Search results for "Activation"

showing 10 items of 2079 documents

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

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
researchProduct

Promiscuity in alkaline phosphatase superfamily. Unraveling evolution through molecular simulations.

2011

We here present a theoretical study of the alkaline hydrolysis of a phosphodiester (methyl p-nitrophenyl phosphate or MpNPP) in the active site of Escherichia coli alkaline phosphatase (AP), a monoesterase that also presents promiscuous activity as a diesterase. The analysis of our simulations, carried out by means of molecular dynamics (MD) simulations with hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, shows that the reaction takes place through a D(N)A(N) or dissociative mechanism, the same mechanism employed by AP in the hydrolysis of monoesters. The promiscuous activity observed in this superfamily can be then explained on the basis of a conserved reaction mechanism. …

Models MolecularReaction mechanismStereochemistrydnaNAlkaline hydrolysis (body disposal)AlkaliesMolecular Dynamics SimulationBiochemistryMolecular mechanicsCatalysisMolecular dynamicsColloid and Surface ChemistryCatalytic DomainphosphodiesterEscherichia colibiologyChemistryHydrolysisActive siteGeneral ChemistryAlkaline PhosphataseEnzymesEnzyme ActivationPhosphodiester bondbiology.proteinAlkaline phosphataseQuantum Theoryalkaline phosphataseJournal of the American Chemical Society
researchProduct

Structural requirements for V2 vasopressin receptor proteolytic cleavage.

1999

The ligand-induced proteolytic cleavage of the V2 vasopressin receptor transiently expressed in COS cells was investigated. After incubation of the cell membranes with a photoreactive ligand possessing full agonistic properties for V2 receptors, approximately 90% of the porcine and bovine V2 vasopressin receptors were cleaved in the upper part of transmembrane helix 2 at a heptapeptide sequence conserved in both vasopressin and oxytocin receptors. The oxytocin receptor was completely resistant to proteolysis after binding the same photoreactive ligand, which is only a partial agonist for this receptor. Chimeric V2/oxytocin receptors obtained by transfer of extracellular domains of the oxyto…

Models MolecularReceptors VasopressinDNA ComplementaryTime FactorsProtein ConformationSwineMolecular Sequence DataBiologyLigandsTransfectionBiochemistryArginine vasopressin receptor 2Enzyme-linked receptorCyclic AMPAnimalsHumansPoint Mutation5-HT5A receptorAmino Acid SequenceCloning MolecularReceptorProtease-activated receptor 2Vasopressin receptorArginine vasopressin receptor 1BDose-Response Relationship DrugSequence Homology Amino AcidProteinsOxytocin receptorProtein Structure TertiaryEnzyme ActivationBiochemistryMicroscopy FluorescenceReceptors OxytocinType C PhospholipasesCOS CellsMutagenesis Site-DirectedCattlehormones hormone substitutes and hormone antagonistsAdenylyl CyclasesProtein BindingEuropean journal of biochemistry
researchProduct

Glutamate 270 plays an essential role in K+-activation and domain closure ofThermus thermophilusisopropylmalate dehydrogenase

2014

The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect…

Models MolecularStereochemistry030303 biophysicsMutantBiophysicsGlutamic AcidLarge scale facilities for research with photons neutrons and ionsSmall angle X-ray scatteringDehydrogenaseBiochemistry3-Isopropylmalate Dehydrogenase03 medical and health scienceschemistry.chemical_compoundIsopropylmalate dehydrogenaseFluorescence resonance energy transferStructural BiologyOxidoreductaseGeneticsMolecular BiologyX-ray crystallography030304 developmental biologychemistry.chemical_classificationSite-directed mutagenesis0303 health sciencesNicotinamidebiologyThermus thermophilusActivation by K+Cell BiologyThermus thermophilusbiology.organism_classificationProtein Structure TertiaryMOPSEnzyme ActivationKineticsCrystallographyEnzymechemistryMutationNAD+ kinaseFEBS Letters
researchProduct

Toward very potent, non-covalent organophosphonate inhibitors of cathepsin C and related enzymes by 2-amino-1-hydroxy-alkanephosphonates dipeptides

2013

Cathepsins play an important role in several human disorders and therefore the design and synthesis of their inhibitors attracts considerable interest in current medicinal chemistry approaches. Due to the presence of a strong sulphydryl nucleophile in the active center of the cysteine type cathepsins, most strategies to date have yielded covalent inhibitors. Here we present a series of non-covalent β-amino-α-hydroxyalkanephosphonate dipeptidic inhibitors of cathepsin C, ranking amongst the best low-molecular weight inhibitors of this enzyme. Their binding modes determined by molecular modelling indicate that the hydroxymethyl fragment of the molecule, not the phosphonate moiety, acts as a t…

