Search results for "DASE"

showing 10 items of 1891 documents

Redox intermediates of plant and mammalian peroxidases: a comparative transient-kinetic study of their reactivity toward indole derivatives.

2002

Abstract A comparative study on the reactivity of five indole derivatives (tryptamine, N-acetyltryptamine, tryptophan, melatonin, and serotonin), with the redox intermediates compound I (k2) and compound II (k3) of the plant enzyme horseradish peroxidase (HRP) and the two mammalian enzymes lactoperoxidase (LPO) and myeloperoxidase (MPO), was performed using the sequential-mixing stopped-flow technique. The calculated bimolecular rate constants (k2, k3) revealed substantial differences regarding the oxidizability of the substrates by redox intermediates at pH 7.0 and 25°C. With HRP it was shown that k2 and k3 are mainly determined by the reduction potential (E°′) of the substrate with k2 bei…

Indole testTryptamineMammalsIndolesbiologyStereochemistryLactoperoxidaseBiophysicsTryptophanSubstrate (chemistry)PlantsBiochemistryHorseradish peroxidaseRedoxchemistry.chemical_compoundKineticschemistryPeroxidasesbiology.proteinAnimalsLactoperoxidaseMolecular BiologyOxidation-ReductionHorseradish PeroxidasePeroxidaseArchives of biochemistry and biophysics
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1,2,4-Oxadiazole topsentin analogs as staphylococcal biofilm inhibitors targeting the bacterial transpeptidase sortase A

2020

The inhibition or prevention of biofilm formation represents an emerging strategy in the war against antibiotic resistance, interfering with key players in bacterial virulence. This approach includes the inhibition of the catalytic activity of transpeptidase sortase A (Srt A), a membrane enzyme responsible for covalently attaching a wide variety of adhesive matrix molecules to the peptidoglycan cell wall in Gram-positive strains. A new series of seventeen 1,2,4-oxadiazole derivatives was efficiently synthesized and screened as potential new anti-virulence agents. The ability of inhibiting biofilm formation was evaluated against both Gram-positive and Gram-negative pathogens. Remarkably, all…

Indoles124-Oxadiazoles Antibiofilm activity Sortase A inhibitors Anti-virulence agents Marine alkaloids Topsentin analogs01 natural scienceslaw.inventionchemistry.chemical_compoundMarine alkaloidslawDrug DiscoveryPathogenchemistry.chemical_classificationOxadiazoles0303 health sciencesChemistry4-OxadiazolesImidazolesGeneral MedicineStaphylococcal InfectionsAminoacyltransferasesAnti-Bacterial AgentsCysteine EndopeptidasesAnti-virulence agentsBiochemistrySortase AAntibiofilm activityPseudomonas aeruginosaTopsentin analogsRecombinant DNA124-Oxadiazoles; Anti-virulence agents; Antibiofilm activity; Marine alkaloids; Sortase A inhibitors; Topsentin analogsStaphylococcus aureus12Sortase A inhibitorsCell LineCell wall03 medical and health sciencesAntibiotic resistanceBacterial Proteins124-OxadiazolesHumansPseudomonas Infections030304 developmental biologyPharmacology010405 organic chemistryOrganic ChemistryBiofilmSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesEnzymeBiofilmsPeptidoglycan
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Inflammatory Response of the Ascidian Ciona intestinalis

2016

Abstract The Ciona intestinalis inflammatory response to several irritants appears to be composed of a complex reaction set. The cellular reactions in the tunic involve hemocyte infiltration, hemocyte and epidermis activities, vacuolization, and cell disruption, while cell products can contribute to form capsule components and/or cause a tunic wound. In this response, the involvement of the pharynx, as the main immune-competent organ, has been disclosed by a lipopolysaccharide challenge that upregulates innate immunity genes and transcription activation genes. The pharynx responds through hemocyte recruitment into the pharynx vessels, enhancement of galectin-like lectins in the serum hemoly…

InflammationProphenoloxidaseInnate immune systemAscidianCiona intestinaliSettore BIO/05 - ZoologiaMedicine (miscellaneous)HemocyteLipopolysaccharideInflammationProphenoloxidaseBiologybiology.organism_classificationCell biologyImmune systemImmunologymedicineAlternative complement pathwayPharynxCiona intestinalismedicine.symptomCytokineLectinGeneGalectin
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Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation.

