Search results for "OXIDASE"

showing 10 items of 927 documents

Pathophysiological role of oxidative stress in systolic and diastolic heart failure and its therapeutic implications

2015

Abstract Systolic and diastolic myocardial dysfunction has been demonstrated to be associated with an activation of the circulating and local renin–angiotensin–aldosterone system (RAAS), and with a subsequent inappropriately increased production of reactive oxygen species (ROS). While, at low concentrations, ROS modulate important physiological functions through changes in cellular signalling and gene expression, overproduction of ROS may adversely alter cardiac mechanics, leading to further worsening of systolic and diastolic function. In addition, vascular endothelial dysfunction due to uncoupling of the nitric oxide synthase, activation of vascular and phagocytic membrane oxidases or mit…

Mitochondrial ROSmedicine.medical_specialtyXanthine OxidasePhosphodiesterase InhibitorsDiastoleAngiotensin-Converting Enzyme InhibitorsReviewmedicine.disease_causeNitric OxideCardiovascular SystemAntioxidantsInternal medicinemedicineHumansEndothelial dysfunctionHeart Failure DiastolicEjection fractionNitratesbusiness.industryDiastolic heart failureNADPH OxidasesStroke VolumeVitaminsHydralazinemedicine.diseaseHydralazineExercise TherapyMitochondriaOxidative StressHeart failureCardiologyDrug Therapy CombinationNitric Oxide SynthaseCardiology and Cardiovascular MedicinebusinessReactive Oxygen SpeciesOxidative stressmedicine.drugHeart Failure Systolic
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Cholesterol oxidase: ultrahigh-resolution crystal structure and multipolar atom model-based analysis

2015

International audience; Author(s) of this paper may load this reprint on their own web site or institutional repository provided that this cover page is retained. Republication of this article or its storage in electronic databases other than as specified above is not permitted without prior permission in writing from the IUCr. For further information see http://journals.iucr.org/services/authorrights.html Acta Cryst. (2015). D71, 954-968 Zarychta et al. · Cholesterol oxidase research papers 954 http://dx. Examination of protein structure at the subatomic level is required to improve the understanding of enzymatic function. For this purpose, X-ray diffraction data have been collected at 100…

Models MolecularElectron densityCholesterol oxidaseProtein ConformationCrystallography X-Ray010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureStructural Biologycholesterol oxidase[CHIM.CRIS]Chemical Sciences/Cristallography[CHIM]Chemical Sciences030304 developmental biologyFlavin adenine dinucleotide0303 health sciencesHydrogen bondIntermolecular forceResolution (electron density)Hydrogen BondingGeneral MedicineStreptomyces0104 chemical sciencesBond lengthCrystallographychemistryFlavin-Adenine Dinucleotide
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Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly.

2004

The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol. TEM study suggested that this assembly is a regular dodecahedron, containing 12 Prx-2 decamers (Mr 2.62 MDa, external diameter approximately 20 nm). This interpretation has been supported by production of a approximately 1.6 nm 3D reconstruction from the negative stain TEM data, with automated docking of the available X-ray data of the Prx-2 decamer. Comparison with other known protein dodecahedral and viral icosahedral structures indicates that this arrangement…

Models MolecularMaterials scienceErythrocytesIcosahedral symmetryMacromolecular SubstancesMacromolecular SubstancesGeneral Physics and AstronomyCell BiologyPeroxiredoxin 2Polyethylene glycolPeroxiredoxinsNegative stainDodecahedronCrystallographychemistry.chemical_compoundProtein structurechemistryMicroscopy Electron TransmissionPeroxidasesStructural BiologyImage Processing Computer-AssistedHumansGeneral Materials ScienceProtein Structure QuaternaryMacromoleculeMicron (Oxford, England : 1993)
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Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography

2001

Abstract The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II). Single particle analysis from electron micrographs of Prx-II molecules homogeneously orientated across holes in the presence of a thin film of ammonium molybdate and trehalose has facilitated the production of a ≥20 A 3-D reconstruction by angular reconstitution that emphasises the D5 symmetry of the ring-like decamer. The X-ray structure for Prx-II was fitted into the transmission electron microscopic reconstruction by molecular replacement. The surface-rendered transmission electron microscopy (TEM) reconstruction correlates well…

Models MolecularMolybdenumErythrocytesSurface PropertiesCryo-electron microscopyChemistryResolution (electron density)BiophysicsTrehaloseSingle particle analysisPeroxiredoxinsCrystallography X-RayBiochemistryNegative stainMicroscopy ElectronCrystallographyPeroxidasesElectron tomographyStructural BiologyTransmission electron microscopyHumansEnergy filtered transmission electron microscopyOrthorhombic crystal systemMolecular BiologyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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Elucidation of Carbohydrate Molecular Interaction Mechanism of Recombinant and Native ArtinM

2013

[EN] The quartz crystal microbalance (QCM) technique has been applied for monitoring the biorecognition of ArtinM lectins at low horseradish peroxidase glycoprotein (HRP) concentrations, using a simple kinetic model based on Langmuir isotherm in previous work.(18) The latter approach was consistent with the data at dilute conditions but it fails to explain the small differences existing in the jArtinM and rArtinM due to ligand binding concentration limit. Here we extend this analysis to differentiate sugar-binding event of recombinant (rArtinM) and native (jArtinM) ArtinM lectins beyond dilute conditions. Equivalently, functionalized quartz crystal microbalance with dissipation monitoring (…