Models MolecularStereochemistryhydroxyphosphonateBiochemistryCathepsin CCathepsin BCathepsin CInhibitory Concentration 50chemistry.chemical_compoundCathepsin OTransition state analogCathepsin KHumanscysteine proteasePeptide bondcathepsinAminesEnzyme InhibitorsCathepsinDipeptideChemistryMolecular MimicryDipeptidesGeneral MedicineOrganophosphatesEnzyme ActivationinhibitorBiochemistryHydroxy AcidsBiochimie
researchProduct

Interfacial activation-based molecular bioimprinting of lipolytic enzymes

1995

Interfacial activation-based molecular (bio)-imprinting (IAMI) has been developed to rationally improve the performance of lipolytic enzymes in nonaqueous environments. The strategy combinedly exploits (i) the known dramatic enhancement of the protein conformational rigidity in a water-restricted milieu and (ii) the reported conformational changes associated with the activation of these enzymes at lipid-water interfaces, which basically involves an increased substrate accessibility to the active site and/or an induction of a more competent catalytic machinery. Six model enzymes have been assayed in several model reactions in nonaqueous media. The results, rationalized in light of the presen…

Models MolecularSurface PropertiesSwineStereochemistryPhospholipases ACatalysisEnzyme activatorBiomolèculesAnimalsLipasePancreaschemistry.chemical_classificationMultidisciplinarybiologyWaterSubstrate (chemistry)Active siteLipaseCombinatorial chemistryEnzyme ActivationPhospholipases AEnzymechemistrySolventsbiology.proteinEnzimsResearch Article
researchProduct

A Molecular Electron Density Theory Study of the Reactivity of Azomethine Imine in [3+2] Cycloaddition Reactions

2017

The electronic structure and the participation of the simplest azomethine imine (AI) in [3+2] cycloaddition (32CA) reactions have been analysed within the Molecular Electron Density Theory (MEDT) using DFT calculations at the MPWB1K/6-311G(d) level. Electron localisation function (ELF) topological analysis reveals that AI has a pseudoradical structure, while the conceptual DFT reactivity indices characterise this TAC as a moderate electrophile and a good nucleophile. The non-polar 32CA reaction of AI with ethylene takes place through a one-step mechanism with low activation energy, 5.3 kcal/mol-1. A bonding evolution theory (BET) study indicates that this reaction takes place through a non-…

Models MolecularThiosemicarbazones[3+2] cycloaddition reactionsImineMolecular Conformationmolecular mechanismsazomethine iminePharmaceutical ScienceElectronsElectronic structureActivation energy010402 general chemistry01 natural sciencesArticlebonding evolution theoryAnalytical Chemistrychemistry.chemical_compoundNucleophileComputational chemistryDrug Discoveryconceptual density functional theoryMoleculeReactivity (chemistry)organic_chemistryelectron densityPhysical and Theoretical Chemistryazomethine imine; [3+2] cycloaddition reactions; molecular electron density theory; conceptual density functional theory; electron localisation function; bonding evolution theory; electron density; molecular mechanisms; chemical reactivityCycloaddition ReactionMolecular Structure010405 organic chemistrymolecular electron density theoryOrganic ChemistryCycloaddition0104 chemical scienceschemistryChemistry (miscellaneous)ElectrophileQuantum TheoryThermodynamicsMolecular MedicineDensity functional theoryImineselectron localisation functionAzo Compoundschemical reactivityMolecules; Volume 22; Issue 5; Pages: 750
researchProduct

Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
researchProduct

Development of new Coumarin-based profluorescent substrates for human cytochrome P450 enzymes

2018

Cytochrome P450 (CYP) enzymes constitute an essential xenobiotic metabolizing system that regulates the elimination of lipophilic compounds from the body. Convenient and affordable assays for CYP enzymes are important for assessing these metabolic pathways.In this study, 10 novel profluorescent coumarin derivatives with various substitutions at carbons 3, 6 and 7 were developed. Molecular modeling indicated that 3-phenylcoumarin offers an excellent scaffold for the development of selective substrate compounds for various human CYP forms, as they could be metabolized to fluorescent 7-hydroxycoumarin derivatives. Oxidation of profluorescent coumarin derivatives to fluorescent metabolites by 1…

Models MolecularentsyymitoxidationHealth Toxicology and MutagenesisToxicology030226 pharmacology & pharmacyBiochemistrycoumarinFluorescence03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCytochrome P-450 Enzyme SystemCoumarinsCYPenzyme kineticsderivativeCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme kineticskumariiniCYP2A6ta317Pharmacologychemistry.chemical_classificationBenzoflavonesbiologyChemistryCYP1A2fluoresenssiCytochrome P450substraatit (kemia)General MedicineCoumarindrug metabolismMolecular Docking SimulationMetabolic pathwayKineticsEnzymeBiochemistrylääkekemia030220 oncology & carcinogenesisInactivation Metabolicbiology.proteinMicrosomes LiverOxidation-ReductionDrug metabolism
researchProduct