Search results for " phosphatase"

showing 10 items of 329 documents

The Histidinol Phosphate Phosphatase Involved in Histidine Biosynthetic Pathway Is Encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)

2008

Through the screening of a Streptomyces coelicolor genomic library, carried out in a histidinol phosphate phosphatase (HolPase) deficient strain, SCO5208 was identified as the last unknown gene involved in histidine biosynthesis. SCO5208 is a phosphatase, and it can restore the growth in minimal medium in this HolPase deficient strain when cloned in a high or low copy number vector. Moreover, it shares sequence homology with other HolPases recently identified in Actinobacteria. During this work a second phosphatase, SCO2771, sharing no homologies with SCO5208 and all so far described phosphatases was identified. It can complement HolPase activity mutation only at high copy number. Sequence …

Sequence analysisPhosphataseDNA Mutational AnalysisMolecular Sequence DataMutation MissenseStreptomyces coelicolormedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyBacterial ProteinsHistidinol Phosphate Phosphatase Histidine Biosynthesis Streptomyces coelicolormedicineGenomic libraryHistidineAmino Acid SequenceGeneHistidineGeneticsMutationbiologySequence Homology Amino AcidStreptomyces coelicolorGenetic Complementation TestHistidinol-PhosphataseGeneral Medicinebiology.organism_classificationBiosynthetic PathwaysBiochemistryMutant ProteinsLow copy number
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Serine/threonine protein phosphatase PP2A as a relevant target of disulphide stress in acute pancreatitis

2016

SerineBiochemistryChemistryPhysiology (medical)PhosphatasemedicineAcute pancreatitisProtein phosphatase 2ThreonineReceptor protein serine/threonine kinasemedicine.diseaseBiochemistryFree Radical Biology and Medicine
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Effect of rhamnolipids on microbial biomass content and biochemical parameters in soil contaminated with coal tar creosote

2019

AbstractThe objective of the present study was to compare the effect of rhamnolipids on the microbial biomass content and the activity of dehydrogenases (DHA), acid phosphatase (ACP), alkaline phosphatase (ALP), and urease (URE) in soil contaminated with two types of coal tar creosote: type C and type GX-Plus. The experiment was carried out on samples of sandy clay loam under laboratory conditions. Coal tar creosote was added to soil samples at a dose of 0 and 10 g·kg−1 DM, along with rhamnolipids at a dose of 0, 10, 100, and 1000 mg·kg−1 DM. The humidity of the samples was brought to 60% maximum water holding capacity, and the samples were incubated at 20°C. Microbial and biochemical param…

Soil testUreaseQH301-705.5polycyclic aromatic hydrocarbonsBiomass010501 environmental sciencescomplex mixtures01 natural sciencesGeneral Biochemistry Genetics and Molecular Biologylaw.inventionBioremediationbioremediationlawmedicineBiology (General)Coal tarsandy clay loampolycycli aromatic hydrocarbons0105 earth and related environmental sciencesGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceAcid phosphatase04 agricultural and veterinary sciencessoil enzymatic activityCreosoteEnvironmental chemistryLoam040103 agronomy & agriculturebiology.protein0401 agriculture forestry and fisheriesGeneral Agricultural and Biological SciencesResearch Articlemedicine.drugOpen Life Sciences
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Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone.

2013

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation.…

SpermidineProtein tyrosine phosphataseBiochemistryAnalytical Chemistry0302 clinical medicinePhosphorylationDatabases Protein0303 health sciencesProtein Tyrosine Phosphatase Non-Receptor Type 2biologyChemistrySmall molecule3. Good healthCell biologyisothermal titration calorimetryMolecular Docking Simulationmolecular dynamics simulation030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingThermodynamicsHydrophobic and Hydrophilic InteractionsProtein BindingSignal TransductionCell signalingintegrinIntegrinPhosphataseStatic ElectricityBiophysicsAntineoplastic AgentsMolecular Dynamics Simulationta3111mitoxantroneIntegrin alpha1beta1Small Molecule Libraries03 medical and health sciencesSDG 3 - Good Health and Well-beingdifferential scanning fluorimetryHumansBinding siteMolecular Biology030304 developmental biologyT-cell protein tyrosine phosphataseta1182ta3122In vitroProtein Structure TertiaryKineticsCytoplasmbiology.proteinMitoxantronePeptidesBiochimica et Biophysica Acta: Proteins and Proteomics
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A subunit of eukaryotic translation initiation factor 2α-phosphatase (CreP/PPP1R15B) regulates membrane traffic.

