Search results for "kinetics"

showing 10 items of 2224 documents

Strombine dehydrogenase in the demosponge Suberites domuncula: Characterization and kinetic properties of the enzyme crucial for anaerobic metabolism

2008

Previously, the cDNA and the respective gene for a presumed tauropine dehydrogenase (TaDH) from Suberites domuncula (GenBank accession nos. AM712888, AM712889) had been annotated. The conclusion that the sequences encode a TaDH had been inferred from the 68% identity with the TaDH protein from the marine demosponge Halichondria japonica. However, subsequent enzymatic assays shown here indicate that the presumed S. domuncula opine dehydrogenase is in fact a strombine dehydrogenase (StDH). The enzyme StDH is highly specific for glycine and is inhibited by an excess of the substrate pyruvate. Besides kinetic data, we report in this study also on the predicted tertiary and quaternary structure …

Models MolecularPhysiologyGlycineDehydrogenaseBiochemistrySubstrate SpecificityComplementary DNAPyruvic AcidAnimalsAnaerobiosisProtein Structure QuaternaryMolecular Biologychemistry.chemical_classificationOxidoreductases Acting on CH-NH Group DonorsStrombine dehydrogenasebiologyTauropine dehydrogenaseAnaerobic metabolism; Demospongiae; Opine dehydrogenase; Strombine dehydrogenase; Suberites domunculabiology.organism_classificationProtein Structure TertiarySuberites domunculaKineticsEnzymechemistryBiochemistryGlycineFemaleProtein quaternary structureProtein MultimerizationSuberites
researchProduct

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
researchProduct

2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
researchProduct

Identifying three-way DNA junction-specific small-molecules

2012

Three-way junction DNA (TWJ-DNA, also known as 3WJ-DNA) is an alternative secondary DNA structure comprised of three duplex-DNAs that converge towards a single point, termed the branch point. This point is characterized by unique geometrical properties that make its specific targeting by synthetic small-molecules possible. Such a targeting has already been demonstrated in the solid state but not thoroughly biophysically investigated in solution. Herein, a set of simple biophysical assays has been developed to identify TWJ-specific small-molecule ligands; these assays, inspired by the considerable body of work that has been reported to characterize the interactions between small-molecules an…

Models MolecularPorphyrinsSolid-stateNanotechnologyComputational biology010402 general chemistryLigands01 natural sciencesBiochemistrySmall Molecule Libraries03 medical and health scienceschemistry.chemical_compoundPiperidinesFluorescence Resonance Energy TransferTransition TemperatureComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesAza CompoundsSpectrum AnalysisGeneral MedicineDNASmall moleculePorphyrin0104 chemical sciencesG-QuadruplexesSolutions[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsKineticschemistryMetalsThree wayQuinolinesThermodynamicsSingle pointDNA
researchProduct

Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: Inhibition kinetics and docking studies

2014

NS2B-NS3 is a serine protease of the Dengue virus considered a key target in the search for new antiviral drugs. In this study flavonoids were found to be inhibitors of NS2B-NS3 proteases of the Dengue virus serotypes 2 and 3 with IC50 values ranging from 15 to 44 μM. Agathisflavone (1) and myricetin (4) turned out to be noncompetitive inhibitors of dengue virus serotype 2 NS2B-NS3 protease with Ki values of 11 and 4.7 μM, respectively. Docking studies propose a binding mode of the flavonoids in a specific allosteric binding site of the enzyme. Analysis of biomolecular interactions of quercetin (5) with NT647-NHS-labeled Dengue virus serotype 3 NS2B-NS3 protease by microscale thermophoresis…

Models MolecularProteasesSerine Proteinase Inhibitorsvirusesmedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceDengue virusmedicine.disease_causeAntiviral AgentsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoverymedicineMolecular BiologyFlavonoidsSerine proteaseNS3ProteasebiologyMicroscale thermophoresisSerine EndopeptidasesOrganic ChemistryDengue VirusVirologyMolecular Docking SimulationKineticschemistryBiochemistryDocking (molecular)biology.proteinMolecular MedicineMyricetinBioorganic & Medicinal Chemistry
researchProduct

Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases.

