Search results for "cofactor"

showing 10 items of 74 documents

Trichinella spiralisThymidylate Synthase: Developmental Pattern, Isolation, Molecular Properties, and Inhibition by Substrate and Cofactor Analogues

1996

Abstract Thymidylate synthase specific activity was found to remain at a constant level in crude extracts from muscle larvae, isolated (1-15 months after infection) by pepsin-HCl digestion, as well as from adult worms ofTrichinella spiralis.The enzyme was purified and its molecular (monomer mol. wt 35 kD) and kinetic (sequential mechanism with the Kmvalues 3.1 and 19 μM for dUMP and N5,10-methylenetetrahydrofolate, respectively) properties determined. 5-Fluoro-dUMP was a competitive, slow-binding inhibitor of the parasite enzyme. N5,10-methylenetetrahydrofolate analogues 10-propargyl-5,8-dideazafolate (CB3717), ZD1694, BW1843U89, and AG337 were weaker inhibitors of the parasite than regener…

Thymidine kinase activityBiophysicsThiophenesBiologyBiochemistryThymidylate synthaseChromatography AffinityGene Expression Regulation EnzymologicCofactorStructure-Activity RelationshipFolic AcidNon-competitive inhibitionFluorodeoxyuridylateAnimalsHumansEnzyme InhibitorsMolecular BiologyTrichinella spiralischemistry.chemical_classificationATP synthaseMusclesGene Expression Regulation DevelopmentalSubstrate (chemistry)Thymidylate SynthaseCell BiologyMolecular biologyLiver RegenerationRatsKineticsEnzymeLiverchemistryBiochemistryLarvaQuinazolinesbiology.proteinSpecific activityBiochemical and Biophysical Research Communications
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Tubulin-folding cofactor E deficiency is associated with vascular dysfunction and endoplasmatic reticulum stress of vascular smooth muscle cells

2021

Abstract Introduction Endothelial function assessed via flow mediated dilatation (FMD) has shown to predict risk in individuals with established cardiovascular diseases, whereas its predictive value is uncertain in the setting primary prevention. Purpose The aim of the current work was to discover and evaluate novel mediators of vascular dysfunction in the general population and in conditional knock-out transgenic animal models. Methods In order to identify novel targets that were negatively correlated with FMD and investigate their contribution in vascular function, a Genome Wide Association Study (GWAS) of 5,000 participants was performed and subsequently immune cell-, endothelial- and va…

Tubulin foldingVascular smooth musclebusiness.industryMedicineCOFACTOR ECardiology and Cardiovascular MedicinebusinessReticulumCell biologyEuropean Heart Journal
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Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation.

2013

Iron (Fe) is an essential element for all eukaryotic organisms because it functions as a cofactor in a wide range of biochemical processes. Cells have developed sophisticated mechanisms to tightly control Fe utilization in response to alterations in cellular demands and bioavailability. In response to Fe deficiency, the yeast Saccharomyces cerevisiae activates transcription of the CTH1 and CTH2 genes, which encode proteins that bind to AU-rich elements (AREs) within the 3′ untranslated regions (3′UTRs) of many mRNAs, leading to metabolic reprogramming of Fe-dependent pathways and decreased Fe storage. The precise mechanisms underlying Cth1 and Cth2 function and regulation are incompletely u…

Untranslated regionSaccharomyces cerevisiae ProteinsIronRNA StabilitySaccharomyces cerevisiaeMolecular Sequence DataSaccharomyces cerevisiaeBiologyCofactorTristetraprolinIn vivoTranscription (biology)Gene Expression Regulation FungalAutoregulationRNA MessengerMolecular BiologyGene3' Untranslated RegionsAU Rich ElementsBase SequenceCell BiologyArticlesbiology.organism_classificationMolecular biologyAdaptation PhysiologicalYeastCell biologyDNA-Binding Proteinsbiology.proteinTranscription FactorsMolecular and cellular biology
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Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation.

