Search results for "Substrate"

showing 10 items of 1018 documents

Optimization Strategy of Novel Peptide-Based Michael Acceptors for the Treatment of Human African Trypanosomiasis

2019

This paper describes an optimization strategy of the highly active vinyl ketone 3 which was recognized as a strong inhibitor of rhodesain of Trypanosoma brucei rhodesiense, endowed with a ksecond v...

Trypanosoma brucei rhodesienseStrong inhibitorKetoneStereochemistryProtein ConformationPeptide01 natural sciences03 medical and health sciencesStructure-Activity RelationshipSUBSTRATEDrug DiscoverymedicineHumansAfrican trypanosomiasisSulfonesBIOLOGICAL EVALUATION030304 developmental biologyWARHEADchemistry.chemical_classification0303 health sciencesMolecular StructureChemistryDERIVATIVESTrypanosoma brucei rhodesienseCYSTEINE PROTEASES RHODESAIN BIOLOGICAL EVALUATION CATHEPSIN-L INHIBITORS BRUCEI PEPTIDOMIMETICS FALCIPAIN-2 DERIVATIVES SUBSTRATE WARHEADBRUCEImedicine.diseaseFALCIPAIN-2Trypanocidal Agents0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidasesTrypanosomiasis AfricanCYSTEINE PROTEASES RHODESAINCATHEPSIN-LMolecular MedicineINHIBITORSPEPTIDOMIMETICS
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Structure-based engineering of strictosidine synthase: auxiliary for alkaloid libraries.

2007

SummaryThe highly substrate-specific strictosidine synthase (EC 4.3.3.2) catalyzes the biological Pictet-Spengler condensation between tryptamine and secologanin, leading to the synthesis of about 2000 monoterpenoid indole alkaloids in higher plants. The crystal structure of Rauvolfia serpentina strictosidine synthase (STR1) in complex with strictosidine has been elucidated here, allowing the rational site-directed mutation of the active center of STR1 and resulting in modulation of its substrate acceptance. Here, we report on the rational redesign of STR1 by generation of a Val208Ala mutant, further describing the influence on substrate acceptance and the enzyme-catalyzed synthesis of 10-m…

TryptamineCHEMBIOLStrictosidine synthaseMICROBIOStereochemistryProtein ConformationClinical BiochemistryMutantDrug Evaluation PreclinicalMutation MissenseCrystallography X-RayProtein EngineeringBiochemistryIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaDrug DiscoveryCatharanthusCarbon-Nitrogen LyasesMolecular BiologyVinca AlkaloidsPlant ProteinsPharmacologybiologyMolecular StructureGeneral Medicinebiology.organism_classificationLyaseBiochemistrychemistryStrictosidinebiology.proteinMutagenesis Site-DirectedMolecular MedicineSecologaninProtein BindingChemistrybiology
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3D-Structure and function of strictosidine synthase--the key enzyme of monoterpenoid indole alkaloid biosynthesis.

2008

Strictosidine synthase (STR; EC 4.3.3.2) plays a key role in the biosynthesis of monoterpenoid indole alkaloids by catalyzing the Pictet-Spengler reaction between tryptamine and secologanin, leading exclusively to 3alpha-(S)-strictosidine. The structure of the native enzyme from the Indian medicinal plant Rauvolfia serpentina represents the first example of a six-bladed four-stranded beta-propeller fold from the plant kingdom. Moreover, the architecture of the enzyme-substrate and enzyme-product complexes reveals deep insight into the active centre and mechanism of the synthase highlighting the importance of Glu309 as the catalytic residue. The present review describes the 3D-structure and …

TryptamineStrictosidine synthaseATP synthasebiologyMolecular StructurePhysiologyStereochemistryProtein ConformationPlant Sciencebiology.organism_classificationSecologanin Tryptamine AlkaloidsSubstrate Specificitychemistry.chemical_compoundProtein structurechemistryBiosynthesisBiochemistryRauvolfia serpentinaStrictosidineCarbon-Nitrogen LyasesGeneticsbiology.proteinSecologaninVinca AlkaloidsPlant physiology and biochemistry : PPB
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Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine

2005

Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine were obtained by the hanging-drop technique at 302–304 K with potassium sodium tartrate tetrahydrate as precipitant. All crystals belong to space group R3. The native STR1 crystals diffract to 2.95 Å and have unit-cell parameters a = b = 150.3, c = 122.4 Å. The tryptamine complex crystals diffract to 2.38 Å, with unit-cell parameters a = b = 147.3, c = 122.3 Å.

TryptamineStrictosidine synthaseTetrahydratebiologyStereochemistryPotassium sodium tartrateSubstrate (chemistry)General MedicineRauwolfiaTryptamineslaw.inventionchemistry.chemical_compoundchemistryBiosynthesisStructural BiologylawCarbon-Nitrogen Lyasesbiology.proteinHeterologous expressionCrystallizationCrystallizationPlant ProteinsActa Crystallographica Section D Biological Crystallography
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ASSESSING SPREADABILITY OF WARM SEASON SPECIES USED FOR TURFGRASS ON THREE TYPES OF SUBSTRATE IN THE MEDITERRANEAN ENVIRONMENT

2014

The aim of the study was to examine the performance of turfgrass warm season species, including 6 varieties of Cynodon dactylon in comparison with Zoysia japonica and Paspalum vaginatum in three substrates with different soil textures (sandy loam, sandy clay loam, clay), to find the one or the ones that adapt best in the Mediterranean environment. The results showed the best perfomances in sandy loam substrate and for C.dactylon cv. Transcontinental, Capriola and La Paloma. Z. japonica, Zenith, had lower values.