2020

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors …

Models MolecularProtein Conformation alpha-HelicalMolecular modelStereochemistryPhosphorous AcidsSwinePhenylalaninelcsh:QR1-502PhenylalanineCD13 Antigenscomputer-aided simulationsInhibitory postsynaptic potential01 natural sciencesBiochemistrylcsh:MicrobiologyArticlePhenylalanine derivativesSubstrate SpecificitySmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipAnimalsHumansProtein Interaction Domains and MotifsEnzyme Inhibitorsphosphonic acid inhibitorsMolecular Biology030304 developmental biologyAlaninechemistry.chemical_classification0303 health sciencesInhibitory potentialBinding Sites010405 organic chemistryChemistryAminobutyratesFluorineBromine0104 chemical sciencesIsoenzymesKineticsEnzymehuman and porcine alanine aminopeptidasefluorine and bromine substitutionThermodynamicsProtein Conformation beta-StrandProtein BindingBiomolecules
researchProduct

QM/MM calculations of kinetic isotope effects in the chorismate mutase active site.

2003

Kinetic isotope effects have been computed for the Claisen rearrangement of chorismate to prephenate in aqueous solution and in the active site of chorismate mutase from B. subtilus. These included primary 13C and 18O and secondary 3H effects for substitutions at the bond-making and bond-breaking positions. The initial structures of the putative stationary points on the potential energy surface, required for the calculations of isotope effects using the CAMVIB/CAMISO programs, have been selected from hybrid QM/MM molecular dynamical simulations using the DYNAMO program. Refinement of the reactant complex and transition-state structures has been carried out by means of AM1/CHARMM24/TIP3P cal…

Models MolecularProtein ConformationKinetic schemeBiochemistryCatalysisQM/MMIsotopesComputational chemistryKinetic isotope effectComputer SimulationPhysical and Theoretical ChemistryAqueous solutionBinding SitesbiologyChemistryOrganic ChemistryActive siteClaisen rearrangementSolutionsKineticsPotential energy surfacebiology.proteinChorismate mutaseQuantum TheoryThermodynamicsGasesSoftwareBacillus subtilisChorismate MutaseOrganicbiomolecular chemistry
researchProduct

Concentration dependent effects of commonly used pesticides on activation versus inhibition of the quince (Cydonia Oblonga) polyphenol oxidase

2009

Polyphenol oxidase (PPO) catalyzes the oxidation of o-diphenols to their respective quinones which undergo autopolymerization and form dark pigments. The interaction of PPO with various substrates and effectors remains the focus of intensive investigations due to the enzyme's key role in pigments biosynthesis including animal melanogenesis and fruit/fungi enzymatic browning. In this study, the effect of a range of commonly used pesticides on the enzyme activity has been evaluated using the purified quince (Cydonia oblonga Miller) PPO. The biochemical analysis showed that, in the presence of high pesticide concentrations, the enzyme was competitively inhibited, particularly with benomyl, car…

Models MolecularProtein ConformationMolecular Sequence DataCrystallography X-RayToxicologyPolyphenol oxidasechemistry.chemical_compoundCarbarylParathion methylAmino Acid SequenceEnzyme InhibitorsIpomoea batatasPesticidesCatechol oxidaseRosaceaeDose-Response Relationship DrugbiologyReverse Transcriptase Polymerase Chain ReactionComputational BiologyGeneral MedicineNucleic acid amplification techniqueEnzyme assayEnzyme ActivationKineticsParathionchemistryBiochemistryPolyphenolFruitbiology.proteinElectrophoresis Polyacrylamide GelNucleic Acid Amplification TechniquesCatechol OxidaseFood ScienceFood and Chemical Toxicology
researchProduct

The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study.

2021

AbstractSolvent access to the protein interior plays an important role in the function of many proteins. Phytochromes contain a specific structural feature, a hairpin extension that appears to relay structural information from the chromophore to the rest of the protein. The extension interacts with amino acids near the chromophore, and hence shields the chromophore from the surrounding solvent. We envision that the detachment of the extension from the protein surface allows solvent exchange reactions in the vicinity of the chromophore. This can facilitate for example, proton transfer processes between solvent and the protein interior. To test this hypothesis, the kinetics of the protonation…

Models MolecularProtein ConformationProtonation010402 general chemistryPhotochemistry01 natural sciencespH jump03 medical and health scienceschemistry.chemical_compoundPhytochrome ADeprotonationBacterial ProteinsPhotostationary statePhysical and Theoretical Chemistrychromophore protein systems030304 developmental biology0303 health sciencesBiliverdinBinding SitesPhytochromeProtein dynamicsBiliverdineconformational substatesChromophoreHydrogen-Ion Concentrationsolvent gating0104 chemical sciencesKineticschemistryprotein dynamicsSolventsSpectrophotometry UltravioletproteiinitvalokemiaDeinococcusPhytochromeProtonsPhotochemicalphotobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
researchProduct

NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
researchProduct