethanol, and lactate was in molar proportions of approximately 2.5:1:1:0.3, and in high reducing conditions (−320 mV), the production was in molar proportions of 2:0.6:1:2. The modification of metabolic fluxes was due to an ORP effect on the synthesis or stability of some fermentation enzy…

MESH : Models Chemical0106 biological sciencesMESH: Oxidation-ReductionMESH : Acetic AcidMESH : Escherichia coliMESH : NADFormatesOxaloacetatesMESH: Phosphoenolpyruvate CarboxylaseSuccinic AcidMESH: Alcohol DehydrogenaseMESH : CarbonMESH : EthanolMESH: Carbon Dioxide01 natural sciencesPhosphoenolpyruvatechemistry.chemical_compoundModels[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAcetic Acid0303 health sciencesbiologyMESH: Escherichia coliMESH: Models ChemicalMESH : Acetyl Coenzyme AMESH: NADLactic acidMESH : Carbon DioxideBiochemistryFormic AcidsMESH: PhosphoenolpyruvateMESH: Acetic AcidMESH: Pyruvate KinaseMESH : Phosphoenolpyruvate CarboxylaseMESH: Oxaloacetic AcidsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: EthanolPhysiology and MetabolismPyruvate KinaseElectronsChemicalMESH: CarbonMESH : Formic AcidsChemostatMicrobiologyMESH: Fermentation03 medical and health sciencesAcetic acidMESH : Alcohol DehydrogenaseAcetyl Coenzyme AMESH : Fermentation010608 biotechnology[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliFormate[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLactic Acid[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyAlcohol dehydrogenaseMESH : Oxidation-ReductionMESH: ElectronsEthanolEthanolMESH : Succinic AcidAlcohol DehydrogenaseCarbon DioxideNADMESH: Formic AcidsMESH : Pyruvate KinaseCarbonOxaloacetic AcidsPhosphoenolpyruvate CarboxylaseMESH: Succinic Acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryModels ChemicalSuccinic acidMESH : Lactic AcidMESH : Oxaloacetic AcidsFermentationbiology.proteinFermentationMESH: Lactic AcidMESH : ElectronsMESH : PhosphoenolpyruvateMESH: Acetyl Coenzyme A
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Effects of indole-3-acetic acid on Sinorhizobium meliloti survival and on symbiotic nitrogen fixation and stem dry weight production

2009

We evaluated the effects of the main auxin phytohormone, indole-3-acetic acid (IAA), on the central metabolism of Sinorhizobium meliloti strain 1021. We either treated the Sinorhizobium meliloti 1021 strain with 0.5 mM IAA (1021+) or use a derivative, RD64, of the same strain harbouring a pathway for IAA biosynthesis converting tryptophan into IAA via indoleacetamide. We assayed the activity of key enzymes in the major energy-yielding pathways (Entner-Doudoroff, Embden-Meyerhof-Parnas, pentose phosphate, glyoxylate bypass and tricarboxylic acid cycle). We found that activity of two main regulative tricarboxylic acid (TCA) cycle enzymes was increased. Citrate synthase (CS) activity, as compa…

PolyestersHydroxybutyratesDehydrogenaseCitrate (si)-SynthaseApplied Microbiology and BiotechnologyCell survival . PHB . TCA . Nitrogen fixationchemistry.chemical_compoundBacterial ProteinsPlant Growth RegulatorsAcetyl Coenzyme AAuxinNitrogen FixationMedicago truncatulaCitrate synthaseKetoglutarate Dehydrogenase ComplexBiomasschemistry.chemical_classificationSinorhizobium melilotiMicrobial ViabilityIndoleacetic AcidsPlant StemsbiologyTryptophanfood and beveragesGeneral MedicineMetabolismbiology.organism_classificationCitric acid cycleBiochemistrychemistrybiology.proteinIndole-3-acetic acidSinorhizobium melilotiBiotechnologyApplied Microbiology and Biotechnology
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The yeast histone acetyltransferase A2 complex, but not free Gcn5p, binds stably to nucleosomal arrays.

2000

We have investigated the structural basis for the differential catalytic function of the yeast Gcn5p-containing histone acetyltransferase (HAT) A2 complex and free recombinant yeast Gcn5p (rGcn5p). HAT A2 is shown to be a unique complex that contains Gcn5p, Ada2p, and Ada3p, but not proteins specific to other related HAT A complexes, e.g. ADA, SAGA. Nevertheless, HAT A2 produces the same unique polyacetylation pattern of nucleosomal substrates reported previously for ADA and SAGA, demonstrating that proteins specific to the ADA and SAGA complexes do not influence the enzymatic activity of Gcn5p within the HAT A2 complex. To investigate the role of substrate interactions in the differential …

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyBiochemistrySubstrate SpecificityFungal ProteinsHistonesTetramerAcetyl Coenzyme AAcetyltransferasesparasitic diseasesCentrifugation Density GradientAnimalsMolecular BiologyHistone Acetyltransferaseschemistry.chemical_classificationSubstrate (chemistry)AcetylationCell BiologyHistone acetyltransferaseYeastChromatinRecombinant ProteinsTrypsinizationNucleosomesN-terminusDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)EnzymechemistryBiochemistryAcetylationBiophysicsbiology.proteinChickensProtein KinasesThe Journal of biological chemistry
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