2012

The constitutive reverter of eIF2α phosphorylation (CReP)/PPP1r15B targets the catalytic subunit of protein phosphatase 1 (PP1c) to phosphorylated eIF2α (p-eIF2α) to promote its dephosphorylation and translation initiation. Here, we report a novel role and mode of action of CReP. We found that CReP regulates uptake of the pore-forming Staphylococcus aureus α-toxin by epithelial cells. This function was independent of PP1c and translation, although p-eIF2α was involved. The latter accumulated at sites of toxin attack and appeared conjointly with α-toxin in early endosomes. CReP localized to membranes, interacted with phosphomimetic eIF2α, and, upon overexpression, induced and decorated a pop…

Staphylococcus aureusanimal structuresEndosomePopulationPhosphataseBacterial ToxinsEukaryotic Initiation Factor-2EndosomesBiologyBiochemistryExocytosisProtein Structure SecondaryEukaryotic translationProtein Phosphatase 1Initiation factorAnimalsHumansPhosphorylationeducationPeptide Chain Initiation TranslationalMolecular Biologyeducation.field_of_studyCell MembraneTranslation (biology)Epithelial CellsCell BiologyCell biologyProtein Structure TertiaryProtein TransportPhosphorylationRabbitsK562 CellsThe Journal of biological chemistry
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Reaction Rate Modeling in Cryoconcentrated Solutions: Alkaline Phosphatase Catalyzed DNPP Hydrolysis

2000

The hydrolysis of disodium p-nitrophenyl phosphate catalyzed by alkaline phosphatase was chosen as a model to study the kinetics of changes in frozen food products. The initial reaction rate was determined in concentrated sucrose solutions down to -24 degrees C, and the enzymatic characteristics K(M) and V(max) were calculated. The experimental data were compared to the kinetics predicted by assuming that the reaction was viscosity dependent. Indeed, an analysis of the enzymatic reaction demonstrated that both the diffusion of the substrate and the flexibility of the enzyme segments were controlled by the high viscosity of the media. When the temperature was too low for the viscosity to be …

StereochemistryChemistryHydrolysisDiffusionInorganic chemistryKineticsTemperatureSubstrate (chemistry)Concentration effectGeneral ChemistryAlkaline PhosphataseCatalysisCatalysisNitrophenolsSolutionsReaction rateViscosityOrganophosphorus CompoundsGeneral Agricultural and Biological SciencesGlass transitionJournal of Agricultural and Food Chemistry
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The mechanism of hydrolysis of beta-glycerophosphate by kidney alkaline phosphatase.

1975

1. To identify the functional groups that are involved in the conversion of β-glycerophosphate by alkaline phosphatase (EC 3.1.3.1) from pig kidney, the kinetics of alkaline phosphatase were investigated in the pH range 6.6-10.3 at substrate concentrations of 3 μM-30 mM. From the plots of log ṼH+ against pH and log ṼH+/KH+m against pH one functional group with pK = 7.0 and two functional groups with pK = 9.1 were identified. These groups are involved in substrate binding. Another group with pK = 8.8 was found, which in its unprotonated form catalyses substrate conversion. 2. GSH inhibits the alkaline phosphatase reversibly and non-competitively by attacking the bound Zn(II). 3. The influenc…

StereochemistrySwineKidneyBiochemistrychemistry.chemical_compoundHydrolysisAnimalsMagnesiumBinding siteMolecular Biologychemistry.chemical_classificationBinding SitesHydrolysisSubstrate (chemistry)Cell BiologyGlutathioneHydrogen-Ion ConcentrationPhosphateAlkaline PhosphataseGlutathioneKineticsZincEnzymechemistryModels ChemicalGlycerophosphatesFunctional groupAlkaline phosphataseResearch ArticleThe Biochemical journal
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The Marine Sponge-Derived Inorganic Polymers, Biosilica and Polyphosphate, as Morphogenetically Active Matrices/Scaffolds for the Differentiation of …