2015

Novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation were developed; some of them possess K(i) values in the micromolar range. We studied the structure-activity relationship of these derivatives and we performed docking studies, which allowed us to find out the key interactions established by the inhibitors with the target enzyme. Biological results indicate that the nature of the P2 and P3 substituents and their binding to the S2/S3 pockets is strictly interdependent.

InhibitorMolecular modelCell SurvivalClinical BiochemistryTrypanosoma brucei bruceiAntiprotozoal AgentsPharmaceutical ScienceMolecular modelingCysteine Proteinase InhibitorsBiochemistryCell Linechemistry.chemical_compoundMiceStructure-Activity RelationshipCysteine ProteasesDrug DiscoveryAnimalsMolecular Biology3-Bromo isoxazolinechemistry.chemical_classificationDipeptide-likeDipeptideBinding SitesOrganic ChemistryDipeptidesIsoxazolesCombinatorial chemistryProtein Structure TertiaryMolecular Docking SimulationCysteine EndopeptidasesEnzymeRhodesainchemistryWarheadDocking (molecular)Drug DesignMolecular MedicineRhodesain Dipeptide-like 3-Bromo isoxazoline Inhibitor Molecular modelingBioorganicmedicinal chemistry
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Electrocatalytic reduction of dioxygen to water by tren-capped porphyrins, functional models of cytochrome c oxidase

1999

International audience; Two different tren-capped porphyrins—in which the two metals, iron and copper, are more or less off-centered—are shown to be efficient catalysts for the reduction of O2 to H2O; surprisingly, their iron-only complexes are shown to be even more effective 4e- catalysts when adsorbed on a graphiteelectrode.

Inorganic chemistrychemistry.chemical_element010402 general chemistryPhotochemistry[ CHIM ] Chemical Sciences01 natural sciencesCatalysisCatalysisReduction (complexity)Adsorption[CHIM] Chemical SciencesMaterials Chemistry[CHIM]Chemical SciencesCytochrome c oxidaseGraphite electrodebiology010405 organic chemistryChemistryMetals and AlloysGeneral ChemistryCopper0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsCeramics and Compositesbiology.protein
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A novel target of lithium therapy.

2000

Phosphatases converting 3'-phosphoadenosine 5'-phosphate (PAP) into adenosine 5'-phosphate are of fundamental importance in living cells as the accumulation of PAP is toxic to several cellular systems. These enzymes are lithium-sensitive and we have characterized a human PAP phosphatase as a potential target of lithium therapy. A cDNA encoding a human enzyme was identified by data base screening, expressed in Escherichia coli and the 33 kDa protein purified to homogeneity. The enzyme exhibits high affinity for PAP (K(m)1 microM) and is sensitive to subtherapeutic concentrations of lithium (IC(50)=0.3 mM). The human enzyme also hydrolyzes inositol-1, 4-bisphosphate with high affinity (K(m)=0…

Inositol-14-bisphosphateDNA ComplementaryBicinePhosphataseMolecular Sequence DataBiophysicschemistry.chemical_elementSaccharomyces cerevisiaeLithiummedicine.disease_causeBiochemistrychemistry.chemical_compoundStructural BiologyNucleotidasesComplementary DNAPhosphataseGeneticsmedicineEscherichia coliHumansAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliIC50Chromatography High Pressure Liquidchemistry.chemical_classificationExpressed Sequence TagsBase Sequence3′-Phosphoadenosine 5′-phosphateCell BiologyMolecular biologyAdenosineAdenosine MonophosphatePhosphoric Monoester HydrolasesAdenosine DiphosphateEnzymechemistryBiochemistryLithiummedicine.drugHumanFEBS letters
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Molecular characterization of a male-specific glycosyl hydrolase, Lma-p72, secreted on to the abdominal surface of the Madeira cockroach Leucophaea m…

2003

0264-6021 (Print) Journal Article Research Support, Non-U.S. Gov't; The epicuticular surface protein Lma-p72 is specific to the abdominal secretions of Leucophaea maderae (Madeira cockroach) adult males. Natural Lma-p72 was purified and the complete cDNA sequence determined by reverse-transcription PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p72 was expressed in the tergal and sternal glands. Sequence alignment indicates that Lma-p72 is closely related to the family 1 glycosyl hydrolases (EC 3.2.1). Native Lma-p72 was proved to be active in the abdominal secretions and exhibit a beta-galactosidase-like activity. Ho…

