Search results for "glyceraldehyde-3-phosphate dehydrogenase"

showing 10 items of 30 documents

A critical role of plastidial glycolytic Glyceraldehyde-3-Phosphate Dehydrogenase in the control of plant metabolism and development

2009

3 páginas.

PlastidArabidopsisDehydrogenasePlant ScienceSerine biosynthesisGenes PlantPlant RootsGene Expression Regulation EnzymologicSerinechemistry.chemical_compoundBiosynthesisGene Expression Regulation PlantSerineGlycolysisRNA MessengerPlastidsAmino AcidsPhosphorylationPhylogenyGlyceraldehyde 3-phosphate dehydrogenasebiologyArabidopsis ProteinsGAPDHGenetic Complementation TestGlyceraldehyde-3-Phosphate DehydrogenasesMetabolismLipid MetabolismArticle AddendumPlant LeavesProtein TransportCytosolMetabolic pathwayPhenotypeBiochemistrychemistryMutationbiology.proteinCarbohydrate MetabolismGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisResearch Article
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Interactions between abscisic acid and plastidial glycolysis in Arabidopsis

2011

[EN] The phytohormone abscisic acid (ABA) controls the development of plants and plays a crucial role in their response to adverse environmental conditions like salt and water stress.1-3 Complex interactions between ABA and sugar signal transduction pathways have been shown. However, the role played by glycolysis in these interactions is not known. In the associated study,4 we investigated the interactions between plastidial glycolytic glyceraldehyde-3-phosphate dehydrogenase (GAPCp) and ABA signal transduction in Arabidopsis. We followed physiological, genetic and genomic approaches to understand the processes and mechanisms underlying the ABAglycolysis interactions. Our results indicated …

PlastidArabidopsisPlant Sciencechemistry.chemical_compoundAmino acid homeostasisArabidopsisTranscriptional regulationBIOQUIMICA Y BIOLOGIA MOLECULARHomeostasisPlastidsAmino AcidsTranscription factorAbscisic acidGlyceraldehyde 3-phosphate dehydrogenasebiologyArabidopsis Proteinsorganic chemicalsfungiGlyceraldehyde-3-Phosphate Dehydrogenasesfood and beveragesbiology.organism_classificationArticle AddendumGAPCpSugar-ABA interactionschemistryBiochemistryMutationABA signal transductionbiology.proteinCarbohydrate MetabolismGlyceraldehyde- 3-phosphate dehydrogenaseSignal transductionSugar signal transductionGlycolysisAbscisic AcidSignal Transduction
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Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase fromCandida albicans

1999

We report here the purification of a functionally active recombinant glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Candida albicans. The GAPDH protein encoded by the TDH1 gene was obtained as a glutathione S-transferase fusion protein by expression in the vector pGEX-4T-3, and purified by affinity chromatography and thrombin digestion. The purified protein displays GAPDH enzymatic activity (42 micromol NADH min(-1) mg(-1)) as well as the laminin and fibronectin binding activities previously described. In addition, the recombinant GAPDH is covalently modified by NAD linkage; this modification is stimulated by nitric oxide and probably involves a sulfhydryl group (cysteine) residue si…

Recombinant Fusion ProteinsDehydrogenaseBiologyMicrobiologyChromatography Affinitylaw.inventionchemistry.chemical_compoundstomatognathic systemAffinity chromatographylawGlyceraldehydeCandida albicansEscherichia coliGeneticsCloning MolecularMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseGlutathione TransferaseThrombinGlyceraldehyde-3-Phosphate DehydrogenasesMolecular biologyRecombinant ProteinsKineticschemistryBiochemistryFibronectin bindingbiology.proteinRecombinant DNAGlyceraldehyde 3-phosphateCysteineFEMS Microbiology Letters
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The formation of hybrid complexes between isoenzymes of glyceraldehyde‐3‐phosphate dehydrogenase regulates its aggregation state, the glycolytic acti…

