Search results for "PHOSPHATASE"

showing 10 items of 499 documents

The inorganic polymer, polyphosphate, blocks binding of SARS-CoV-2 spike protein to ACE2 receptor at physiological concentrations

2020

Graphical abstract The inorganic physiological polymer, polyphosphate, blocks binding of SARS-CoV-2 spike protein to ACE2 receptor at physiological concentrations. This discovery proposes polyphosphate as a new member of the host's antiviral innate immune defense.

Models Molecular0301 basic medicineAntiviral AgentsBiochemistryArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolyphosphatesPolyphosphateHuman Umbilical Vein Endothelial Cellsotorhinolaryngologic diseasesHumansPlateletReceptorneoplasmsPharmacologychemistry.chemical_classificationBinding assayInnate immune systemSARS-CoV-2 spike S-proteinLigand binding assayPolyphosphateCOVID-19pathological conditions signs and symptomsdigestive system diseasesCOVID-19 Drug TreatmentAmino acidsurgical procedures operative030104 developmental biologyEnzymechemistryBiochemistry030220 oncology & carcinogenesisSpike Glycoprotein CoronavirusNanoparticlesAlkaline phosphataseAngiotensin-Converting Enzyme 2Protein BindingReceptors CoronavirusBiochemical Pharmacology
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Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis

2008

We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile D9, and several other residues potentially implicated in substrate turnover and/or Mg(2+) binding. To enlighten the catalytic mechanism of dephosphorylation, we constructed sEH phosphatase active-site mutants by site-directed mutagenesis. A total of 18 mutants were constructed and recombinantly expressed in Escherichia coli as soluble pro…

Models MolecularEpoxide hydrolase 2Molecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthMass SpectrometryPhosphatesDephosphorylation1315 Structural BiologyProtein structureStructural Biology1312 Molecular BiologyHumansPhosphofructokinase 2Amino Acid SequenceBinding siteProtein Structure QuaternarySite-directed mutagenesisMolecular BiologyEpoxide HydrolasesBinding SitesChemistrySubstrate (chemistry)Phosphoric Monoester HydrolasesRecombinant ProteinsProtein Structure TertiaryProtein SubunitsBiochemistryMutagenesis Site-Directed570 Life sciences; biologyDimerizationSequence AlignmentChromatography Liquid
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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Promiscuity in alkaline phosphatase superfamily. Unraveling evolution through molecular simulations.

2011

We here present a theoretical study of the alkaline hydrolysis of a phosphodiester (methyl p-nitrophenyl phosphate or MpNPP) in the active site of Escherichia coli alkaline phosphatase (AP), a monoesterase that also presents promiscuous activity as a diesterase. The analysis of our simulations, carried out by means of molecular dynamics (MD) simulations with hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, shows that the reaction takes place through a D(N)A(N) or dissociative mechanism, the same mechanism employed by AP in the hydrolysis of monoesters. The promiscuous activity observed in this superfamily can be then explained on the basis of a conserved reaction mechanism. …

Models MolecularReaction mechanismStereochemistrydnaNAlkaline hydrolysis (body disposal)AlkaliesMolecular Dynamics SimulationBiochemistryMolecular mechanicsCatalysisMolecular dynamicsColloid and Surface ChemistryCatalytic DomainphosphodiesterEscherichia colibiologyChemistryHydrolysisActive siteGeneral ChemistryAlkaline PhosphataseEnzymesEnzyme ActivationPhosphodiester bondbiology.proteinAlkaline phosphataseQuantum Theoryalkaline phosphataseJournal of the American Chemical Society
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Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli.