Turfgrass substrate spreadability mediterranean environmentSettore AGR/02 - Agronomia E Coltivazioni Erbacee
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Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type …

1999

We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzym…

TyrosinaseCatecholschemistry.chemical_elementPhotochemistrySpectrum Analysis RamanBiochemistrylaw.inventionTreesInorganic Chemistrychemistry.chemical_compoundlawPolymer chemistryEnzyme InhibitorsElectron paramagnetic resonanceCatechol oxidaseCatecholBinding SitesCyanidesbiologyMonophenol MonooxygenaseSpectrophotometry AtomicElectron Spin Resonance SpectroscopySubstrate (chemistry)Bridging ligandHydrogen-Ion ConcentrationPlantsPhenylthioureaCopperMolecular WeightchemistryHemocyaninsbiology.proteinSpectrophotometry UltravioletOxygen bindingCatechol OxidaseCopperJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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Indirect oxidation of the antitumor agent procarbazine by tyrosinase—Possible application in designing anti-melanoma prodrugs

2008

The interaction of tyrosinase with the anticancer drug procarbazine has been investigated. In the presence of the enzyme alone no oxidation of this dialkylhydrazine above the background level was observed. However, when phenolic substrates (4-tert-butylcatechol or N-acetyl-l-tyrosine) were included in the reaction mixture, procarbazine was rapidly degraded. Oxygen consumption measurements showed that in a mixture both the phenolic substrate and the drug were oxidized. The major product of procarbazine degradation was isolated and identified as azoprocarbazine, the first active metabolite of this drug detected in previous in vivo and in vitro studies. This indirect oxidation of the hydrazine…

TyrosinaseClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentstyrosinaseProcarbazineBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundOxygen ConsumptionIn vivoDrug DiscoverymelanomamedicineOrganic chemistryProdrugsHydrazine (antidepressant)PhenolsMolecular BiologyActive metaboliteMolecular StructureMonophenol MonooxygenaseOrganic ChemistrySubstrate (chemistry)hydrazineProdrugHydrazineschemistryProcarbazineMolecular Medicineredox exchangeprodrugAgaricalesOxidation-Reductionmedicine.drugBioorganic & Medicinal Chemistry Letters
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NOSIP, a novel modulator of endothelial nitric oxide synthase activity.

2001

Production of nitric oxide (NO) in endothelial cells is regulated by direct interactions of endothelial nitric oxide synthase (eNOS) with effector proteins such as Ca2+-calmodulin, by posttranslational modifications such as phosphorylation via protein kinase B, and by translocation of the enzyme from the plasma membrane caveolae to intracellular compartments. Reversible acylation of eNOS is thought to contribute to the intracellular trafficking of the enzyme; however, protein factor(s) that govern the translocation of the enzyme are still unknown. Here we have used the yeast two-hybrid system and identified a novel 34 kDa protein, termed NOSIP (eNOS interacting protein), which avidly binds …

Ubiquitin-Protein LigasesMolecular Sequence DataCHO CellsCaveolaeBiochemistryNitric oxideSubstrate Specificitychemistry.chemical_compoundEnosCaveolaeCricetinaeTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyProtein kinase BCalcimycinBinding SitesbiologyAkt/PKB signaling pathwayGene Expression Profilingbiology.organism_classificationImmunohistochemistryPrecipitin TestsTransport proteinCell biologyNitric oxide synthaseProtein TransportchemistryBiochemistrybiology.proteinEndothelium VascularNitric Oxide SynthaseCarrier ProteinsSequence AlignmentIntracellularBiotechnologyProtein BindingFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Modeling of kinetic and static friction between an elastically bent nanowire and a flat surface

2011

Friction forces for a nanowire (NW) elastically bent on flat substrate were investigated both theoretically and experimentally. Models based on elastic beam theory were proposed considering balance of external, frictional, and elastic forces along the NW. The distributed friction force was determined for two cases: (i) the NW was uniformly dragged at its midpoint and bent by kinetic friction forces and (ii) the NW was held in a bent state by static friction forces. The first case considers a uniform distribution of kinetic friction along the NW and enables the measurement of the friction force from the elastically deformed NW profile. The second case exploits the interplay between static fr…

Uniform distribution (continuous)Materials scienceMechanical EngineeringBent molecular geometryNanowireNanotechnologySubstrate (electronics)MechanicsTribologyCondensed Matter PhysicsKinetic energyMomentumMechanics of MaterialsGeneral Materials ScienceWaferJournal of Materials Research
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A comparative evaluation of shear bond strength between feldspathic porcelain and lithium di silicate ceramic layered to a zirconia core? An in vitro…

2020

Background The bond strength between the zirconia core and ceramic veneer is the weakest component in the layered structure. Delamination of veneering ceramic is reported as one of the most frequent problems associated with Veneered Zirconia restorations. The aim of this study is to compare the shear bond strength of lithium di silicate porcelain to that of feldspathic porcelain on a zirconia Substrate. Material and Methods Two groups (group A and B) of zirconia blocks with each group having 20 samples were fabricated according to Schmitz Schulmeyer method. Group A (n =20 ) samples were veneered with feldspathic veneering porcelain and Group B (n=20) samples were veneered with heat pressed …

Universal testing machineMaterials scienceBond strengthResearchmedicine.medical_treatmentDelaminationchemistry.chemical_element:CIENCIAS MÉDICAS [UNESCO]Substrate (building)chemistryvisual_artUNESCO::CIENCIAS MÉDICASvisual_art.visual_art_mediummedicineLithiumVeneerCubic zirconiaCeramicOral SurgeryComposite materialGeneral Dentistry
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