Search results for "Substrate Specificity"

showing 10 items of 217 documents

Carotenoid binding sites in LHCIIb

2000

The major light-harvesting complex of photosystem II can be reconstituted in vitro from its bacterially expressed apoprotein with chlorophylls a and b and neoxanthin, violaxanthin, lutein, or zeaxanthin as the only xanthophyll. Reconstitution of these one-carotenoid complexes requires low-stringency conditions during complex formation and isolation. Neoxanthin complexes (containing 30–50% of the all-trans isomer) disintegrate during electrophoresis, exhibit a largely reduced resistance against proteolytic attack; in addition, energy transfer from Chl b to Chl a is easily disrupted at elevated temperature. Complexes reconstituted in the presence of either zeaxanthin or lutein contain nearly …

ChlorophyllLuteinPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesXanthophyllsBiologyBinding CompetitiveBiochemistrySubstrate SpecificityLight-harvesting complexchemistry.chemical_compoundNeoxanthinZeaxanthinsTrypsinProtein PrecursorsCarotenoidPlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll ALuteinPhotosystem II Protein Complexfood and beveragesPigments BiologicalPlantsbeta CaroteneCarotenoidseye diseasesZeaxanthinEnergy TransferchemistryBiochemistryXanthophyllElectrophoresis Polyacrylamide GelApoproteinsViolaxanthinEuropean Journal of Biochemistry
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Determination of major human cytochrome P450s activities in 96-well plates using liquid chromatography tandem mass spectrometry.

2007

At the early stage of drug discovery, thousands of new chemical entities (NCEs) may be screened before a single candidate can be identified for development. Evaluation of the effect of NCEs on human CYP450 enzyme activities is a key issue in pharmaceutical development as it may explain inter-subject variability, drug-drug interactions, non-linear pharmacokinetics and toxic effects. A liquid chromatography tandem mass spectrometry (HPLC-MS/MS) method has been developed for the fast and routine analysis of major human CYP450s enzyme activities (CYP1A2, CYP2A6, CYP2B6, CYP2C9, CYP2C19, CYP2D6, CYP2E1 and CYP3A4) in primary hepatocyte cell cultures. The high sensitivity and selectivity of mass …

ChromatographyChemistryDrug discoveryCYP1A2Drug Evaluation PreclinicalGeneral MedicineToxicologyTandem mass spectrometryMass spectrometrySubstrate SpecificityPharmacokineticsCytochrome P-450 Enzyme SystemLiquid chromatography–mass spectrometryTandem Mass SpectrometryDrug DesignHepatocytesHumansCYP2A6Drug metabolismCells CulturedChromatography LiquidToxicology in vitro : an international journal published in association with BIBRA
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Core Histones Are Glutaminyl Substrates for Tissue Transglutaminase

1996

Chicken erythrocyte core histones are glutaminyl substrates in the transglutaminase (TGase) reaction with monodansylcadaverine (DNC) as donor amine. The modification is very fast when compared with that of many native substrates of TGase. Out of the 18 glutamines of the four histones, nine (namely glutamine 95 of H2B; glutamines 5, 19, and 125 of H3; glutamines 27 and 93 of H4; and glutamines 24, 104, and 112 of H2A) are the amine acceptors in free histones. The use of Gln112 of H2A requires a temperature-dependent partial unfolding of the histone, showing that structural determinants are decisive for the glutamine specificity. The structures of H2A and H2B do not appreciably change upon mo…

Circular dichroismErythrocytesTissue transglutaminaseGlutamineGuinea PigsMolecular Sequence DataIn Vitro TechniquesBiochemistrySubstrate SpecificityHistoneschemistry.chemical_compoundCadaverineAnimalsNucleosomeAmino Acid SequenceMolecular BiologyPeptide sequenceTransglutaminasesMolecular StructurebiologyMethylamineCell BiologyNucleosomesChromatinGlutamineKineticsHistonechemistryBiochemistrybiology.proteinJournal of Biological Chemistry
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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

1995

Processing of the hepatitis C virus polyprotein is accomplished by a series of cotranslational and posttranslational cleavages mediated by host cell signalases and two virally encoded proteinases. Of these the NS3 proteinase is essential for processing at the NS3/4A, NS4A/4B, NS4B/5A, and NS5A/5B junctions. Processing between NS3 and NS4A occurs in cis, implying an intramolecular reaction mechanism, whereas cleavage at the other sites can also be mediated in trans. Sequence analysis of the amino termini of mature cleavage products and comparisons of amino acid residues around the scissile bonds of various hepatitis C virus isolates identified amino acid residues which might contribute to su…