2011

C(4)-Dicarboxylate uptake transporter B (DcuB) of Escherichia coli is a bifunctional transporter that catalyzes fumarate/succinate antiport and serves as a cosensor of the sensor kinase DcuS. Sites and domains of DcuB were analyzed for their topology relative to the cytoplasmic or periplasmic side of the membrane and their accessibility to the water space. For the topology studies, DcuB was fused at 33 sites to the reporter enzymes PhoA and LacZ that are only active when located in the periplasm or the cytoplasm, respectively. The ratios of the PhoA and LacZ activities suggested the presence of 10 or 11 hydrophilic loops, and 11 or 12 α-helical transmembrane domains (TMDs). The central part…

Models MolecularRecombinant Fusion ProteinsMolecular Sequence Datalac operonTopologyBiochemistryProtein Structure SecondaryPolyethylene GlycolsProtein structureBacterial ProteinsCatalytic DomainStilbenesAmino Acid SequenceCysteineBinding sitePeptide sequenceDicarboxylic Acid TransportersEscherichia coli K12ChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceAlkaline PhosphataseTransmembrane domainMembrane proteinBiochemistryLac OperonEthylmaleimideSulfonic AcidsHydrophobic and Hydrophilic InteractionsCysteineBiochemistry
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Reversed Enantioselectivity of Diisopropyl Fluorophosphatase against Organophosphorus Nerve Agents by Rational Design

2009

Diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is an efficient and robust biocatalyst for the hydrolysis of a range of highly toxic organophosphorus compounds including the nerve agents sarin, soman, and cyclosarin. In contrast to the substrate diisopropyl fluorophosphate (DFP) the nerve agents possess an asymmetric phosphorus atom, which leads to pairs of enantiomers that display markedly different toxicities. Wild-type DFPase prefers the less toxic stereoisomers of the substrates which leads to slower detoxification despite rapid hydrolysis. Enzyme engineering efforts based on rational design yielded two quadruple enzyme mutants with reversed enantioselectivity and overall en…

Models MolecularSarinStereochemistryRational designCyclosarinStereoisomerismGeneral ChemistryNervous SystemBiochemistryCatalysisKineticschemistry.chemical_compoundOrganophosphorus CompoundsPhosphoric Triester HydrolasesColloid and Surface ChemistrychemistrySomanHydrolasemedicineDiisopropyl fluorophosphateChemical Warfare AgentsCrystallizationDiisopropyl-fluorophosphatasemedicine.drugNerve agentJournal of the American Chemical Society
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The nuclear autoantigen La/SS-associated antigen B: One gene, three functional mRNAs

1997

Transcription of the gene encoding for the nuclear autoantigen La resulted in three mRNA forms. A promoter switching combined with an alternative splicing pathway replaced exon 1 with either exon 1´ or exon 1´´. The exon 1´´ donor splice site was located 4 nts downstream of the exon 1´ donor splice site. All three La mRNA forms were expressed in all the tissues analysed including peripheral blood lymphocytes, liver, fetal spleen, cultured primary endothelial cells, and mouse LTA cell lines permanently transfected with the human La gene. Both the exons 1´ and 1´´ had unusual structures. They contained GC-rich regions and an oligo(U)-tail of 23 uridine residues. Moreover, they encoded for thr…

Molecular Sequence DataBiologyAutoantigensPolymerase Chain ReactionBiochemistryMiceExonExon trappingAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyGeneRibonucleoproteinAdenosine TriphosphatasesMessenger RNASplice site mutationBase SequenceAlternative splicingExonsSequence Analysis DNACell BiologyMolecular biologyOpen reading frameGenetic TechniquesRibonucleoproteinsResearch ArticleTranscription Factors
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Receptor protein-tyrosine phosphatases: origin of domains (catalytic domain, Ig-related domain, fibronectin type III module) based on the sequence of…

2001

Abstract Reversible tyrosine phosphorylation of proteins is one of the major regulatory physiological events in response to cell-cell- and cell-matrix contact in Metazoa. Previously it was documented that the tyrosine phosphorylating enzymes, the tyrosine kinases (TKs), are autapomorphic characters of Metazoa, including sponges. In this paper the tyrosine dephosphorylating enzymes, the protein-tyrosine phosphatases (PTPs), are studied which can be grouped into two subfamilies, the soluble PTPs and the receptor PTPs (RPTPs). PTPs are characterized by one PTPase domain which interestingly comprises sequence similarity to yeast PTPs. In contrast to the PTPs, the RPTPs – which have been found o…

