Search results for "Glucosyltransferases"

showing 10 items of 28 documents

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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Characterization of the cleavage site and function of resulting cleavage fragments after limited proteolysis of Clostridium difficile toxin B (TcdB) …

2005

Clostridium difficiletoxin B (TcdB) is a single-stranded protein consisting of a C-terminal domain responsible for binding to the host cell membrane, a middle part involved in internalization, and the N-terminal catalytic (toxic) part. This study shows that TcdB is processed by a single proteolytic step which cleaves TcdB10463between Leu543and Gly544and the naturally occurring variant TcdB8864between Leu544and Gly545. The cleavage occurs at neutral pH and is catalysed by a pepstatin-sensitive protease localized in the cytoplasm and on the cytoplasmic face of intracellular membranes. The smaller N-terminal cleavage products [63 121 Da (TcdB10463) and 62 761 Da (TcdB8864)] harbour the cytotox…

Endosomemedia_common.quotation_subjectBacterial ToxinsMolecular Sequence DataClostridium difficile toxin BCleavage (embryo)MicrobiologyCricetulusBacterial ProteinsCricetinaeChlorocebus aethiopsAnimalsAmino Acid SequenceInternalizationLungVero CellsCells Culturedmedia_commonHost cell membraneClostridioides difficileChemistryFibroblastsMolecular biologyCytosolBiochemistryGlucosyltransferasesCytoplasmIntracellularPeptide HydrolasesSubcellular FractionsMicrobiology
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Genetic rearrangements in the pathogenicity locus of Clostridium difficile strain 8864 – implications for transcription, expression and enzymatic act…

1998

The pathogenicity locus (PaLoc) of Clostridium difficile isolate 8864 was investigated to locate genetic rearrangements that would explain the exceptional pathogenicity of this particular isolate. Two major changes were defined: an insertion of 1.1 kb between the two genes tcdA and tcdE, coding for the enterotoxin and an accessory protein of unknown function, respectively, and a deletion of 5.9 kb encompassing the 3' ends of tcdA and tcdC. Transcription of the tcdA-E genes is severely affected by both rearrangements, explaining the demonstrated complete lack of TcdA polypeptide. We present a model of coordinate, growth-related transcription of the tcdA-E genes that confirms our previous fin…

GlycosylationGlycoside HydrolasesTranscription GeneticBacterial ToxinsMolecular Sequence DataLocus (genetics)Chromosomal translocationEnterotoxinBiologyHomology (biology)law.inventionBacterial ProteinsGTP-Binding ProteinslawTranscription (biology)GeneticsAmino Acid SequenceMolecular BiologyGeneGeneticsClostridioides difficileGene Expression Regulation BacterialMolecular biologyRecombinant ProteinsAntisense RNAGenes BacterialGlucosyltransferasesRecombinant DNASequence AlignmentMolecular and General Genetics MGG
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Lack of correlation between trehalose accumulation, cell viability and intracellular acidification as induced by various stresses in Saccharomyces ce…

1998

A pma1-1 mutant of Saccharomyces cerevisiae with reduced H+-ATPase activity and the isogenic wild-type strain accumulated high levels of trehalose in response to a temperature upshift to 40 éC and after addition of 10% ethanol, but only modest levels in response to a rapid drop in external pH and after addition of decanoic acid. There was, however, no correlation between the absolute levels of trehalose in the stressed cells and their viability. All these treatments induced a significant decrease in intracellular pH, and surprisingly, this decrease was very similar in both strains, indicating that intracellular acidification could not be the triggering mechanism for trehalose accumulation i…

Hot TemperatureTime FactorsATP synthaseEthanolIntracellular pHMutantSaccharomyces cerevisiaeTrehaloseSaccharomyces cerevisiaeBiologyHydrogen-Ion Concentrationbiology.organism_classificationMicrobiologyTrehaloseYeastArtificial Gene FusionFungal Proteinschemistry.chemical_compoundchemistryBiochemistryGlucosyltransferasesbiology.proteinViability assayAcidsIntracellularMicrobiology (Reading, England)
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Age- and training-related changes in the collagen metabolism of rat skeletal muscle