2014

The two marine inorganic polymers, biosilica (BS), enzymatically synthesized from ortho-silicate, and polyphosphate (polyP), a likewise enzymatically synthesized polymer consisting of 10 to >100 phosphate residues linked by high-energy phosphoanhydride bonds, have previously been shown to display a morphogenetic effect on osteoblasts. In the present study, the effect of these polymers on the differential differentiation of human multipotent stromal cells (hMSC), mesenchymal stem cells, that had been encapsulated into beads of the biocompatible plant polymer alginate, was studied. The differentiation of the hMSCs in the alginate beads was directed either to the osteogenic cell lineage by …

Stromal cellAlginatesPolymersCellular differentiationOsteogenesis DistractionPharmaceutical ScienceBone Morphogenetic Protein 2biosilica; polyphosphate; multipotent stromal cells; mesenchymal stem cells; alkaline phosphatase; 3D cell/tissue printing; distraction osteogenesisBone morphogenetic protein 2ChondrocyteArticleCollagen Type IGlucuronic AcidPolyphosphatesDrug Discoverymedicinemultipotent stromal cellsAnimalsHumansbiosilicaPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Collagen Type IImesenchymal stem cells3D cell/tissue printingOsteoblastsTissue ScaffoldsChemistryHexuronic AcidsMesenchymal stem cellBiomaterialpolyphosphateCell DifferentiationAnatomyChondrogenesisAlkaline PhosphataseSilicon DioxideCell biologyPoriferamedicine.anatomical_structuredistraction osteogenesislcsh:Biology (General)Alkaline phosphataseMarine Drugs
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The influence of bone allograft processing on osteoblast attachment and function

2004

In order to assess the influence of eight different sterilisation and disinfection methods for bone allografts on adhesion, proliferation, and differentiation of human bone marrow stromal cells (BMSC), cells were grown in culture and then plated onto pieces of human bone allografts. Following processing methods were tested: autoclavation (AUT), low-temperature-plasma sterilisation of demineralised allografts (D-LTP), ethylene oxide sterilisation (EtO), fresh frozen bone (FFB), 80 degrees C-thermodisinfection (80 degrees C), gamma-irradiation (Gamma), chemical solvent disinfection (CSD), and Barrycidal-disinfection (BAR). The seeding efficiency was determined after one hour to detect the num…

Stromal cellCell Survivalmedicine.medical_treatmentOsteocalcinPopulationGene ExpressionBone Marrow CellsIn Vitro TechniquesBone graftingAndrologyCell AdhesionmedicineHumansTransplantation HomologousOrthopedics and Sports MedicineViability assayCell adhesioneducationCells CulturedBone Marrow Transplantationeducation.field_of_studyOsteoblastsbiologyChemistrySterilizationCell DifferentiationOsteoblastAlkaline PhosphataseTransplantationmedicine.anatomical_structureImmunologyOsteocalcinbiology.proteinStromal CellsCell DivisionJournal of Orthopaedic Research
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Inhibition of B2 receptor internalization delays its dephosphorylation

1997

SucroseReceptor Bradykinin B2Immunoprecipitationmedia_common.quotation_subjectBradykininBradykininCell LineDephosphorylationRadioligand Assaychemistry.chemical_compoundOkadaic AcidConcanavalin APhosphoprotein PhosphatasesHumansEnzyme InhibitorsPhosphorylationInternalizationOxazolesBradykinin Receptor AntagonistsSkinmedia_commonPharmacologyChemistryReceptors BradykininOkadaic acidFibroblastsPrecipitinPrecipitin TestsRadioligand AssayBiochemistryCantharidinIrritantsAutoradiographyPhosphorylationElectrophoresis Polyacrylamide GelMarine ToxinsImmunopharmacology
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