Search results for "Substrate Specificity"

showing 10 items of 217 documents

Partial purification and characterization of an NAD-dependent 3 beta-hydroxysteroid dehydrogenase from Clostridium innocuum

1989

In nine strains of Clostridium innocuum, 3 beta-hydroxysteroid-dehydrogenating activities were detected. 3 beta, 7 alpha, 12 alpha-Trihydroxy- and 3 beta-hydroxy-12-keto-5 beta-cholanoic acids were identified as reduction products of the respective 3-keto bile acids by gas-liquid chromatography and gas-liquid chromatography-mass spectrometry. One strain was shown to contain a NAD-dependent 3 beta-hydroxysteroid dehydrogenase. Enzyme production was constitutive in the absence of added bile acids. The specific enzyme activity was significantly reduced by growth medium supplementation with 3-keto bile acids, with trisubstituted acids being more effective than disubstituted ones. A pH optimum o…

3-Hydroxysteroid DehydrogenasesIon chromatographyDehydrogenaseApplied Microbiology and BiotechnologySubstrate SpecificityBile Acids and SaltsFeceschemistry.chemical_compoundHumansNucleotideClostridiumchemistry.chemical_classificationGrowth mediumChromatographyClostridium innocuumEcologybiologyHydrogen-Ion Concentrationbiology.organism_classificationMolecular WeightKineticsEnzymechemistryBiochemistryNAD+ kinaseBacteriaResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

1999

Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains of Alzheimer’s disease patients, is derived by proteolytic cleavage of the amyloid precursor protein (APP). Proteolytic cleavage of APP by a putative α-secretase within the Aβ sequence precludes the formation of the amyloidogenic peptides and leads to the release of soluble APPsα into the medium. By overexpression ofa disintegrinandmetalloprotease (ADAM), classified as ADAM 10, in HEK 293 cells, basal and protein kinase C-stimulated α-secretase activity was increased severalfold. The proteolytically activated form of ADAM 10 was localized by cell surface biotinylation in the plasma membrane, but the m…

ADAM10Molecular Sequence DataBiologyKidneyTransfectionCell LineSubstrate SpecificityADAM10 ProteinAmyloid beta-Protein PrecursorEndopeptidasesAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPoint MutationADAM17 ProteinAmino Acid SequenceCloning MolecularProtein kinase AProtein Kinase CSecretory pathwayBinding SitesMultidisciplinaryHEK 293 cellsP3 peptideMembrane ProteinsMetalloendopeptidasesBiological SciencesPeptide FragmentsRecombinant Proteinscarbohydrates (lipids)ADAM ProteinsKineticsZincAlpha secretaseBiochemistryMutagenesis Site-Directedbiology.proteinCattleAmyloid Precursor Protein SecretasesProceedings of the National Academy of Sciences
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Human liver cytosolic epoxide hydrolases.

1988

Human liver epoxide hydrolases were characterized by several criteria and a cytosolic cis-stilbene oxide hydrolase (cEHcso) was purified to apparent homogeneity. Styrene oxide and five phenylmethyloxiranes were tested as substrates for human liver epoxide hydrolases. With microsomes activity was highest with trans-2-methylstyrene oxide, followed by styrene 7, 8-oxide, cis-2-With methylstyrene oxide, cis-1,2-dimethylstyrene oxide, trans-1, 2-dimethylstyrene oxide and 2, 2-dimethylstyrene oxide. With cytosol the same order was obtained for the first three substrates, whereas activity with 2, 2-dimethylstyrene oxide was higher than with cis-1,2-dimethylstyrene oxide and no hydrolysis occurred …

AdultBiochemistryStyreneSubstrate Specificitychemistry.chemical_compoundCytosolStyrene oxideHydrolaseAnimalsHumansEpoxide hydrolaseEpoxide HydrolasesImmunochemistryChromatography Ion ExchangeRatsIsoelectric pointchemistryBiochemistryLiverMicrosomal epoxide hydrolaseEpoxide HydrolasesMicrosomeChromatography GelMicrosomes LiverEpoxy CompoundsElectrophoresis Polyacrylamide GelIsoelectric FocusingEuropean journal of biochemistry
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Determinants of Substrate Specificity in the NS3 Serine Proteinase of the Hepatitis C Virus

