Search results for "Phosphotransferase"

showing 10 items of 52 documents

Evidence of a New MoYpd1p Phosphotransferase Isoform in the Multistep Phosphorelay System of Magnaporthe oryzae

2021

Different external stimuli are perceived by multiple sensor histidine kinases and transmitted by phosphorylation via the phosphotransfer protein Ypd1p in the multistep phosphorelay system of the high osmolarity glycerol signaling pathway of filamentous fungi. How the signal propagation takes place is still not known in detail since multiple sensor histidine kinase genes in most filamentous fungi are coded in the genome, whereas only one gene for Ypd1p exists. That raises the hypothesis that various Ypd1p isoforms are produced from a single gene sequence, perhaps by alternative splicing, facilitating a higher variability in signal transduction. We found that the mRNA of MoYPD1 in the rice bl…

Microbiology (medical)Gene isoformQH301-705.5MutantPlant ScienceBiology<i>Magnaporthe oryzae</i>Phosphotransferasealternative splicingphosphotransferComplementary DNAanatomy_morphologyBiology (General)GeneEcology Evolution Behavior and SystematicsCommunicationAlternative splicingHistidine kinasephosphorelayhigh osmolarity glycerol (HOG) pathwayMagnaporthe oryzaeCell biologyProteomehistidine kinasesYPD1signalingsignal transductionJournal of Fungi
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Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder.

2014

Background: Mutations in phosphomannomutase2 cause glycosylation disorder, a disease without a cure that will largely benefit from accurate ligand-bound models. Results: We obtained two models of phospomannomutase2 bound to glucose 1,6-bisphosphate and validated them with limited proteolysis. Conclusion: Ligand binding induces a large conformational transition in PMM2. Significance: We produce and validate closed-form models of PMM2 that represent a starting point for rational drug discovery.

Models MolecularPELEGlycosylationProtein Conformation1Molecular Sequence DataGlucose-6-PhosphateGlycosylation Inhibitor6-bisphosphate; PELE; computer modeling; drug discovery; glycosylation; glycosylation inhibitor; ligand-binding protein; phosphomannomutaseLigandsDrug DiscoveryAnimalsHumansAmino Acid Sequence16-BisphosphateProtein UnfoldingTemperatureLigand-binding Proteinphosphomannomutase 2 and mass spectrometryPhosphotransferases (Phosphomutases)PhosphomannomutaseMutationProteolysisMetabolism Inborn ErrorsMolecular BiophysicsPeptide HydrolasesProtein BindingComputer ModelingThe Journal of biological chemistry
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Evolution of arginine deiminase (ADI) pathway genes

2002

We have analyzed the evolution of the three genes encoding structural enzymes of the arginine deiminase (ADI) pathway, arginine deiminase (ADI), ornithine transcarbamoylase (OTC), and carbamate kinase (CK) in a wide range of organisms, including Archaea, Bacteria, and Eukarya. This catabolic route was probably present in the last common ancestor to all the domains of life. The results obtained indicate that these genes have undergone a complex evolutionary history, including horizontal transfer events, duplications, and losses. Therefore, these genes are not adequate to infer organismal relationships at deep branching levels, but they provide an insight into how catabolic genes evolved and …

Most recent common ancestorHydrolasesMolecular Sequence DataBiologyModels BiologicalEvolution MolecularGeneticsAmino Acid SequenceMolecular BiologyArginine deiminase pathwayGeneArginine deiminaseOrnithine CarbamoyltransferasePhylogenyEcology Evolution Behavior and SystematicsGeneticsLikelihood FunctionsBacteriaSequence Homology Amino AcidPhylogenetic treeCarbamate kinaseFungiSequence Analysis DNAPhosphotransferases (Carboxyl Group Acceptor)ArchaeaMetabolic pathwayHorizontal gene transferMolecular Phylogenetics and Evolution
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Nucleoside phosphotransferase in animal tissues

1984

Nucleoside phosphotransferase
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Development of nucleoside phosphotransferase activity in the cerebral hemispheres of embryonal and adult chick.

1981

In the cerebral hemispheres of the chick embryo, the level of nucleoside phosphotransferase activity is much higher than that of thymidine kinase and it increases progressively during development up to the adult stage. Therefore nucleoside phosphotransferase is not coupled with DNA synthesis.

PharmacologyAginganimal structuresNucleoside phosphotransferase activityDNA synthesisPhosphotransferasesBrainEmbryoNucleosidesCell BiologyChick EmbryoBiologyDevelopmentThymidine KinaseCellular and Molecular NeuroscienceBiochemistryThymidine kinaseembryonic structuresNucleoside phosphotransferaseMolecular MedicineAnimalsAdult stageMolecular BiologyChickensExperientia
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Effects of N2, O2'-dibutyril cyclic GMP on the nucleoside phosphotransferase activity of the retina of the chick embryos.

1977

In the retina of the chick embryo, 2 different forms of nucleoside phosphotransferase take part in the phosphorylation of thymidine. One is an unstable form with higher molecular weight. The other with lower m. wt is a stable form. This paper shows that N2, O2′-dibutyril cyclic GMP causes a marked decrement of the activity of the unstable nucleoside phosphotransferase.