2004

AbstractIron (Fe) is an essential micronutrient for virtually all organisms and serves as a cofactor for a wide variety of vital cellular processes. Although Fe deficiency is the primary nutritional disorder in the world, cellular responses to Fe deprivation are poorly understood. We have discovered a posttranscriptional regulatory process controlled by Fe deficiency, which coordinately drives widespread metabolic reprogramming. We demonstrate that, in response to Fe deficiency, the Saccharomyces cerevisiae Cth2 protein specifically downregulates mRNAs encoding proteins that participate in many Fe-dependent processes. mRNA turnover requires the binding of Cth2, an RNA binding protein conser…

Untranslated regionSaccharomyces cerevisiae ProteinsTranscription GeneticIronSaccharomyces cerevisiaeMolecular Sequence DataDown-RegulationRNA-binding proteinSaccharomyces cerevisiaeBiologyGeneral Biochemistry Genetics and Molecular BiologyCofactorTristetraprolinGene Expression Regulation FungalMRNA degradationmedicineRNA MessengerRNA Processing Post-TranscriptionalMessenger RNABase SequenceBiochemistry Genetics and Molecular Biology(all)Mechanism (biology)Iron deficiencybiology.organism_classificationmedicine.diseaseDNA-Binding ProteinsBiochemistryMutationbiology.proteinPlasmidsCell
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High yielding one-pot enzyme-catalyzed synthesis of UDP-glucose in gram scales

2001

Abstract Uridine diphosphoglucose is an important cofactor of glucosylating enzymes. A simple and high yielding one-pot enzymatic synthesis of UDPG on a gram scale from glucose via hexokinase, phosphoglucomutase and UDPG pyrophosphorylase (UGPase) is described. Repetitive addition of substrate was used to avoid inhibition of UGPase. The approach allows recovery of active enzymes and their re-use. The synthesis of UDP-[4-13C]-glucose on a 0.5 g scale resulted in a final yield of 70% and a purity of >95% after chromatographic purification.

Uridine Diphosphate GlucoseMagnetic Resonance SpectroscopyUTP-Glucose-1-Phosphate UridylyltransferaseBiochemistryHigh yieldingCatalysisCofactorAnalytical Chemistrychemistry.chemical_compoundHexokinaseCarbon RadioisotopesGramchemistry.chemical_classificationHexokinaseChromatographyMolecular StructurebiologyOrganic ChemistrySubstrate (chemistry)General MedicineGlucoseEnzymePhosphoglucomutasechemistryBiochemistryYield (chemistry)biology.proteinPhosphoglucomutaseCarbohydrate Research
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NAD(P)H regeneration is the key for heterolactic fermentation of hexoses in Oenococcus oeni

2002

Oenococcus oeni (formerly Leuconostoc oenos) can perform malolactic fermentation, converting L-malate to L-lactate and carbon dioxide, in wines. The energy and redox potential required to support the growth of the micro-organism are supplied mainly by the consumption of carbohydrates via the heterolactic pathway. In the first steps of hexose metabolism two molecules of NAD(P)(+) are consumed, which must be regenerated in later reactions. The aim of this work was to test if aerobic growth of O. oeni promotes higher cell yields than anaerobic conditions, as has been shown for other lactic acid bacteria. O. oeni M42 was found to grow poorly under aerobic conditions with glucose as the only car…

WineFructoseMicrobiologyCofactorchemistry.chemical_compoundMalolactic fermentationAnaerobiosisOenococcus oenibiologyEthanolFructoseCarbohydratebiology.organism_classificationAerobiosisLactic acidCulture MediaGram-Positive CocciGlucosechemistryBiochemistryFermentationbiology.proteinNAD+ kinaseAnaerobic exerciseLeuconostocNADP
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The noncovalent dimerization of a G-quadruplex/hemin DNAzyme improves its biocatalytic properties.