1997

AbstractProcessing of the nonstructural polyprotein of the hepatitis C virus (HCV) requires the serine-type proteinase located in the amino-terminal domain of NS3. To identify residues within NS3 determining substrate specificity, a mutation analysis was performed. Using sequence alignments and three-dimensional structure predictions, amino acids assumed to be important for specificity were replaced and the enzymes were tested in an intracellulartrans-processing assay for their effects on cleavage of an NS4B-5B substrate. For some of the substitutions at positions 133, 134, 135, 136, 138, 152, 155, 157, and 169, slightly reduced processing efficiencies were observed but in no case was the s…

Alaninechemistry.chemical_classificationModels MolecularNS3virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsAmino acidSubstrate SpecificitySerinechemistryBiochemistryValineVirologyHumansAmino Acid SequenceThreonineLeucineIsoleucineSequence AlignmentVirology
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Diastereoselective Synthesis of 2-Phenylselenenyl-1,3-anti-Diols and 2-Phenylselenenyl-1,3-anti-Azido-Alcohols via Hydroxy- and Azido-Selenenylation …

2005

A method to synthesize 2-phenylselenenyl-1,3-anti-diols and 2-phenyl- selenenyl-1,3-anti-azidoalcohols via hydroxy- or azido-selenenylation of trans-allylic alcohols is reported. Moreover, the first example of hydroxyl-selenenylation of an allylic azide is presented. Yields ranging from moderate to good and diastereomeric ratios up to 95:5 are achieved.

Allylic rearrangementAzidesPropanolsPharmaceutical SciencediolsSelenic AcidHydroxylationModels BiologicalArticleAnalytical ChemistrySubstrate Specificitylcsh:QD241-441seleniraniun ionchemistry.chemical_compoundlcsh:Organic chemistryOrganoselenium CompoundsDrug DiscoveryOrganic chemistryPhysical and Theoretical ChemistrySelenium Compoundsseleniraniun ion.organic chemicalsOrganic ChemistryDiastereomerfood and beveragesStereoisomerismSettore CHIM/06 - Chimica Organicadiastereoselective synthesis azido selenelylazation reactionchemistryChemistry (miscellaneous)AlcoholsMolecular MedicineAzideMolecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
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A highly enantioselective abiotic receptor for malate dianion in aqueous solution

2006

The highly enantioselective molecular recognition of the malate dianion by a synthetic receptor in aqueous solution has been studied by potentiometric titrations, mass spectrometry (ESI-MS), diffusion measurements (PGSE NMR) and molecular modeling. Garcia-España Monsonis, Enrique, Enrique.Garcia-Es@uv.es

AnionsModels MolecularMalate dianionSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyMolecular modelUNESCO::QUÍMICADiffusionPotentiometric titrationMalatesMolecular modelingAbiotic receptorMass spectrometry:QUÍMICA [UNESCO]CatalysisSubstrate SpecificityMolecular recognitionComputational chemistryMaterials ChemistryOrganic chemistryAqueous solutionReceptorAbiotic componentEnantioselectiveAqueous solutionMolecular StructureChemistrySpectrometryMeasurementsMetals and AlloysEnantioselective synthesisWaterHydrogen BondingStereoisomerismGeneral ChemistryGeneral MedicineUNESCO::QUÍMICA::Química macromolecularCombinatorial chemistrySurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsSolutionsCeramics and CompositesPotentiometryEnantioselective ; Abiotic receptor ; Malate dianion ; Aqueous solution ; Spectrometry ; Measurements ; Molecular modeling:QUÍMICA::Química macromolecular [UNESCO]
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Mechanism of interaction of betanin and indicaxanthin with human myeloperoxidase and hypochlorous acid.

2005

Hypochlorous acid (HOCl) is the most powerful oxidant produced by human neutrophils and contributes to the damage caused by these inflammatory cells. It is produced from H2O2 and chloride by the heme enzyme myeloperoxidase (MPO). Based on findings that betalains provide antioxidant and anti-inflammatory effects, we performed the present kinetic study on the interaction between the betalains, betanin and indicaxanthin, with the redox intermediates, compound I and compound II of MPO, and its major cytotoxic product HOCl. It is shown that both betalains are good peroxidase substrates for MPO and function as one-electron reductants of its redox intermediates, compound I and compound II. Compoun…

AntioxidantIndolesHypochlorous acidStereochemistryPyridinesmedicine.medical_treatmentBiophysicsIn Vitro TechniquesBiochemistryMedicinal chemistryRedoxAntioxidantsSubstrate Specificitychemistry.chemical_compoundBetalainmedicineHumansMolecular BiologyBetaninPeroxidasebiologyBetanin myeloperoxidase nitrite low-density lipoproteins atherosclerosisCell BiologyOxidantsBetaxanthinsHypochlorous AcidKineticschemistryMyeloperoxidasebiology.proteinFerricBetacyaninsInflammation MediatorsIndicaxanthinOxidation-Reductionmedicine.drugBiochemical and biophysical research communications
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New evidence for the multiplicity of ubiquinone- and inhibitor-binding sites in the mitochondrial complex I.