Insect Proteins/*genetics/secretionMaleOligosaccharidesCockroachesRecombinant Proteins/chemistryBiochemistryPolymerase Chain ReactionEpitheliumPheromonesLactoneschemistry.chemical_compoundGlycoside Hydrolases/*genetics/secretionGlycoside hydrolaseNorthernCockroaches/*genetics/metabolismIn Situ HybridizationOligosaccharides/metabolismbiologyBlottingRecombinant ProteinsBiochemistryExocrine Glands/enzymologyLarvaInsect ProteinsHydrocarbons/pharmacologyFemaleResearch ArticleDNA ComplementaryGlycoside HydrolasesMolecular Sequence DataSequence alignmentComplementary/geneticsGluconatesExocrine GlandsComplementary DNAbiology.animalHydrolaseAnimalsGlycosylMolecular BiologyCockroachEpithelium/physiologyPheromones/chemistry/metabolismEdman degradationBiological TransportCell BiologyDNABlotting Northernbeta-Galactosidasebiology.organism_classificationMolecular biologyHydrocarbonsGluconates/pharmacologyBlaberidaechemistrybeta-Galactosidase/metabolism
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Effects of aldicarb and propoxur on cytotoxicity and lipid peroxidation in CHO-K1 cells

2010

Abstract Cytotoxic effects of aldicarb, its sulfone and sulfoxide, and propoxur, lipid peroxidation and antioxidant parameters in Chinese Hamster Ovary (CHO-K1) cells were determined. d , l -buthionine-( S , R )-sulfoximine (BSO) was assayed to determine the role of GSH in the protection against carbamate cytotoxicity. Pre-treatment with 60 μM BSO, induced a significant decrease in the glutathione reductase (GR; 64–141%), the glutathione peroxidase (GPx; 10–30%) and the glutathione S-transferase (GST; 59–93%) activities, and its GSH levels (79–85%), while the oxidized glutathione (GSSG) levels significantly increased (64–78%) respect to experiment non-BSO-pretreated. Carbamates BSO pre-trea…

InsecticidesAntioxidantmedicine.medical_treatmentGlutathione reductaseCHO CellsPharmacologyPropoxurToxicologymedicine.disease_causeAntioxidantsLipid peroxidationchemistry.chemical_compoundCricetulusCricetinaemedicineAnimalschemistry.chemical_classificationGlutathione peroxidaseGeneral MedicineGlutathionePropoxurMalondialdehydeGlutathionechemistryBiochemistryLipid PeroxidationAldicarbOxidative stressFood ScienceFood and Chemical Toxicology
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Effects of four carbamate compounds on antioxidant parameters

2009

Abstract The effect of four carbamates, aldicarb and its metabolites (aldicarb sulfone and aldicarb sulfoxide) and propoxur on glutathione content and the activity of the enzymes involved in the sulfur-redox cycle in the mammalian cellular model CHO-K1 cells after 24-h exposure were determined. Carbamate exposure resulted in a depletion of intracellular reduced glutathione (GSH) content, no change was observed in oxidized glutathione (GSSG) and a decrease in GSH/GSSG ratio was detected. After carbamates exposition a GSH/GSSG decreases in ranged from 12.44% to 21.35% of control was observed. Depletion of GSH levels was accompanied by the induction of glutathione reductase (GR) after 24 h exp…

InsecticidesCarbamateAntioxidantAldicarbHealth Toxicology and Mutagenesismedicine.medical_treatmentGlutathione reductaseCHO CellsPropoxurmedicine.disease_causeAntioxidantschemistry.chemical_compoundCricetulusCricetinaemedicineAnimalschemistry.chemical_classificationGlutathione PeroxidaseGlutathione DisulfideGlutathione peroxidasePublic Health Environmental and Occupational HealthGeneral MedicineGlutathionePropoxurGlutathionePollutionOxidative StressGlutathione ReductasechemistryBiochemistryEnzyme InductionAldicarbOxidative stressEcotoxicology and Environmental Safety
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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