Models MolecularPROTEIN ADSORPTIONSURFACEKM+Horseradish peroxidaselaw.inventionsymbols.namesakelawQUARTZ-CRYSTAL MICROBALANCEBINDINGQUIMICA ANALITICAMaterials ChemistryPhysical and Theoretical ChemistrySPECIFICITYGlycoproteinsBinding SitesChromatographybiologyChemistryLectinLangmuir adsorption modelQuartz crystal microbalanceQuartz Crystal Microbalance TechniquesLECTINRecombinant ProteinsSurfaces Coatings and FilmsMannose-Binding LectinsSolvation shellHYDRATION-SHELLQuartz Crystal Microbalance TechniquesBiophysicsbiology.proteinRecombinant DNAsymbolsPlant LectinsBIOMOLECULAR ADSORPTIONARTOCARPINProtein adsorption
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Effect of temperature and ligand protonation on the electronic ground state in Cu( ii ) polymers having unusual secondary interactions: a magnetic an…

2018

International audience; Two new copper(II) polymeric complexes, {[Cu(HPymat)(H2O)](NO3)}n (1) and [Cu2(Pymat)2(H2O)3]n (2), have been synthesized using the Schiff base ligand H2Pymat [H2Pymat = (E)-2-(1-(pyridin-2-yl)-methyleneamino)terephthalic acid]. Complex 1 is a cationic 1D polymer, whereas complex 2 is a two dimensional polymer. Both complexes were crystallographically, spectroscopically and magnetically characterized. Theoretical studies were performed and the catecholase activity of the complexes was also examined. Complex 1 is a ferromagnetically coupled complex with J = 2.8 cm−1 and 2 shows antiferromagnetic coupling with J = −1.6 cm−1. Both complexes show notable features in the …

Models MolecularPolymerschemistry.chemical_elementProtonation010402 general chemistryCrystallography X-RayLigands01 natural scienceslaw.inventionInorganic Chemistrychemistry.chemical_compoundlawCoordination ComplexesMolecule[CHIM]Chemical SciencesElectron paramagnetic resonanceSchiff baseMolecular Structure010405 organic chemistryLigandMagnetic PhenomenaTemperatureTwo-dimensional polymer[CHIM.MATE]Chemical Sciences/Material chemistryHydrogen-Ion ConcentrationCopper0104 chemical sciencesCrystallography[CHIM.POLY]Chemical Sciences/PolymerschemistryQuantum TheoryProtonsGround stateCatechol OxidaseCopper
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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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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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Tyrosinase versus Catechol Oxidase: One Asparagine Makes the Difference

2015

Tyrosinases mediate the ortho-hydroxylation and two-electron oxidation of monophenols to ortho-quinones. Catechol oxidases only catalyze the oxidation of diphenols. Although it is of significant interest, the origin of the functional discrimination between tyrosinases and catechol oxidases has been unclear. Recently, it has been postulated that a glutamate and an asparagine bind and activate a conserved water molecule towards deprotonation of monophenols. Here we demonstrate for the first time that a polyphenoloxidase, which exhibits only diphenolase activity, can be transformed to a tyrosinase by mutation to introduce an asparagine. The asparagine and a conserved glutamate are necessary to…

Models MolecularStereochemistryCopper proteinTyrosinase010402 general chemistrymedicine.disease_cause01 natural sciencesCatalysischemistry.chemical_compoundDeprotonationmedicineMoleculeAsparagineCatechol oxidaseCatecholMutationbiologyMonophenol Monooxygenase010405 organic chemistryGeneral Chemistry0104 chemical scienceschemistryBiochemistrybiology.proteinAsparagineCatechol OxidaseAngewandte Chemie International Edition
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Synthesis, in vitro activity, and three-dimensional quantitative structure-activity relationship of novel hydrazine inhibitors of human vascular adhe…

2010

Vascular adhesion protein-1 (VAP-1) belongs to the semicarbazide-sensitive amine oxidases (SSAOs) that convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases (MAOs), but their substrate specificities are partly overlapping. VAP-1 has been proposed as a target for anti-inflammatory drug therapy because of its role in leukocyte adhesion to endothelium. Here, we describe the synthesis and in vitro activities of novel series of VAP-1 selective inhibitors. In addition, the molecular dynamics simulations performed for VAP-1 reveal that the movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those s…

Models MolecularSubstrate SpecificitiesQuantitative structure–activity relationshipMolecular ConformationQuantitative Structure-Activity RelationshipMolecular Dynamics SimulationLigandsMolecular dynamicsCricetulusCricetinaeDrug DiscoveryAnimalsHumansMonoamine OxidaseBinding SitesChemistryStereoisomerismIn vitrorespiratory tract diseasesRatsMonoamine neurotransmitterHydrazinesBiochemistryDocking (molecular)Molecular MedicineAmine gas treatingAmine Oxidase (Copper-Containing)Cell Adhesion MoleculesVASCULAR ADHESION PROTEIN 1Protein BindingJournal of medicinal chemistry
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