Search results for "Substrate Specificity"

showing 10 items of 217 documents

2′,5′-oligoadenylate synthetase from a lower invertebrate, the marine sponge Geodia cydonium, does not need dsRNA for its enzymatic activity

2002

AbstractRecently, the presence of 2′,5′-linked oligoadenylates and a high 2′,5′-oligoadenylate synthetase activity were discovered in a lower invertebrate, the marine sponge Geodia cydonium. It has been demonstrated that mammalian 2–5A synthetase isozymes require a dsRNA cofactor for their enzymatic activity. Our results show that, unlike mammalian 2–5A synthetases, the 2–5A synthetase from the sponge acts in a dsRNA-independent manner in vitro. A prolonged incubation of the G. cydonium extract with a high concentration of a micrococcal nuclease had no effect on the activity of the 2–5A synthetase. At the same time, the micrococcal nuclease was effective within 30 min in degrading dsRNA nee…

Gene isoformInterferon InducersGeodia cydoniumdsRNABiologyIsozymePC12 CellsCofactorSubstrate SpecificitySpecies SpecificitySponge2'5'-Oligoadenylate SynthetaseAnimalsMicrococcal Nuclease2–5A synthetaseMolecular BiologyRNA Double-Strandedchemistry.chemical_classificationOligoribonucleotidesEnzymatic activity2'-5'-OligoadenylateAdenine NucleotidesRNACell BiologyHydrogen-Ion ConcentrationEnzymes ImmobilizedIn vitroPoriferaRatsEnzymePoly I-CBiochemistrychemistrybiology.proteinMicrococcal nucleaseBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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The diversity of GABAA receptors. Pharmacological and electrophysiological properties of GABAA channel subtypes.

1998

The amino acid gamma-aminobutyric-acid (GABA) prevails in the CNS as an inhibitory neurotransmitter that mediates most of its effects through fast GABA-gated Cl(-)-channels (GABAAR). Molecular biology uncovered the complex subunit architecture of this receptor channel, in which a pentameric assembly derived from five of at least 17 mammalian subunits, grouped in the six classes alpha, beta, gamma, delta, sigma and epsilon, permits a vast number of putative receptor isoforms. The subunit composition of a particular receptor determines the specific effects of allosterical modulators of the GABAARs like benzodiazepines (BZs), barbiturates, steroids, some convulsants, polyvalent cations, and et…

Gene isoformMacromolecular SubstancesProtein ConformationProtein subunitNeuroscience (miscellaneous)LoreclezoleConvulsantsBiologyInhibitory postsynaptic potentialGABAA-rho receptorSubstrate SpecificityGABA AntagonistsCellular and Molecular NeuroscienceBenzodiazepinesMiceChloride ChannelsmedicineAnimalsHumansProtein IsoformsReceptorGABA Agonistsgamma-Aminobutyric AcidAnestheticsMice KnockoutBinding SitesIon TransportGABAA receptorReceptors GABA-ARecombinant ProteinsRatsElectrophysiologyNeurologyBiochemistryBarbituratesSteroidsHeterologous expressionIon Channel Gatingmedicine.drugMolecular neurobiology
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Efficient Expression and Crystallization System of Cancer-Associated Carbonic Anhydrase Isoform IX.

2015

Human carbonic anhydrase IX (CA IX) is overexpressed in a number of solid tumors and is considered to be a marker for cellular hypoxia that it is not produced in most normal tissues. CA IX contributes to the acidification of the extracellular matrix, which, in turn, favors tumor growth and metastasis. Therefore, CA IX is considered to be a promising anti-cancer drug target. However, the ability to specifically target CA IX is challenging due to the fact that the human genome encodes 15 different carbonic anhydrase isoforms that have a high degree of homology. Furthermore, structure-based drug design of CA IX inhibitors so far has been largely unsuccessful due to technical difficulties regar…

Gene isoformModels MolecularAntineoplastic AgentsIsozymePichiaPichia pastorisSubstrate SpecificityStructure-Activity RelationshipX-Ray DiffractionAntigens NeoplasmCarbonic anhydraseNeoplasmsDrug DiscoverymedicineStructure–activity relationshipHumansCloning MolecularCarbonic Anhydrase IXCarbonic Anhydrase InhibitorsDatabases ProteinCarbonic Anhydraseschemistry.chemical_classificationbiologyChemistryLyasebiology.organism_classificationAcetazolamideIsoenzymesEnzymeBiochemistrybiology.proteinMolecular MedicineAcetazolamideCrystallizationBaculoviridaemedicine.drugJournal of medicinal chemistry
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Midgut aminopeptidase N isoforms from Ostrinia nubilalis: Activity characterization and differential binding to Cry1Ab and Cry1Fa proteins from Bacil…

