Search results for "DASE"

showing 10 items of 1891 documents

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
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Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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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
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Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.

2012

Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane. Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression. In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides. We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase…

Models MolecularProtein ConformationPlasma protein bindingCell membrane03 medical and health sciencesProtein structureZymogenAmyloid precursor proteinmedicineHumans030304 developmental biology0303 health sciencesMultidisciplinaryCrystallographybiologyChemistry030302 biochemistry & molecular biologyCell MembraneMetalloendopeptidasesSheddaseBiological SciencesTransmembrane protein3. Good healthCell biologyProtein Structure Tertiarymedicine.anatomical_structureBiochemistryEctodomainbiology.proteinDimerizationProtein BindingProceedings of the National Academy of Sciences of the United States of America
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Jararhagin-derived RKKH Peptides Induce Structural Changes in α1I Domain of Human Integrin α1β1

2003

Integrin alpha(1)beta(1) is one of four collagen-binding integrins in humans. Collagens bind to the alphaI domain and in the case of alpha(2)I collagen binding is competitively inhibited by peptides containing the RKKH sequence and derived from the metalloproteinase jararhagin of snake venom from Bothrops jararaca. In alpha(2)I, these peptides bind near the metal ion-dependent adhesion site (MIDAS), where a collagen (I)-like peptide is known to bind; magnesium is required for binding. Published structures of the ligand-bound "open" conformation of alpha(2)I differs significantly from the "closed" conformation seen in the structure of apo-alpha(2)I near MIDAS. Here we show that two peptides,…

Models MolecularProtein ConformationStereochemistryIntegrinAlpha (ethology)PeptideCrystallography X-RayBinding CompetitiveBiochemistryCollagen Type IProtein Structure SecondaryIntegrin alpha1beta1Protein structureCrotalid VenomsHumansMagnesiumAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesCalorimetry Differential ScanningMolecular StructurebiologyMetalloendopeptidasesCell BiologyPeptide FragmentsRecombinant ProteinsSpectrometry FluorescencechemistryJararhaginHelixbiology.proteinCrystallizationJournal of Biological Chemistry
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Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism

2000

The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites, although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins, and tyrosinases and catecholoxidases (commonly referred to as phenoloxidases in arthropods) catalyze the hydroxylation of monophenols or the oxidation of o-diphenols to o-quinones, or both. Tyrosinases are activated in vivo by limited proteolytic cleavage, which might open up substrate access to the catalytic site. It has recently been demonstrated that if hemocyanins are subjected to similar proteolytic treatments (in vitro) they also exhibit at least catecholoxidase reactivity. On the basis of their molecular st…

Models MolecularProtein ConformationTyrosinasemedicine.medical_treatmentchemical and pharmacologic phenomenaBiochemistrySubstrate SpecificityHydroxylationchemistry.chemical_compoundProtein structuremedicineAnimalsBinding siteCatechol oxidaseMolecular Biologychemistry.chemical_classificationBinding SitesMolecular StructurebiologyMonophenol MonooxygenaseHemocyaninEnzyme ActivationEnzymechemistryBiochemistryStructural biologyHemocyaninsbiology.proteinCatechol OxidaseTrends in Biochemical Sciences
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Cis autocatalytic cleavage of glycine-linked Zika virus NS2B-NS3 protease constructs.

2019

The flaviviral heterodimeric serine protease NS2B-NS3, consisting of the NS3 protease domain and the NS2B co-factor, is essential for ZIKA virus maturation and replication in cells. For in vitro studies a 'linked' construct, where a polyglycine linker connects NS2BCF and NS3pro , is often used. This construct undergoes autocatalytic cleavage. Here, we show that linked ZIKV NS2BCF -NS3pro is cleaved in cis in the NS2BCF exclusively at position R95 and not at the previously proposed alternate cleavage site at residue R29 in the NS3pro . Cleavage neither affects protease stability nor activity, despite some observed differences in spectroscopic behavior. This minimally modified construct may t…

Models MolecularProtein Conformationmedicine.medical_treatmentBiophysicsViral Nonstructural ProteinsCleavage (embryo)ArginineVirus ReplicationBiochemistryCatalysisZika virus03 medical and health sciencesViral ProteinsStructural BiologyGeneticsmedicineHomeostasisMolecular Biology030304 developmental biologySerine protease0303 health sciencesNS3ProteasebiologyChemistryCircular Dichroism030302 biochemistry & molecular biologySerine EndopeptidasesCell BiologyZika Virusbiology.organism_classificationIn vitroRecombinant ProteinsFlavivirusSpectrometry FluorescenceBiochemistrybiology.proteinProtein MultimerizationPeptidesLinkerPeptide HydrolasesFEBS lettersReferences
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The NS3/4A proteinase of the hepatitis C virus: unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy

1999

The hepatitis C virus (HCV) is a major causative agent of transfusion-acquired and sporadic non-A, non-B hepatitis worldwide. Infections most often persist and lead, in approximately 50% of all patients, to chronic liver disease. As is characteristic for a member of the family Flaviviridae, HCV has a plus-strand RNA genome encoding a polyprotein, which is cleaved co- and post-translationally into at least 10 different products. These cleavages are mediated, among others, by a virally encoded chymotrypsin-like serine proteinase located in the N-terminal domain of non-structural protein 3 (NS3). Activity of this enzyme requires NS4A, a 54-residue polyprotein cleavage product, to form a stable…

Models MolecularProtein ConformationvirusesHepatitis C virusMolecular Sequence DataHepacivirusViral Nonstructural ProteinsBiologymedicine.disease_causeAntiviral AgentsSerineProtein structureVirologymedicineProtease InhibitorsAmino Acid SequenceHepatitischemistry.chemical_classificationNS3HepatologySerine EndopeptidasesRNAmedicine.diseaseVirologyNS2-3 proteaseInfectious DiseasesEnzymechemistryRNA HelicasesJournal of Viral Hepatitis
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Irreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates

2010

The formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheolog…

Models MolecularProtein FoldingCircular dichroismGelationProtein ConformationDiffusionBiophysicsProtein aggregationUnfoldingchemistry.chemical_compoundDifferential scanning calorimetryProtein structureAnimalsQuantitative Biology::BiomoleculesChemistryPrecipitation (chemistry)Circular DichroismTemperaturePercolationGeneral MedicineBlood Coagulation FactorsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Thermal irreversibilityCrystallographyChemical physicsThermodynamicsMuramidaseProtein foldingLysozymeProtein aggregation
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Calculation of partition coefficient and hydrophobic moment of the secondary structure of lysozyme

2001

A method that permits a semiquantitative estimate of the partitioning of any solute between any two media is presented. As an example, the partition coefficients and hydrophobic moment of the secondary structure of lysozyme are calculated. Program GSCAP is written as a version of Pascal's solvent-dependent conformational analysis (SCAP) program. The dipole moments calculated for the helices are trebled with respect to that for the sheet. For helices, the main contribution to the water-accessible surface area is the hydrophobic term, while the hydrophilic part dominates in the sheet. Molecular globularity and the three studied partition coefficients differentiate between helices and sheet.

Models MolecularQuantitative Biology::BiomoleculesChromatographyOrganic ChemistrySolvationGeneral MedicineBiochemistryProtein Structure SecondaryAnalytical ChemistryGibbs free energyCondensed Matter::Soft Condensed MatterPartition coefficientchemistry.chemical_compoundsymbols.namesakeDipolechemistrysymbolsThermodynamicsMoleculeMuramidaseLysozymeProtein secondary structureJournal of Chromatography A
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