2019

The glycolytic enzyme glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) has been traditionally considered a housekeeping protein involved in energy generation. However, evidence indicates that GAPDHs from different origins are tightly regulated and that this regulation may be on the basis of glycolysis‐related and glycolysis‐unrelated functions. In Saccharomyces cerevisiae, Tdh3 is the main GAPDH, although two other isoenzymes encoded by TDH1 and TDH2 have been identified. Like other GAPDHs, Tdh3 exists predominantly as a tetramer, although dimeric and monomeric forms have also been isolated. Mechanisms of Tdh3 regulation may thus imply changes in its oligomeric state or be based in its abil…

Saccharomyces cerevisiae Proteinslcsh:BiotechnologySaccharomyces cerevisiaeMicrobiologiaBioengineeringDehydrogenaseSaccharomyces cerevisiaeProtein aggregationApplied Microbiology and BiotechnologyBiochemistryIsozyme03 medical and health scienceslcsh:TP248.13-248.65Tdh2Tdh1Tdh3Ceramide synthaseResearch ArticlesGlyceraldehyde 3-phosphate dehydrogenase030304 developmental biologySphingolipids0303 health sciencesbiology030306 microbiologyChemistryGlyceraldehyde-3-Phosphate Dehydrogenasesbiology.organism_classificationLipidsSphingolipidYeastIsoenzymesMetabolismBiochemistrybiology.proteinGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Protein aggregationEnzimsGlycolysisFlux (metabolism)Research ArticleBiotechnologyMicrobial Biotechnology
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Starvation and temperature upshift cause an increase in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protei…

2003

The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase (cwGAPDH) activity in Saccharomyces cerevisiae increases (two- to 10-fold, depending on the strain) in response to starvation and temperature upshift. Assays using transformants carrying pTDH, a yeast centromer derivative plasmid containing the Candida albicans TDH3 gene (encoding GAPDH) fused in frame with the yeast SUC2-coding region for internal invertase, showed that starvation and/or temperature upshift result in a similar increase in both cwGAPDH and cell wall-associated invertase activities. In addition, this incorporation of GAPDH protein into the cell wall in response to stress does not require (i) de novo protein sy…

Saccharomyces cerevisiaeDehydrogenaseSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyMicrobiologyFungal ProteinsCell WallGene Expression Regulation FungalCandida albicansCandida albicansGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationTemperatureGlyceraldehyde-3-Phosphate DehydrogenasesGeneral Medicinebiology.organism_classificationMolecular biologyYeastCytosolEnzymeInvertasechemistryBiochemistryStarvationbiology.proteinFEMS Yeast Research
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Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde-3-phosphate dehydr…

2003

We have checked the ability of the Candida albicans GAPDH polypeptide, which lacks a conventional N-terminal signal peptide, to reach the cell wall in Saccharomyces cerevisiae by using an intracellular form of the yeast invertase as a reporter protein. A hybrid TDH3-SUC2 gene containing the C. albicans TDH3 promoter sequences and a coding region encoding a fusion protein formed by the C. albicans GAPDH polypeptide, fused at its C-terminus with the yeast internal invertase, was constructed in a centromer derivative plasmid and transformed into a Suc(-) S. cerevisiae strain. Transformants displayed invertase activity measured in intact whole cells, and were able to grow on sucrose as the sole…

Signal peptideSaccharomyces cerevisiae ProteinsGlycoside HydrolasesSaccharomyces cerevisiaeMolecular Sequence DataBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryGene productFungal ProteinsTransformation Geneticstomatognathic systemCell WallGene Expression Regulation FungalCandida albicansGeneticsAmino Acid SequenceCandida albicansDNA FungalPeptide sequenceGlyceraldehyde 3-phosphate dehydrogenaseBase Sequencebeta-FructofuranosidaseMembrane ProteinsRNA Fungalbiology.organism_classificationBlotting NorthernMolecular biologyFusion proteinRecombinant ProteinsInvertaseBiochemistrybiology.proteinGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)BiotechnologyPlasmidsYeast (Chichester, England)
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Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability

2008

17 pages.-- PMID: 18809573 [PubMed].-- Printed version published on Dec 2008.