2013

Aminopeptidase N (APN) isoforms from Lepidoptera are known for their involvement in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis. These enzymes belong to a protein family with at least eight different members that are expressed simultaneously in the midgut of lepidopteran larvae. Here, we focus on the characterization of the APNs from Ostrinia nubilalis (OnAPNs) to identify potential Cry receptors. We expressed OnAPNs in insect cells using a baculovirus system and analyzed their enzymatic activity by probing substrate specificity and inhibitor susceptibility. The interaction with Cry1Ab and Cry1Fa proteins (both found in transgenic insect-resistant maize) was …

Gene isoformendocrine systemCD13 AntigensMothsBiochemistrySubstrate SpecificityOstriniaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisToxicity TestsSf9 CellsAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis ToxinsbiologyfungiMidgutbiology.organism_classificationLigand (biochemistry)Molecular biologyEndotoxinsGastrointestinal TractIsoenzymesBlotEnzymechemistryBiochemistryInsect ScienceProtein BindingInsect Biochemistry and Molecular Biology
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Active Site Mapping of Xylan-Deconstructing Enzymes with Arabinoxylan Oligosaccharides Produced by Automated Glycan Assembly

2017

Xylan-degrading enzymes are crucial for the deconstruction of hemicellulosic biomass, making the hydrolysis products available for various industrial applications such as the production of biofuel. To determine the substrate specificities of these enzymes, we prepared a collection of complex xylan oligosaccharides by automated glycan assembly. Seven differentially protected building blocks provided the basis for the modular assembly of 2-substituted, 3-substituted, and 2-/3-substituted arabino- and glucuronoxylan oligosaccharides. Elongation of the xylan backbone relied on iterative additions of C4-fluorenylmethoxylcarbonyl (Fmoc) protected xylose building blocks to a linker-functionalized …

GlycanGlycoside HydrolasesStereochemistryOligosaccharidesSOLID-PHASE SYNTHESISXylose010402 general chemistryARABINOXYLANPLANT CELL WALL01 natural sciencesCatalysisSubstrate Specificity//purl.org/becyt/ford/1 [https]chemistry.chemical_compoundHydrolysisCellvibrioGlucuronoxylanCatalytic DomainArabinoxylan//purl.org/becyt/ford/1.4 [https]Organic chemistryBacteroidesGlycoside hydrolaseSolid-Phase Synthesis Techniqueschemistry.chemical_classificationbiology010405 organic chemistryHydrolysisCARBOHYDRATESOtras Ciencias QuímicasOrganic ChemistryCiencias QuímicasActive siteGeneral ChemistryXylan0104 chemical sciencescarbohydrates (lipids)Xylosidaseschemistrybiology.proteinXylansENZYMESCIENCIAS NATURALES Y EXACTAS
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Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis.

2003

The plant enzyme arbutin synthase isolated from cell suspension cultures of Rauvolfia serpentina and heterologously expressed in Escherichia coli is a member of the NRD1beta family of glycosyltransferases. This enzyme was used to prove, by site-directed mutagenesis, suggested catalytic domains and reaction mechanisms proposed for enzyme-catalyzed glycosylation. Replacement of amino acids far from the NRD domain do not significantly affect arbutin synthase activity. Exchange of amino acids at the NRD site leads to a decrease of enzymatic activity, e.g. substitution of Glu368 by Asp. Glu368, which is a conserved amino acid in glycosyltransferases located at position 2 and is important for enz…

GlycosylationStereochemistryMolecular Sequence DataBiologyBiochemistryPolymerase Chain ReactionGene Expression Regulation EnzymologicRauwolfiaSubstrate Specificitychemistry.chemical_compoundCatalytic DomainGlycosyltransferaseEscherichia coliAmino Acid SequenceSite-directed mutagenesisConserved SequenceDNA Primerschemistry.chemical_classificationBinding SitesATP synthaseSequence Homology Amino AcidMutagenesisArbutinGlycosyltransferasesEnzyme assayRecombinant ProteinsAmino acidEnzymechemistryBiochemistryAmino Acid Substitutionbiology.proteinMutagenesis Site-DirectedEuropean journal of biochemistry
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Oxidative DNA base damage induced by singlet oxygen and photosensitization: recognition by repair endonucleases and mutagenicity.

