Search results for "Rauwolfia"

showing 10 items of 33 documents

Cytotoxicity of the indole alkaloid reserpine from Rauwolfia serpentina against drug-resistant tumor cells.

2015

Abstract Background: The antihypertensive reserpine is an indole alkaloid from Rauwolfia serpentina and exerts also profound activity against cancer cells in vitro and in vivo. The present investigation was undertaken to investigate possible modes of action to explain its activity toward drug-resistant tumor cells. Material and methods: Sensitive and drug-resistant tumor cell lines overexpressing P-glycoprotein (ABCB1/MDR1), breast cancer resistance protein (ABCG2/BCRP), mutation-activated epidermal growth factor receptor (EGFR), wild-type and p53-knockout cells as well as the NCI panel of cell lines from different tumor origin were analyzed. Reserpine's cytotoxicity was investigated by res…

ATP Binding Cassette Transporter Subfamily BReserpineAngiogenesisPharmaceutical SciencePharmacologyBiologyRauwolfiaGene Knockout TechniquesCell Line TumorDrug DiscoverymedicineATP Binding Cassette Transporter Subfamily G Member 2HumansCytotoxicityPharmacologyWnt signaling pathwayReserpineAntineoplastic Agents PhytogenicDrug Resistance MultipleNeoplasm ProteinsErbB ReceptorsMolecular Docking SimulationComplementary and alternative medicineCell cultureApoptosisDoxorubicinDrug Resistance NeoplasmCancer cellMolecular MedicineATP-Binding Cassette TransportersErlotinibTumor Suppressor Protein p53medicine.drugPhytomedicine : international journal of phytotherapy and phytopharmacology
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Arbutin synthase, a novel member of the NRD1β glycosyltransferase family, is a unique multifunctional enzyme converting various natural products and …

2002

Plant glucosyltransferases (GTs) play a crucial role in natural product biosynthesis and metabolization of xenobiotics. We expressed the arbutin synthase (AS) cDNA from Rauvolfia serpentina cell suspension cultures in Escherichia coli with a 6 x His tag and purified the active enzyme to homogeneity. The recombinant enzyme had a temperature optimum of 50 degrees C and showed two different pH optima (4.5 and 6.8 or 7.5, depending on the buffer). Out of 74 natural and synthetic phenols and two cinnamyl alcohols tested as substrates for the AS, 45 were accepted, covering a broad range of structural features. Converting rates comparable to hydroquinone were not achieved. In contrast to this broa…

DNA ComplementaryStereochemistryMolecular Sequence DataClinical BiochemistryPharmaceutical ScienceBiochemistryRauwolfiaSubstrate SpecificityXenobioticschemistry.chemical_compoundGlucosyltransferasesBiosynthesisMultienzyme ComplexesDrug DiscoveryGlycosyltransferaseGlycosylAmino Acid SequenceCloning MolecularMolecular BiologyPhylogenychemistry.chemical_classificationBiological ProductsBase SequenceSequence Homology Amino AcidbiologyOrganic ChemistryArbutinArbutinTemperatureGlycosyltransferasesSubstrate (chemistry)Hydrogen-Ion ConcentrationRecombinant ProteinsKineticsEnzymeBiochemistrychemistrybiology.proteinMolecular MedicineGlucosyltransferaseSequence AlignmentBioorganic & Medicinal Chemistry
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Acetyltransfer in natural product biosynthesis--functional cloning and molecular analysis of vinorine synthase.

2004

Vinorine synthase (EC 2.3.1.160) catalyses the acetyl-CoA- or CoA-dependent reversible formation of the alkaloids vinorine (or 11-methoxy-vinorine) and 16-epi-vellosimine (or gardneral). The forward reaction leads to vinorine, which is a direct biosynthetic precursor along the complex pathway to the monoterpenoid indole alkaloid ajmaline, an antiarrhythmic drug from the Indian medicinal plant Rauvolfia serpentina. Based on partial peptide sequences a cDNA clone was isolated and functionally expressed in Escherichia coli. The Km values of the native enzyme for gardneral and acetyl-CoA were determined to be 7.5 and 57 microM. The amino acid sequence of vinorine synthase has highest level of i…

DNA ComplementaryStereochemistrySequence analysisClinical BiochemistryMolecular Sequence DataPharmaceutical ScienceSequence alignmentBiochemistryRauwolfiaIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundBiosynthesisAcetyltransferasesSequence Analysis ProteinDrug DiscoveryConsensus sequenceAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencechemistry.chemical_classificationATP synthasebiologyChemistryOrganic ChemistryAcetylationAmino acidBiochemistryAcetyltransferasebiology.proteinMutagenesis Site-DirectedMolecular MedicineSequence AlignmentBioorganicmedicinal chemistry
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Deoxysarpagine Hydroxylase — A Novel Enzyme Closing a Short Side Pathway of Alkaloid Biosynthesis in Rauvolfia

2002

Microsomal preparations from cell suspension cultures of the Indian plant Rauvolfia serpentina catalyze the hydroxylation of deoxysarpagine under formation of sarpagine. The newly discovered enzyme is dependent on NADPH and oxygen. It can be inhibited by typical cytochrome P450 inhibitors such as cytochrome c, ketoconazole, metyrapone, tetcyclacis and carbon monoxide. The CO-effect is reversible with light (450 nm). The data indicate that deoxysarpagine hydroxylase is a novel cytochrome P450-dependent monooxygenase. A pH optimum of 8.0 and a temperature optimum of 35 degrees C were determined. K(m) values were 25 microM for NADPH and 7.4 microM for deoxysarpagine. Deoxysarpagine hydroxylase…