Untranslated regionUmbilical VeinsRNA StabilityRNA StabilityGlyceraldehyde-3'-phosphate dehydrogenase (GAPDH)Plasma protein bindingstomatognathic systemHumansmRNA stabilityS-Glutathionylation3' Untranslated RegionsMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseRegulation of gene expressionMessenger RNAEndothelin-1biologyThree prime untranslated regionGlyceraldehyde-3-Phosphate DehydrogenasesArticlesCell BiologyGlutathioneOxidative StressGene Expression RegulationBiochemistryEndothelin-1 (ET-1)biology.proteinOxidation-ReductionProtein Binding
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The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM/MM approach

2013

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been identified as a key enzyme involved in glycolysis processes for energy production in the Trypanosoma cruzi parasite. This enzyme catalyses the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) in the presence of inorganic phosphate (Pi) and nicotinamide adenosine dinucleotide (NAD+). The catalytic mechanism used by GAPDH has been intensively investigated. However, the individual roles of Pi and the C3 phosphate of G3P (Ps) sites, as well as some residues such as His194 in the catalytic mechanism, remain unclear. In this study, we have employed Molecular Dynamics (MD) simulations within hybrid quantum mechanical/molecular …

biocatalysisEnzims proteolíticsParàsitsStereochemistryTrypanosoma cruziGeneral Physics and AstronomyDehydrogenaseMolecular Dynamics SimulationNicotinamide adenine dinucleotideOxidative PhosphorylationSubstrate Specificityglyceraldehyde 3 phosphate dehydrogenaseQM/MMchemistry.chemical_compoundstomatognathic systemGlyceraldehydePhysical and Theoretical Chemistrynicotinamide adenine dinucleotideGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationbiologyGlyceraldehyde-3-Phosphate DehydrogenasesActive siteNADmolecular dynamicsEnzymechemistryBiochemistryBiocatalysisbiology.proteinQuantum TheoryNAD+ kinaseOxidation-ReductionPhysical Chemistry Chemical Physics
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The Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase activity increases in response to starvation and temperature upshi…

2002

We have determined the effect of environmental factors (mild thermal upshift and starvation) on the Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase (cwGAPDH) activity. Temperature upshift (from 28 to 37 degrees C) and/ or starvation (at 28 or 37 degrees C in water) of exponentially growing yeast cells caused an increase in cwGAPDH activity (3 to 5-, and 7 to 8-fold, respectively). This increase in activity did not correlate with an increase in the amount of cwGAPDH protein present, as determined by flow cytometry, immunoelectron microscopy and Western-blotting. These results indicate that thermal upshift and starvation cause an activation of the cwGAPDH in C. …

biologymedicine.diagnostic_testImmunoelectron microscopyTemperatureGlyceraldehyde-3-Phosphate DehydrogenasesDehydrogenaseGeneral Medicinebiology.organism_classificationYeastCorpus albicansFlow cytometryCell wallFungal ProteinsInfectious DiseasesBiochemistryCell WallCandida albicansbiology.proteinmedicineCandida albicansGlyceraldehyde 3-phosphate dehydrogenaseMedical mycology
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Prolonging in utero-like oxygenation after birth diminishes oxidative stress in the lung and brain of mice pups☆

2013

Background Fetal-to-neonatal transition is associated with oxidative stress. In preterm infants, immaturity of the antioxidant system favours supplemental oxygen-derived morbidity and mortality. Objectives To assess if prolonging in utero-like oxygenation during the fetal-to-neonatal transition limits oxidative stress in the lung and brain, improving postnatal adaptation of mice pups. Material and methods Inspiratory oxygen fraction (FiO2) in pregnant mice was reduced from 21% (room air) to 14% (hypoxia) 8–12 h prior to delivery and reset to 21% 6–8 h after birth. The control group was kept at 21% during the procedure. Reduced (GSH) and oxidized (GSSG) glutathione and its precursors [γ-glut…