Molecular Sequence DataImmunoglobulinsBiologyPolymerase Chain ReactionEvolution Molecularchemistry.chemical_compoundCatalytic DomainGene duplicationGeneticsAnimalsAmino Acid SequenceTyrosineCloning MolecularPhylogenychemistry.chemical_classificationPhylogenetic treeSequence Homology Amino AcidTyrosine phosphorylationGeneral MedicineProtein-Tyrosine KinasesAmino acidFibronectinsPoriferaProtein Structure TertiaryOpen reading framechemistryBiochemistryPhosphorylationProtein Tyrosine PhosphatasesTyrosine kinaseSequence AnalysisGene
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The phosphorylated pathway of serine biosynthesis is essential both for male gametophyte and embryo development and for root growth in Arabidopsis.

2013

This study characterizes the phosphorylated pathway of Ser biosynthesis (PPSB) in Arabidopsis thaliana by targeting phosphoserine phosphatase (PSP1), the last enzyme of the pathway. Lack of PSP1 activity delayed embryo development, leading to aborted embryos that could be classified as early curled cotyledons. The embryo-lethal phenotype of psp1 mutants could be complemented with PSP1 cDNA under the control of Pro35S (Pro35S:PSP1). However, this construct, which was poorly expressed in the anther tapetum, did not complement mutant fertility. Microspore development in psp1.1/psp1.1 Pro35S:PSP1 arrested at the polarized stage. The tapetum from these lines displayed delayed and irregular devel…

MutantCitric Acid CycleGreen Fluorescent ProteinsImmunoblottingArabidopsisPlant ScienceBiologyPlant RootsSerineMicrosporeMicroscopy Electron TransmissionGene Expression Regulation PlantArabidopsisSerineArabidopsis thalianaAmino AcidsPhosphorylationResearch ArticlesTapetumArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionGene Expression Regulation DevelopmentalEmbryoPhosphoserine phosphataseCell Biologybiology.organism_classificationPlants Genetically ModifiedPhosphoric Monoester HydrolasesBiosynthetic PathwaysBiochemistryMicroscopy FluorescenceMutationSeedsPollenGlycolysisThe Plant cell
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Determining a healthy reference range and factors potentially influencing PRO-C3 – A biomarker of liver fibrosis

2021

Background & Aims Progressive fibrosis has been identified as the major predictor of mortality in patients with non-alcoholic fatty liver disease (NAFLD). Several biomarkers are currently being evaluated for their ability to substitute the liver biopsy as the reference standard. Recent clinical studies in NAFLD/NASH patients support the utility of PRO-C3, a marker of type III collagen formation, as a marker for the degree of fibrosis, disease activity, and effect of treatment. Here we establish the healthy reference range, optimal sample handling conditions for both short- and long-term serum storage, and robustness for the PRO-C3 assay. Methods PRO-C3 was measured in 269 healthy volunteers…

NASH-CRN NASH Clinical Research NetworkBiopsyDiseaseAST aspartate aminotransferaseRC799-869Ethnic groupsGastroenterologyNIMBLE Non-Invasive Biomarkers of Metabolic Liver Disease (consortium)FibrosisImmunology and AllergyBody mass indexmedicine.diagnostic_testFatty liverNAS NAFLD Activity ScoreGastroenterologyDiseases of the digestive system. GastroenterologyHospitalsNPV negative predictive valueLiver biopsyBiomarker (medicine)Research Articlemedicine.medical_specialtyNAFLD non-alcoholic fatty liver diseaseADAM A Disintegrin and MetalloproteasesNASH non-alcoholic steatohepatitisReference rangeReference valuesAUROC area under the receiver operating characteristics curveInternal medicineALT alanine aminotransferaseBiopsyInternal MedicinemedicineHumansFIB-4 fibrosis-4Healthy volunteersHepatologyALP alkaline phosphatasebusiness.industryCLSI Clinical and Laboratory Standards InstituteT2DM type 2 diabetes mellitusELF™ test Enhanced Liver Fibrosis testmedicine.diseaseLITMUS Liver Investigation: Testing Marker Utility in Steatohepatitis (consortium)Collagen type IIIFibrosisPPV positive predictive valueReference standardsbusinessBody mass indexBiomarkersNon-alcoholic fatty liver disease
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