Search results for "Monooxygenase"

showing 10 items of 171 documents

Charged Tags for the Identification of Oxidative Drug Metabolites Based on Electrochemistry and Mass Spectrometry

2020

Abstract Most of the active pharmaceutical ingredients like Metoprolol are oxidatively metabolized by liver enzymes, such as Cytochrome P450 monooxygenases into oxygenates and therefore hydrophilic products. It is of utmost importance to identify the metabolites and to gain knowledge on their toxic impacts. By using electrochemistry, it is possible to mimic enzymatic transformations and to identify metabolic hot spots. By introducing charged‐tags into the intermediate, it is possible to detect and isolate metabolic products. The identification and synthesis of initially oxidized metabolites are important to understand possible toxic activities. The gained knowledge about the metabolism will…

Spectrometry Mass Electrospray IonizationAlkylationPyridinesElectrospray ionizationPyridinium CompoundsMass spectrometryHydroxylationlcsh:Chemistrydrug metabolitesCytochrome P-450 Enzyme Systemcharged tagsChromatography High Pressure Liquidmass spectrometrychemistry.chemical_classificationActive ingredientChromatographybiologyCommunicationanodic oxidationCytochrome P450General ChemistryMetabolismElectrochemical TechniquesMonooxygenaseCommunicationsEnzymelcsh:QD1-999chemistryelectrochemistrybiology.proteinOxidation-ReductionDrug metabolismMetoprololSignal TransductionChemistryOpen
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Kinetic properties of hexameric tyrosinase from the crustacean Palinurus elephas.

2008

Tyrosinases catalyze hydroxylation of monophenols to o-diphenols and their subsequent oxidation to o-quinones, whereas catecholoxidases catalyze only the latter reaction. Both enzymes occur in all organisms and are Type 3 copper proteins that perform the first steps of melanin formation. In arthropods, they play an essential role in the sclerotization of the exoskeleton. Very few phenoloxidases are characterized structurally or kinetically and the existence of an actual tyrosinase activity has not been demonstrated in most cases. Here we present for the first time a complete kinetic characterization of a tyrosinase from a crustacean (Palinurus elephas) including the influence of inhibitors.…

StereochemistryCopper proteinTyrosinaseDopamineAllosteric regulationTyramineCooperativityBiologyBiochemistryBinding CompetitiveHydroxylationchemistry.chemical_compoundNon-competitive inhibitionAnimalsMimosinePhysical and Theoretical ChemistryEnzyme InhibitorsPalinuridaechemistry.chemical_classificationBinding SitesMolecular StructureMonophenol MonooxygenaseGeneral MedicinePhenylthioureaKineticsEnzymechemistryBiochemistryMimosineAllosteric SitePhotochemistry and photobiology
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Vulnerability of peripheral catecholaminergic neurons to MPTP is not regulated by alpha-synuclein.

2010

Although generally considered a prototypical movement disorder, Parkinson's disease is commonly associated with a broad-spectrum of non-motor symptoms, including autonomic dysfunctions caused by significant alterations in catecholaminergic neurons of the peripheral sympathetic nervous system. Here we present evidence that alpha-synuclein is highly expressed by sympathetic ganglion neurons throughout embryonic and postnatal life and that it is found in tyrosine hydroxylase-positive sympathetic fibers innervating the heart of adult mice. However, mice deficient in alpha-synuclein do not exhibit any apparent alterations in sympathetic development. Sympathetic neurons isolated from mouse embryo…

Sympathetic nervous system1-Methyl-4-phenylpyridiniumα-Synuclein knockoutTyrosine 3-MonooxygenaseNeurotoxinsNeurotrophic factorSubstantia nigraBiologylcsh:RC321-571chemistry.chemical_compoundMiceCatecholaminesSympathetic Fibers PostganglionicParkinsonian DisordersNeurotrophic factorsmedicineNeurotoxinAutonomic gangliaAnimalslcsh:Neurosciences. Biological psychiatry. NeuropsychiatryCells CulturedNeuronsGanglia SympatheticCell DeathMPTPSympathetic ganglionMice Mutant Strainsnervous system diseasesMPP+medicine.anatomical_structureNeurologychemistrynervous system1-Methyl-4-phenyl-1236-tetrahydropyridinePeripheral nervous systemSympathetic nervous systemNerve Degenerationalpha-SynucleinCatecholaminergic cell groupsPeripheral nervous systemNeuroscienceNeurobiology of disease
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The use of clonal mRNA as an antigenic format for the detection of antigen-specific T lymphocytes in IFN-gamma ELISPOT assays.