gsr (glutathione reductase gene)pgd phosphogluconate dehydrogenase geneGPX1FiO2 inspiratory oxygen fractionγ-GC (gamma-glutamyl cysteine)PhysiologyBiochemistryMice0302 clinical medicinePregnancyquinone oxidoreductase 1) [noq1 (NAD(P)H]NAD(P)H Dehydrogenase (Quinone)gapdh glyceraldehyde-3-phosphate dehydrogenase geneP7 1 week after birthGSH (reduced glutathione)Oxidoreductases Acting on Sulfur Group Donorsme1 (malic enzyme 1 gene)glutathioneLungSpO2 oxygen saturationlcsh:QH301-705.5γ-GC–NEM gamma-glutamyl cysteine covalently bonded to N-ethylmaleimidechemistry.chemical_classification0303 health sciencesGSSG oxidized glutathioneGlutathione peroxidaseO14 (hypoxia group FiO2=14%)Brainm/z mass-to-charge ratioG18 18th day of gestationCell Hypoxia3. Good healthpgd (phosphogluconate dehydrogenase gene)In uterogclm glutamylcysteine ligase modifier subunit genesrnx1 sulfiredoxin 1 genelcsh:Medicine (General)me1 malic enzyme 1 genesrnx1 (sulfiredoxin 1 gene)gclm (glutamylcysteine ligase modifier subunit gene)γ-GC–NEM (gamma-glutamyl cysteine covalently bonded to N-ethylmaleimide)trxnd1 (thioredoxin reductase 1 gene)redox regulation03 medical and health sciencesnoq1 NAD(P)H:quinone oxidoreductase 1γ-GC gamma-glutamyl cysteineCySH L-cysteinePregnancyg6pdx (glucose 6 phosphate dehydrogenase gene)GlutathioneOxygenationgapdh (glyceraldehyde-3-phosphate dehydrogenase gene)medicine.diseaseMice Inbred C57BLOxygenP1 24 h after birthGCL glutamylcysteine ligasechemistryOxidative stressRedox regulationNEM (N-ethylmaleimide)O14 hypoxia group (FiO2=14%)GSH reduced glutathioneClinical Biochemistrymedicine.disease_causechemistry.chemical_compoundGlutathione Peroxidase GPX1GS–NEM reduced glutathione covalently bonded to N-ethylmaleimideSpO2 (oxygen saturation)oxidative stressg6pdx glucose 6 phosphate dehydrogenase genelcsh:R5-920GSSG (oxidized glutathione)G18 (18th day of gestation)gsr glutathione reductase geneGlutathionegpx1 glutathione peroxidase 1 genemedicine.anatomical_structurem/z (mass-to-charge ratio)LC–MS/MS (liquid chromatography coupled to tandem mass spectrometry)FemaleLC–MS/MS liquid chromatography coupled to tandem mass spectrometryO21 (normoxia group FiO2=21%)paO2 (partial pressure of oxygen)gpx1 (glutathione peroxidase 1 gene)Research Papernoq1 (NAD(P)H:quinone oxidoreductase 1)CySH (l-cysteine)FiO2 (inspiratory oxygen fraction)CyS–NEM (cysteine covalently bonded to N-ethylmaleimide)030225 pediatricsmedicineP7 (1 week after birth)AnimalsGCL (glutamylcysteine ligase)P1 (24 h after birth)O21 normoxia group (FiO2=21%)CyS–NEM cysteine covalently bonded to N-ethylmaleimide030304 developmental biologyGlutathione PeroxidaseLungOrganic ChemistryGS–NEM (reduced glutathione covalently bonded to N-ethylmaleimide)trxnd1 thioredoxin reductase 1 geneMolecular biologypaO2 partial pressure of oxygenAnimals NewbornGene Expression Regulationlcsh:Biology (General)NEM N-ethylmaleimidefetal-to-neonatal transitionoxygenOxidative stressFetal-to-neonatal transition
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