Cleavage factorvirusesMolecular Sequence DataImmunologyHepacivirusCleavage and polyadenylation specificity factorViral Nonstructural ProteinsBiologyCleavage (embryo)MicrobiologySubstrate SpecificityScissile bondVirologyHumansAmino Acid SequenceAmino AcidsPeptide sequencechemistry.chemical_classificationNS3Cleavage stimulation factorHydrolysisSerine Endopeptidasesbiochemical phenomena metabolism and nutritionAmino acidchemistryBiochemistryMutagenesisInsect ScienceProtein Processing Post-TranslationalRNA HelicasesHeLa CellsResearch ArticleJournal of Virology
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Strategies to In Vitro Assessment of Major Human CYP Enzyme Activities by Using Liquid Chromatography Tandem Mass Spectrometry

2008

At the early stage of drug discovery, thousands of new chemical entities (NCEs) may be screened before a single candidate can be identified for development. Determining the role of CYP enzymes in the metabolism of a compound and evaluating the effect of NCEs on human CYP activities are key issues in pharmaceutical development as they may explain inter-subject variability, drug-drug interactions, non-linear pharmacokinetics and toxic effects. Reliable methods for determining enzyme activities are needed to characterize an individual CYP enzyme and to obtain a tool for the evaluation of its role in drug metabolism in humans. Different liquid chromatography tandem mass spectrometry methodologi…

Clinical BiochemistryDrug Evaluation PreclinicalIn Vitro TechniquesTandem mass spectrometrySubstrate SpecificityCytochrome P-450 Enzyme SystemPharmacokineticsTandem Mass SpectrometryIn vivoLiquid chromatography–mass spectrometryCytochrome P-450 Enzyme InhibitorsHumansPharmacokineticsEnzyme inducerChromatography High Pressure LiquidCytochrome P-450 Enzyme InhibitorsPharmacologyChromatographybiologyDrug discoveryChemistryPharmaceutical PreparationsBiochemistryEnzyme InductionHepatocytesMicrosomes Liverbiology.proteinDrug metabolismCurrent Drug Metabolism
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Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface.

2003

In most lipases a mobile element or lid domain covers the catalytic site of the enzyme and the lid opening event, which usually proceed at a lipid-water interface, is required to form the catalytically competent lipase. We report here a noticeable increase in activity of two fungal lipases assayed in aqueous solution in absence of any interface when adding submicellar concentrations of amphipathic physiological molecules like long-chain acyl-CoAs. The catalytic activity was dramatically dependent on the acyl chain length of the amphiphile and could be related with a lid-opening process. Our data support that lipase activation can be triggered in the absence of a well-defined interface, and …

Conformational changeCatalysisSubstrate SpecificityAcyl-CoAchemistry.chemical_compoundAmphiphileLipaseMolecular Biologychemistry.chemical_classificationAqueous solutionbiologyChemistryWaterEstersCell BiologyLipaseLipid MetabolismGeotrichumLipidsEnzyme ActivationSolutionsEnzymeBiochemistrybiology.proteinAcyl Coenzyme ALong chainRhizopusBiochimica et biophysica acta
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Comparison of virtual high-throughput screening methods for the identification of phosphodiesterase-5 inhibitors.

2011

Reliable and effective virtual high-throughput screening (vHTS) methods are desperately needed to minimize the expenses involved in drug discovery projects. Here, we present an improvement to the negative image-based (NIB) screening: the shape, the electrostatics, and the solvation state of the target protein’s ligand-binding site are included into the vHTS. Additionally, the initial vHTS results are postprocessed with molecular mechanics/generalized Born surface area (MMGBSA) calculations to estimate the favorability of ligand-protein interactions. The results show that docking produces very good early enrichment for phosphodiesterase-5 (PDE-5); however, in general, the NIB and the ligand-…

Cyclic Nucleotide Phosphodiesterases Type 5Virtual screeningHigh-Throughput Screening MethodsDrug discoveryChemistryGeneral Chemical EngineeringHigh-throughput screeningMedical screeningStatic ElectricityDrug Evaluation PreclinicalNanotechnologyGeneral ChemistryComputational biologyLibrary and Information SciencesMolecular Dynamics SimulationPhosphodiesterase 5 InhibitorsLigandsComputer Science ApplicationsHigh-Throughput Screening AssaysSubstrate SpecificityUser-Computer InterfaceDocking (molecular)Catalytic DomainJournal of chemical information and modeling
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A convenient chemo-enzymatic synthesis and 18F-labelling of both enantiomers of trans-1-toluenesulfonyloxymethyl-2-fluoromethyl-cyclopropane