2020

While many protein enzymes exert their functions through multimerization, which improves both selectivity and activity, this has not yet been demonstrated for other naturally occurring catalysts. Here, we report a multimerization effect applied to catalytic DNAs (or DNAzymes) and demonstrate that the enzymatic efficiency of G-quadruplexes (GQs) in interaction with the hemin cofactor is remarkably enhanced by homodimerization. The resulting non-covalent dimeric GQ–DNAzyme system provides hemin with a structurally defined active site in which both the cofactor (hemin) and the oxidant (H2O2) are activated. This new biocatalytic system efficiently performs peroxidase- and peroxygenase-type biot…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyDeoxyribozyme010402 general chemistryG-quadruplex01 natural sciencesCofactor03 medical and health scienceschemistry.chemical_compoundheterocyclic compounds030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryActive siteGeneral Chemistry[CHIM.CATA]Chemical Sciences/CatalysisCombinatorial chemistry[SDE.ES]Environmental Sciences/Environmental and Society0104 chemical sciencesChemistryEnzymebiology.proteinSelectivityPeroxidaseHeminChemical science
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Citrate lyases of lactic acid bacteria

1998

Citrate Iyase is a key enzyme of the citrate metabolism which is involved in flavor and texture of many fermented milk products. Citrate Iyase which catalyses the cleavage of citrate into oxaloacetate and acetate is a multienzyme complex composed of three proteins: an acyl carrier protein (ACP); a citrate, acetate-ACP transferase; and a citryl-S-ACP Iyase. The citrate Iyase is active only when the thioester residue of the prosthetic group bound to ACP is acetylated. In the presence of citrate, the transferase mediates the formation of citryl-S-acyl carrier protein by acyl exchange and liberation of acetate. Then the Iyase subunit cleaves the citryl-S-ACP with libe- ration of oxaloacetate an…

biologyATP citrate lyasefood and beverages[SDV.IDA] Life Sciences [q-bio]/Food engineeringbiology.organism_classificationCofactorLactic acidchemistry.chemical_compoundAcyl carrier protein[SDV.AEN] Life Sciences [q-bio]/Food and NutritionBiochemistrychemistryLeuconostoc mesenteroidesbiology.proteinTransferaseLeuconostocCitrate synthaselipids (amino acids peptides and proteins)ComputingMilieux_MISCELLANEOUSFood Science
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Optical sensing of cyanide using hybrid biomolecular films

2006

The selective sensing of cyanide anions in water has been studied using a hybrid biomaterial composed of a mesoporous TiO2 film of crystalline nanoparticles and the protein hemoglobin. The mesoporous structure of the film prevents protein unfolding and also stabilizes the oxidized form of the prosthetic groups. Low-levels of cyanide anions (<0.2 ppm (0.2 mgr/L)) can be detected by monitoring the changes in the optical properties of the hybrid biomolecular films upon cyanide binding to the heme groups.

biologyCyanideInorganic chemistryBiomaterialNanoparticleBioinorganic chemistryPhotochemistryCofactorInorganic Chemistrychemistry.chemical_compoundchemistryMaterials Chemistrybiology.proteinsense organsHemoglobinPhysical and Theoretical ChemistryMesoporous materialHemeInorganic Chemistry Communications
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l ‐carnitine: Structure and Function

2011

l-carnitine is found in nearly all living cells. l-carnitine present in human body can be either provided by a biosynthetic pathway or by food. Carnitine plays a major role in lipid and energy metabolism. In the human body, the primary role of l-carnitine is to shuttle long-chain fatty acids into the mitochondria where they are used to produce energy. l-carnitine is also involved in the peroxisomal oxidative metabolism and serves as a cofactor for various enzymatic reactions. Several reports suggest that l-carnitine may act as an anti-oxidant agent and limit the deleterious effects of free radicals. Many studies have estimated the role and the potential effectiveness of l-carnitine in vario…

biologySkeletal muscleLipid metabolismPhysical exerciseMitochondrionPeroxisomeCofactormedicine.anatomical_structureBiochemistrybiology.proteinmedicineCarnitineFunction (biology)medicine.drugeLS
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