Deoxysarpagine hydroxylase activityLightCytochromeStereochemistryClinical BiochemistryPharmaceutical ScienceBiochemistryRauwolfiaIndole AlkaloidsHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemRauvolfia serpentinaDrug DiscoveryMolecular BiologyPlant Proteinschemistry.chemical_classificationCarbon MonoxidebiologyChemistryDeoxysarpagine hydroxylaseCytochrome cOrganic ChemistryTemperatureHydrogen-Ion ConcentrationMonooxygenasebiology.organism_classificationSecologanin Tryptamine AlkaloidsKineticsEnzymeBiochemistrybiology.proteinMolecular MedicineAryl Hydrocarbon HydroxylasesNADPBioorganic & Medicinal Chemistry
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Analysis of Rauwolfia Alkaloids Employing Capillary Electrophoresis-Mass Spectrometry

1997

Abstract Capillary electrophoresis-mass spectrometry (CE-MS) was applied to analyse extracts of roots and cell suspension cultures from Rauwolfia serpentina. Most of the alkaloids known to be present in the respective plant material have been resolved via CE and assigned according to their electrospray mass spectra.

ElectrosprayChromatographyCapillary electrophoresisApocynaceaebiologyRauwolfia alkaloidCapillary actionChemistryMass spectrumMolecular MedicineMass spectrometrybiology.organism_classificationCapillary electrophoresis–mass spectrometryNatural Product Letters
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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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Glucosylation of isatin-3-oxime followed by 2D in situ NMR in plant cells at highest magnetic field without labelling.

2001

The glucosylation of isatin-3-oxime (1) was monitored by in situ 2D 1H-13C inverse correlated gradient assisted NMR spectroscopy in plant cell suspension cultures of Rauvolfia serpentina without labelling. The applied high magnetic field of 800 MHz allowed measurements within 20 min at concentrations of 1 of 5.76 mM. Complete glucosylation of 1 occurs inside the cells within 72 hours. During this time isatin-3-oxime-glucoside (2) accumulates without further metabolism.

In situIsatinGlycosylationAnalytical chemistryCatalysisMass SpectrometryRauwolfiaGlucosidesRauvolfia serpentinaLabellingCulture TechniquesNuclear Magnetic Resonance BiomolecularChromatography High Pressure LiquidChromatographyPlants MedicinalbiologyMolecular StructureChemistrybeta-GlucosidaseMetabolismNuclear magnetic resonance spectroscopyPlant cellbiology.organism_classificationCarbonMagnetic fieldMolecular MedicineIsatin-3-oximeHydrogenNatural product letters
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Purification, partial amino acid sequence and structure of the product of raucaffricine-O-β-d-glucosidase from plant cell cultures of Rauwolfia serpe…

1999

Plant cell suspension cultures of Rauwolfia produce within 1 week approximately 250 nkat/l of raucaffricine-O-beta-D-glucosidase. A five step procedure using anion exchange chromatography, chromatography on hydroxylapatite, gel filtration and FPLC-chromatography on Mono Q and Mono P delivered in a yield of 0.9% approximately 1200-fold enriched glucosidase. A short protocol employing DEAE sepharose, TSK 55 S gel chromatography and purification on Mono Q gave a 5% recovery of glucosidase which was 340-fold enriched. SDS-PAGE showed a Mr for the enzyme of 61 kDa. The enzyme is not glycosylated. Structural investigation of the enzyme product, vomilenine, demonstrated that the alkaloid exists in…

LinamaraseMolecular Sequence DataSize-exclusion chromatographyPlant ScienceHorticultureBiologyBiochemistryMass SpectrometryRauwolfiaIndole AlkaloidsGel permeation chromatographychemistry.chemical_compoundHydrolaseAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyPeptide sequenceCells CulturedPlant Proteinschemistry.chemical_classificationEndoproteinase Lys-CPlants Medicinalbeta-GlucosidaseGeneral MedicineSecologanin Tryptamine AlkaloidsAmino acidMolecular WeightDEAE-SepharosechemistryBiochemistrybiology.proteinCell DivisionGlucosidasesPhytochemistry
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3-Oxo-rhazinilam:  A New Indole Alkaloid from Rauvolfia serpentina × Rhazya stricta Hybrid Plant Cell Cultures

2000

A new monoterpenoid indole alkaloid, 3-oxo-rhazinilam (1), was isolated from intergeneric somatic hybrid cell cultures of Rauvolfia serpentina and Rhazya stricta, and the structure was determined by detailed 1D and 2D NMR analysis. It was also proved that 3-oxo-rhazinilam (1) is a natural constituent of the hybrid cells.

Magnetic Resonance SpectroscopyLactamsPharmaceutical SciencePharmacognosyRhazya strictaRhazinilamMass SpectrometryRauwolfiaAnalytical Chemistrychemistry.chemical_compoundAlkaloidsRauvolfia serpentinaDrug DiscoveryBotanyCells CulturedPharmacologyPlants MedicinalIndole alkaloidbiologyApocynaceaeOrganic ChemistryIndolizinesbiology.organism_classificationCoculture TechniquesTerpenoidSomatic fusionComplementary and alternative medicinechemistryMolecular MedicineSpectrophotometry UltravioletJournal of Natural Products
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In vivo NMR at 800 MHz to monitor alkaloid metabolism in plant cell cultures without tracer labeling.

2001

Magnetic Resonance SpectroscopyPlants MedicinalChemistryGeneral ChemistryNuclear magnetic resonance spectroscopyPlant cellBiochemistrySecologanin Tryptamine AlkaloidsCatalysisRauwolfiaColloid and Surface ChemistryBiochemistryIn vivoTRACERSecologanin Tryptamine AlkaloidsAlkaloid metabolismJournal of the American Chemical Society
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