2000

We have analyzed the recognition by various repair endonucleases of DNA base modifications induced by three oxidants, viz. [4-(tert-butyldioxycarbonyl)benzyl]triethylammonium chloride (BCBT), a photochemical source of tert-butoxyl radicals, disodium salt of 1,4-etheno-2,3-benzodioxin-1,4-dipropanoic acid (NDPO(2)), a chemical source of singlet oxygen, and riboflavin, a type-I photosensitizer. The base modifications induced by BCBT, which were previously shown to be mostly 7,8-dihydro-8-oxoguanine (8-oxoGua) residues, were recognized by Fpg and Ogg1 proteins, but not by endonuclease IIII, Ntg1 and Ntg2 proteins. In the case of singlet oxygen induced damage, 8-oxoGua accounted for only 35% of…

GuanineDNA LigasesLightGuanineDNA damageRiboflavinMolecular Sequence DataToxicologySubstrate Specificitychemistry.chemical_compoundEndonucleaseBacterial ProteinsGeneticsPhotosensitizerPentosyltransferasesMolecular BiologybiologyBase SequenceSinglet oxygenEscherichia coli ProteinsMutagenesisCorticoviridaeProteinsEndonucleasesDNA-(apurinic or apyrimidinic site) lyaseOxygenBiochemistrychemistryDNA ViralMutationbiology.proteinOxidation-ReductionDNADNA DamageMutation research
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Distinct Site Specificity of Two Pea Histone Deacetylase Complexes

2001

We report on the site specificity of two intact pea histone deacetylase complexes. HD1 deacetylates lysines 5 and 16 of H4 in the order K16 > K5, while in the case of H3 the preferred order is K4 >> K18 approximately K9. The specificity of the HD2 complex is markedly different. The preferred residues in H4 are K8 approximately K5 > K16, while in H3 deacetylation, the complex HD2 prefers sites 4 and 18. To obtain these results, we have used a novel procedure based on the SPOT technique, a method to synthesize peptides on membrane supports. Different sets of membranes with sequentially overlapping histone peptides containing acetylated lysines in the sites corresponding to all in vivo acetyla…

Histone deacetylase 5Histone deacetylase 2ChemistryHDAC11HDAC10PeasSAP30BiochemistryHistone DeacetylasesSubstrate SpecificityBiochemistryHistone H2AHistone deacetylase complexDeacetylase activityBiochemistry
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Characterization of Acylating and Deacylating Activities of an Extracellular Phospholipase A2 in a Water-Restricted Environment

1994

The behavior of porcine pancreatic phospholipase A2 (ppPLA2) in monophasic low-water media has been explored, for the first time, in a systematic manner. It has been investigated how a number of variables can modulate both acylating and deacylating activities of the enzyme, and several interesting, unexpected results are presented. Among the most relevant, when placing ppPLA2 in the water-restricted environment, are the following: (i) it displays a remarkable alteration of its specificity toward the substrate polar head relative to all-water medium; (ii) it is quite severely inhibited by lysophosphatidylcholine (LPC), which has important implications, particularly concerning its acylation a…

Hot TemperatureSwineStereochemistryAcylationOleic AcidsBinding CompetitiveBiochemistryPhospholipases ASubstrate SpecificityAcylationchemistry.chemical_compoundPhospholipase A2Enzyme StabilityExtracellularAnimalsPancreasEdetic Acidchemistry.chemical_classificationEsterificationbiologyChemistryHydrolysisLysophosphatidylcholinesWaterSubstrate (chemistry)In vitroKineticsPhospholipases A2LysophosphatidylcholineEnzymeBiochemistryYield (chemistry)Phosphatidylcholinesbiology.proteinCalciumExtracellular SpaceOleic AcidBiochemistry
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Study and characterization of polyphenol oxidase from eggplant (Solanum melongena L.)

2011

ABSTRACT: In this study the catecholase and cresolase activities of eggplant polyphenol oxidase (PPO) were investigated. Enzyme activity was determined by measuring the increase in absorbance using catechol as substrate and 3-methyl-2- benzothiazolinone hydrazone (MBTH) as coupled reagent. The effects of substrate specificity, heat inactivation, temperature, pH, and inhibitors were investigated to understand the enzymatic alteration of ready-to-eat preparations. Browning of vegetables was determined through a colorimeter. Decrease of lightness (L*) and increase of color difference values (ΔE*) were correlated with tissue browning. Antibrowning agents were tested on PPO under the same condit…

Hot Temperaturefood industryCatecholsPolyphenol oxidaseSubstrate Specificitychemistry.chemical_compoundAcetic acidEnzyme StabilityBrowningSolanum melongenaFood scienceEnzyme InhibitorsbrowningCatecholbiologySubstrate (chemistry)traditional landracesGeneral ChemistrySettore AGR/15 - Scienze E Tecnologie AlimentariHydrogen-Ion Concentrationpolyphenol oxidase antibrowning food technologies ready-to-eatEnzyme assayMaillard ReactionKineticsBiochemistrychemistryaubergineTartaric acidbiology.proteingermplasm exploitationGeneral Agricultural and Biological SciencesCitric acidCatechol Oxidasetraditional landraces; browning; germplasm exploitation; food industry; aubergine
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