PharmacologyRetinaNucleoside phosphotransferase activityPhosphotransferasesEmbryoCell BiologyChick EmbryoBiologyRetinaCellular and Molecular Neurosciencechemistry.chemical_compoundCyclic gmpmedicine.anatomical_structureBiochemistrychemistryNucleoside phosphotransferasemedicineMolecular MedicinePhosphorylationAnimalsThymidineMolecular BiologyNucleosideCyclic GMPThymidineExperientia
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Rho-mediated activation of PI(4)P5K and lipid second messengers is necessary for promotion of angiogenesis by Semaphorin 4D

2011

Phosphatidylinositol 4-phosphate 5-kinase (PI(4)P5K) is a type I lipid kinase that generates the lipid second messenger phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and functions downstream of RhoA in actin organization. It is known to play an essential role in neurite remodeling, yielding a phenotype identical to that seen in cells treated with Semaphorin 4D (Sema4D), a protein that regulates proliferation, adhesion and migration in many different cell types. Plexin-B1, the receptor for Sema4D, activates RhoA in order to generate a pro-angiogenic signal in endothelial cells. Therefore, we looked in human umbilical vein endothelial cells (HUVEC) to determine if Plexin-B1 e…

Phosphatidylinositol 45-DiphosphateCancer ResearchRHOAPhysiologyAngiogenesisSemaphorin 4DClinical BiochemistrySEMA4DNeovascularization PhysiologicNerve Tissue ProteinsReceptors Cell SurfaceSemaphorinsSynaptojaninBiologySecond Messenger SystemsArticlePI(45)P2chemistry.chemical_compoundAntigens CDRhoSettore BIO/10 - BiochimicaHumansPlexin B1PhosphatidylinositolRho-associated protein kinaseCytoskeletonrho-Associated KinasesPI(4)P5KKinaseCell biologyPhosphotransferases (Alcohol Group Acceptor)AngiogenesiHEK293 CellschemistrySecond messenger systembiology.proteinCalciumrhoA GTP-Binding ProteinAngiogenesis
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Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts

2000

The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…

Phosphatidylinositol 45-Diphosphaterac1 GTP-Binding Proteinrho GTP-Binding ProteinsBacterial ToxinsCellClostridium difficile toxin BRAC1GTPasePhospholipaseBiologyTransfectionBiochemistryMicechemistry.chemical_compoundPhosphoinositide Phospholipase CBacterial ProteinsCell AdhesionmedicineAnimalsPhosphorylationInositol phosphatechemistry.chemical_classificationPhospholipase CCytotoxinsPhosphoric Diester Hydrolases3T3 CellsMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphotransferases (Alcohol Group Acceptor)medicine.anatomical_structurechemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesCalciumSignal TransductionEuropean Journal of Biochemistry
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties.

1993

Fructose 2,6-bisphosphate is the most potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. This study was prompted by the finding that the content of fructose 2,6-bisphosphate in frog skeletal muscle was dramatically increased at the initiation of exercise and was closely correlated with the glycolytic flux during exercise. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, the enzyme system catalyzing the synthesis and degradation of fructose 2,6-bisphosphate, was purified from frog (Rana esculenta) skeletal muscle and its properties were compared with those of the rat muscle type enzyme expressed in Escherichia coli using recombinant DN…

PhysiologyPhosphofructokinase-2BiologyBiochemistrychemistry.chemical_compoundEndocrinologymedicineFructosediphosphatesAnimalsGlycolysisPhosphorylationEcology Evolution Behavior and Systematicschemistry.chemical_classificationMolecular massImmunochemistryMusclesPhosphotransferasesSkeletal muscleRana esculentaFructoseHydrogen-Ion ConcentrationMolecular WeightKineticsmedicine.anatomical_structureEnzymechemistryFructose 26-bisphosphateBiochemistryGRENOUILLEAnimal Science and ZoologyPhosphoenolpyruvate carboxykinaseProtein KinasesJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Partial purification and some properties of a nucleoside phosphotransferase of chick embryos.

1978

A nucleoside phosphotransferase purified about 40fold from chick embryos utilizes efficiently as phosphate donors deoxyribonucleoside and pyrimidine ribonucleoside monophosphates, whereas the pyrimidine deoxyribonucleoside appear to be the preferred acceptors of phosphate. The enzyme is very unstable to heat, dilution and dialysis. A marked enhancement in the stability is caused by nucleotides and it seems associated with the formation of an aggregated state of the protein.

PyrimidineDeoxyribonucleotidesChick EmbryoThymidine KinasePhosphatesSubstrate SpecificityCellular and Molecular Neurosciencechemistry.chemical_compoundNucleoside phosphotransferaseAnimalsNucleotideMolecular BiologyPharmacologychemistry.chemical_classificationPhosphotransferasesNucleosidesCell BiologyRibonucleotidesRibonucleosideChick embryosPhosphateDeoxyribonucleosideEnzymeBiochemistrychemistryMolecular MedicineExperientia
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