2008

The present report is concerned with a stereoselective, reliable route to trans-1,2-disubstituted cyclopropanes and in particular to (S,S)-1-tosyloxymethyl-2-fluoromethyl-cyclopropane (1) and (R,R)-1-tosyloxymethyl-2-fluoromethyl-cyclopropane (ent-1) as conformationally restricted, terminally fluorinated C4-building blocks for medicinal chemistry. The enzymatic kinetic resolution based synthesis of 1 and ent-1 utilises inexpensive, commercially available starting materials. It is based on enantiomeric resolution of rac-cyclopropane carboxylic esters using esterase from Streptomyces diastatochromogenes. Both enantiomers of 1 were prepared selectively in high overall yield over nine steps, st…

CyclopropanesFluorine RadioisotopesStaining and LabelingStereochemistryOrganic ChemistryRadiosynthesisEsterasesStereoisomerismBiochemistryEsteraseStreptomycesSubstrate SpecificityCyclopropaneKinetic resolutionchemistry.chemical_compoundchemistryYield (chemistry)Ethyl acrylateOrganic chemistryStereoselectivityPhysical and Theoretical ChemistryEnantiomerTolueneOrganic & Biomolecular Chemistry
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Isoenzyme-specific phosphorylation of cytochromes P-450 and other drug metabolizing enzymes.

1987

Abstract A series of fourteen cytochrome P-450 isoenzymes was treated with three different protein kinases and found to devide into isoenzymes phosphorylated (i) by both the cyclic AMP-dependent kinase and the calcium-phospholipid-dependent kinase (P-450 PB 3a and PB 2e), (ii) by none of these kinases (P-450 PB 1b, MC 1b, UT 1, and thromboxane synthase), and (iii) by either the cyclic AMP-dependent kinase (P-450 LM 2, PB 2d, and PB 3b) or the calcium-phospholipid-dependent kinase (P-450 PB 1a, PB 2a, MC 1a, LM 3c, and LM 4). Other components of the monooxygenase system, cytochrome P-450 reductase, cytochrome b5, cytochrome b5 reductase as well as microsomal epoxide hydrolase, were poor subs…

CytochromeBiophysicsReductaseBiochemistrySubstrate SpecificityCytochrome P-450 Enzyme SystemCytochrome b5Cyclic AMPAnimalsPhosphorylationMolecular BiologyCytochrome b5 reductaseProtein Kinase CGlutathione TransferasebiologyChemistryKinaseCell BiologyMonooxygenaseMolecular biologyRatsIsoenzymesBiochemistryPharmaceutical PreparationsMicrosomal epoxide hydrolasebiology.proteinThromboxane-A synthaseRabbitsCasein KinasesProtein KinasesBiochemical and biophysical research communications
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All-Atom simulations disclose how cytochrome reductase reshapes the substrate access/egress routes of its partner cyp450s

2020

Cytochromes P450 enzymes (CYP450s) promote the oxidative metabolism of a variety of substrates via the electrons supplied by the cytochrome P450 reductase (CPR) and upon formation of a CPR/CYP450 adduct. In spite of the pivotal regulatory importance of this process, the impact of CPR binding on the functional properties of its partner CYP450 remains elusive. By performing multiple microsecond-long all-Atom molecular dynamics simulations of a 520â »000-Atom model of a CPR/CYP450 adduct embedded in a membrane mimic, we disclose the molecular terms for their interactions, considering the aromatase (HA) enzyme as a proxy of the CYP450 family. Our study strikingly unveils that CPR binding alters…

CytochromeStereochemistryeducationPlasma protein binding-ReductaseMolecular Dynamics Simulation010402 general chemistry01 natural sciencesSubstrate SpecificityElectron Transport03 medical and health sciencesAromataseCytochrome P-450 Enzyme Systemhealth services administrationHumansddc:530General Materials Sciencecardiovascular diseasesP450 EnzymesPhysical and Theoretical Chemistryhealth care economics and organizations030304 developmental biologyNADPH-Ferrihemoprotein Reductase0303 health sciencesOxidative metabolismbiologyChemistrySubstrate (chemistry)Cytochrome P450 reductaseElectron transport chain0104 chemical sciencesAromatase; Cytochrome P-450 Enzyme System; Electron Transport; Humans; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Protein Binding; Substrate SpecificitySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteintherapeuticsProtein Binding
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