2003

Abstract Most assay systems for the quantification of antigen-specific T-cell responses in infectious, malignant and autoimmune disease depend on the peptide antigen format and are therefore restricted to known epitopes and their presenting HLA molecules. Here we tested in ELISPOT assays the application of in vitro-transcribed clonal mRNA as an alternative antigen format covering all potential epitopes of a given antigen. As model antigens, we chose pp65 of human cytomegalovirus (HCMV) and human tyrosinase (hTyr). Antigen-presenting cells (APC) were K562 cells stably transfected with single HLA class I alleles and autologous dendritic cells (DC). As effectors, we applied in vitro-generated …

T-LymphocytesImmunologyAntigen-Presenting CellsEpitopes T-LymphocyteGenes MHC Class IHuman leukocyte antigenBiologyTransfectionEpitopeImmunoenzyme TechniquesViral Matrix ProteinsInterferon-gammaAntigenmedicineImmunology and AllergyHumansInterferon gammaRNA MessengerCloning MolecularMonophenol MonooxygenaseELISPOTTransfectionT lymphocyteDendritic CellsPhosphoproteinsVirologyMolecular biologyElectroporationK562 CellsCD8medicine.drugJournal of immunological methods
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Insect Immune Evasion by Dauer and Nondauer Entomopathogenic Nematodes

2021

The immune response of animals, including insects, is overcome by some parasites. For example, dauer larvae (DL) of the obligate entomopathogenic nematodes (EPNs) Heterorhabditis and Steinernema can invade insects, evade their defenses, and cause death. Although DL were long assumed to be the only infective stage of nematodes, recent reports suggest that L2-L3 larvae of facultative EPNs are also capable of killing insects. There are no studies, to our knowledge, about the role of nonimmunological barriers (the exoskeleton and its openings) in avoiding infection by DL and L2-L3 larvae, or whether these larval stages evade the host immune system in the same way. The objective of this study wa…

Time Factorsanimal structuresmedia_common.quotation_subjectCobra Cardiotoxin ProteinsInsectMicrobiologyAnimalsEcology Evolution Behavior and SystematicsImmune Evasionmedia_commonStrongyloideaAnalysis of VarianceEnzyme PrecursorsLarvaInnate immune systemVirulencebiologyMonophenol MonooxygenaseHost (biology)fungiProphenoloxidaseHeterorhabditisbiology.organism_classificationLepidopteraGalleria mellonellaNematodeLarvaParasitologyCatechol OxidaseJournal of Parasitology
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D2R striatopallidal neurons inhibit both locomotor and drug reward processes.

2009

The specific functions of dopamine D(2) receptor-positive (D(2)R) striatopallidal neurons remain poorly understood. Using a genetic mouse model, we found that ablation of D(2)R neurons in the entire striatum induced hyperlocomotion, whereas ablation in the ventral striatum increased amphetamine conditioned place preference. Thus D(2)R striatopallidal neurons limit both locomotion and, unexpectedly, drug reinforcement.

Time FactorsstriatumParkinson's diseaseStriatumNeurons -- drug effectsEnkephalins -- metabolism10263 Institute of Experimental ImmunologyMiceDopamine Uptake InhibitorsTyrosine 3-Monooxygenase -- geneticsCorpus Striatum -- cytologyDiphtheria ToxinGlutamate Decarboxylase -- metabolismstriatum; indirect opathway; A2A receptors; D2 receptors; locomotion; amphetamine addiction; Parkinson's diseaseNeuronsamphetamine addictionGlutamate DecarboxylaseGeneral NeuroscienceAmphetamine -- pharmacologyNeurodegeneration2800 General NeuroscienceEnkephalinsSciences bio-médicales et agricoleslocomotionmedicine.anatomical_structureA2A receptorsIntercellular Signaling Peptides and ProteinsReceptors Dopamine D2 -- metabolismPsychologyLocomotionmedicine.drugHeparin-binding EGF-like Growth FactorProtein BindingGlobus Pallidus -- cytologyReceptors Dopamine D2 -- deficiencyReinforcement ScheduleTyrosine 3-MonooxygenaseGlutamate Decarboxylase -- geneticsLocomotion -- geneticsIntercellular Signaling Peptides and Proteins -- genetics610 Medicine & healthMice TransgenicNerve Tissue ProteinsDiphtheria Toxin -- pharmacologyGlobus PallidusNeurons -- physiologyLocomotion -- drug effectsRewardDopamineDopamine receptor D2medicineNerve Tissue Proteins -- metabolismAnimalsGene Expression Regulation -- geneticsAmphetamineD2 receptorsReceptors Adenosine A2Receptors Dopamine D2indirect opathwayVentral striatumReceptors Adenosine A2 -- geneticsDopamine Uptake Inhibitors -- pharmacologymedicine.diseaseConditioned place preferenceCorpus StriatumMice Inbred C57BLGene Expression Regulation -- drug effectsAmphetaminenervous systemGene Expression RegulationProtein Binding -- drug effectsTyrosine 3-Monooxygenase -- metabolism570 Life sciences; biologyAutoradiographyConditioning OperantNeuronConditioning Operant -- physiologyNeuroscienceEnkephalins -- geneticsNature neuroscience
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Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors

2008

AbstractPhenoloxidases and hemocyanins have similar type 3 copper centers although they perform different functions. Hemocyanins are oxygen carriers, while phenoloxidases (tyrosinase/catecholoxidase) catalyze the initial step in melanin synthesis. Tyrosinases catalyze two subsequent reactions, whereas catecholoxidases catalyze only the second one. Recent results indicate that hemocyanins can also function as phenoloxidases and here we show for the first time that hemocyanin can be converted to phenoloxidase. Furthermore, its substrate specificity can be switched between catecholoxidase and tyrosinase activity depending on effectors such as hydroxymethyl-aminomethan (Tris) and Mg2+-ions. Thi…

TrisStereochemistrymedicine.medical_treatmentTyrosinaseDopamineAllosteric regulationActivated hemocyaninBiophysicsMagnesium ChlorideTyramineType 3 copper proteinchemical and pharmacologic phenomenaBiochemistryCatalysisSubstrate SpecificityScorpionschemistry.chemical_compoundEnzyme activatorAllosteric RegulationStructural BiologyHemolymphHemolymphGeneticsmedicineAnimalsCatechol oxidaseMolecular BiologyScorpion Pandinus imperatorbiologyMonophenol MonooxygenaseSpectrum AnalysisActive siteCatecholoxidaseHemocyaninCell BiologyEnzyme ActivationchemistryBiochemistryHemocyaninsbiology.proteinTyrosinaseCatechol OxidaseFEBS Letters
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Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type …

1999

We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzym…

TyrosinaseCatecholschemistry.chemical_elementPhotochemistrySpectrum Analysis RamanBiochemistrylaw.inventionTreesInorganic Chemistrychemistry.chemical_compoundlawPolymer chemistryEnzyme InhibitorsElectron paramagnetic resonanceCatechol oxidaseCatecholBinding SitesCyanidesbiologyMonophenol MonooxygenaseSpectrophotometry AtomicElectron Spin Resonance SpectroscopySubstrate (chemistry)Bridging ligandHydrogen-Ion ConcentrationPlantsPhenylthioureaCopperMolecular WeightchemistryHemocyaninsbiology.proteinSpectrophotometry UltravioletOxygen bindingCatechol OxidaseCopperJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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Oxidation of carbidopa by tyrosinase and its effect on murine melanoma

2009

Oxidation of the anti-Parkinsonian agent carbidopa by tyrosinase was investigated. The products of this reaction were identified as 3-(3,4-dihydroxyphenyl)-2-methylpropanoic acid and 6,7-dihydroxy-3-methylcinnoline. These results demonstrate that after oxidation of the catechol moiety to an o-quinone either a redox exchange with the hydrazine group or a cyclization reaction occur. The cyclization product underwent additional oxidation reactions leading to aromatization. The cyclization reaction is undesired in the case of hydrazine-containing anti-melanoma prodrugs and will have to be taken into account in designing such compounds. Carbidopa was tested against B16(F10) melanoma cells in cul…

TyrosinaseClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentstyrosinaseBiochemistryRedoxMicechemistry.chemical_compoundCell Line TumorDrug DiscoverymedicinemelanomaAnimalsMoietyOrganic chemistryProdrugscarbidopaCytotoxicityMolecular BiologyCatecholMonophenol MonooxygenaseChemistryOrganic ChemistryAromatizationhydrazineProdrugCombinatorial chemistryDihydroxyphenylalanineCyclizationCarbidopaMolecular MedicineprodrugOxidation-Reductionmedicine.drugBioorganic & Medicinal Chemistry Letters : a tetrahedron publication for the rapid dissemination of preliminary communication and all aspects of bioorganic chemistry, medicinal chemistry and related disciplines
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Indirect oxidation of the antitumor agent procarbazine by tyrosinase—Possible application in designing anti-melanoma prodrugs

2008

The interaction of tyrosinase with the anticancer drug procarbazine has been investigated. In the presence of the enzyme alone no oxidation of this dialkylhydrazine above the background level was observed. However, when phenolic substrates (4-tert-butylcatechol or N-acetyl-l-tyrosine) were included in the reaction mixture, procarbazine was rapidly degraded. Oxygen consumption measurements showed that in a mixture both the phenolic substrate and the drug were oxidized. The major product of procarbazine degradation was isolated and identified as azoprocarbazine, the first active metabolite of this drug detected in previous in vivo and in vitro studies. This indirect oxidation of the hydrazine…

TyrosinaseClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentstyrosinaseProcarbazineBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundOxygen ConsumptionIn vivoDrug DiscoverymelanomamedicineOrganic chemistryProdrugsHydrazine (antidepressant)PhenolsMolecular BiologyActive metaboliteMolecular StructureMonophenol MonooxygenaseOrganic ChemistrySubstrate (chemistry)hydrazineProdrugHydrazineschemistryProcarbazineMolecular Medicineredox exchangeprodrugAgaricalesOxidation-Reductionmedicine.drugBioorganic & Medicinal Chemistry Letters
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