2000

Determination of the number of ubiquinone- and inhibitor-binding sites in the mitochondrial complex I (NADH:ubiquinone oxidoreductase) is a controversial question with a direct implication for elaborating a suitable model to explain the bioenergetic mechanism of this complicated enzyme. We have used combinations of both selective inhibitors and common ubiquinone-like substrates to demonstrate the multiplicity of the reaction centers in the complex I in contrast with competition studies that have suggested the existence of a unique binding site for ubiquinone. Our results provide new evidence for the existence of at least two freely exchangeable ubiquinone-binding sites with different specif…

BioenergeticsStereochemistryUbiquinoneSubmitochondrial ParticlesBiophysicsBiologyIn Vitro TechniquesBiochemistryModels BiologicalMitochondria HeartSubstrate SpecificityOxidoreductaseAnimalsNADH NADPH OxidoreductasesBinding siteMultiplicity (chemistry)Molecular Biologychemistry.chemical_classificationNADH-Ubiquinone OxidoreductaseBinding SitesElectron Transport Complex IKineticsEnzymechemistryBiochemistryCattleEnergy MetabolismMitochondrial Complex IArchives of biochemistry and biophysics
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UDP-glucosyltransferase activity toward exogenous substrates in Drosophila melanogaster.

1991

To investigate the capacity of Drosophila extracts to glucosylate exogenous substrates we have developed a fast and sensitive method for the detection of UDP-glucosyltransferase activity using 4-nitrophenol, 1-naphthol, or 2-naphthol as substrates. High-performance liquid chromatography was used to separate and quantitate the reaction products, allowing detection of activities that produced as little as 1 pmol of 2-naphthol glucoside (fluorescence detection) or 16 pmol of 4-nitrophenol glucoside (absorbance detection). Optimal activity was found at 43 degrees C and alkaline pH. The affinity of the Drosophila enzyme was 250-fold higher for 1-naphthol or 2-naphthol (Km approximately 4 microM)…

BiophysicsNaphtholsBiochemistryHigh-performance liquid chromatographyUridine DiphosphateSubstrate SpecificityAbsorbanceNitrophenolschemistry.chemical_compoundGlucosideDrosophilidaeAnimalsMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChromatographybiologySubstrate (chemistry)Cell BiologyHydrogen-Ion Concentrationbiology.organism_classificationFluorescenceEnzymeDrosophila melanogasterchemistryBiochemistryGlucosyltransferasesDrosophila melanogasterAnalytical biochemistry
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Selective chromo-fluorogenic detection of DFP (a Sarin and Soman mimic) and DCNP (a Tabun mimic) with a unique probe based on a boron dipyrromethene …

2014

[EN] A novel colorimetric probe (P4) for the selective differential detection of DFP (a Sarin and Soman mimic) and DCNP (a Tabun mimic) was prepared. Probe P4 contains three reactive sites; i.e. (i) a nucleophilic phenol group able to undergo phosphorylation with nerve gases, (ii) a carbonyl group as a reactive site for cyanide; and (iii) a triisopropylsilyl (TIPS) protecting group that is known to react with fluoride. The reaction of P4 with DCNP in acetonitrile resulted in both the phosphorylation of the phenoxy group and the release of cyanide, which was able to react with the carbonyl group of P4 to produce a colour modulation from pink to orange. In contrast, phosphorylation of P4 with…

Boron CompoundsSarinORGANOPHOSPHATE PESTICIDESAcetonitrilesCyanideSomanColorSilica GelNERVE AGENTSCHEMICAL WARFARE AGENTSBiochemistryACETYLCHOLINESTERASESubstrate Specificitychemistry.chemical_compoundQUIMICA ORGANICALimit of DetectionSomanmedicineSENSORSNANOPARTICLESPhenolOrganic chemistryHumansChemical Warfare AgentsPhysical and Theoretical ChemistryPhosphorylationProtecting groupTabunNerve agentLANTHANIDE IONSReagent StripsRHODAMINE-BOrganic ChemistryQUIMICA INORGANICAMolecular MimicryMembranes ArtificialSarinOrganophosphatesFLUORESCENTchemistryMolecular ProbesSolventsColorimetryBODIPYFIELD-EFFECT TRANSISTORSNuclear chemistrymedicine.drugOrganicbiomolecular chemistry
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