1989

The effects of ageing and life-long endurance training on the collagen metabolism of skeletal muscle were evaluated in a longitudinal study. Wistar rats performed treadmill running 5 days a week for 2 years. The activities of collagen biosynthesis enzymes, prolyl-4-hydroxylase and galactosylhydroxylysyl glucosyltransferase, were highest in the muscles of the youngest animals, decreased up to the age of 2 months and from then on remained virtually unchanged. The enzyme activity in young animals was higher in the slow collagenous soleus muscle than in the rectus femoris muscle. The enzyme activity in the soleus muscle was higher for older trained rats than older untrained rats. The relative p…

MaleAgingmedicine.medical_specialtyPhysiologyProcollagen-Proline DioxygenaseConnective tissueRectus femoris muscleBiologyEndurance trainingPhysical Conditioning AnimalPhysiology (medical)Internal medicinemedicineAnimalsOrthopedics and Sports MedicineSoleus muscleMusclesPublic Health Environmental and Occupational HealthSkeletal muscleRats Inbred StrainsGeneral MedicineEnzyme assayRatsmedicine.anatomical_structureEndocrinologyGlucosyltransferasesAgeingbiology.proteinCollagenType I collagenEuropean Journal of Applied Physiology and Occupational Physiology
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Increased prolyl 4-hydroxylase activity in the myocardium of endurance-trained mice.

1983

Endurance training over 3, 10 or 20 days increased the activity of prolyl 4-hydroxylase (PH) in the left ventricle of mice. No increase was observed in the weight of the left ventricle, in galactosylhydroxylysyl glucosyltransferase activity or in hydroxyproline concentration. The increase in PH suggests that the synthesis of collagen increases during physiological adaptation of the heart to endurance exercise without changes in the ventricle weight or its total collagen content.

Malemedicine.medical_specialtyHeart VentriclesProcollagen-Proline DioxygenaseBiologyCellular and Molecular NeuroscienceHydroxyprolinechemistry.chemical_compoundMiceEndurance trainingInternal medicinemedicineAnimalsMolecular BiologyPharmacologychemistry.chemical_classificationMyocardiumCell BiologyOrgan SizeHydrogen-Ion ConcentrationGalactosylhydroxylysyl glucosyltransferaseEnzymemedicine.anatomical_structureEndocrinologychemistryVentricleGlucosyltransferasesPhysical EnduranceMolecular MedicineExperientia
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Increased activities of prolyl 4-hydroxylase and galactosylhydroxylysyl glucosyltransferase, enzymes of collagen biosynthesis, in skeletal muscle of …

1983

The activities of prolyl 4-hydroxylase (PH) and galactosylhydroxylysyl glucosyltransferase (GGT), and the concentration of 4-hydroxyproline were measured in red and white parts of quadriceps femoris muscle of mice after 3, 10, and 20 sessions of daily endurance training. The activities of PH and GGT increased in the red part of the muscle after training for 3 and 10 times and returned to the control level after 20 training sessions. In the white muscle the increase of PH activity was less than in the red muscle. No alteration in GGT activity was observed in the white muscle. The concentration of hydroxyproline was unchanged in the both types of skeletal muscle. The results suggest that coll…

Malemedicine.medical_specialtyTime FactorsPhysiologyClinical BiochemistryProcollagen-Proline DioxygenaseBiologyHydroxyprolinechemistry.chemical_compoundMiceEndurance trainingPhysiology (medical)Internal medicinePhysical Conditioning AnimalmedicineAnimalsReceptorchemistry.chemical_classificationMusclesSkeletal muscleMolecular medicineQuadriceps femoris muscleHindlimbGalactosylhydroxylysyl glucosyltransferaseHydroxyprolinemedicine.anatomical_structureEnzymeEndocrinologychemistryGlucosyltransferasesPflugers Archiv : European journal of physiology
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Nocturnin in the demosponge Suberites domuncula: a potential circadian clock protein controlling glycogenin synthesis in sponges

2012

Sponges are filter feeders that consume a large amount of energy to allow a controlled filtration of water through their aquiferous canal systems. It has been shown that primmorphs, three-dimensional cell aggregates prepared from the demosponge Suberites domuncula and cultured in vitro , change their morphology depending on the light supply. Upon exposure to light, primmorphs show a faster and stronger increase in DNA, protein and glycogen content compared with primmorphs that remain in the dark. The sponge genome contains nocturnin, a light/dark-controlled clock gene, the protein of which shares a high sequence similarity with the related molecule of higher metazoans. The sponge nocturnin …

Models MolecularAryl hydrocarbon receptor nuclear translocatorGlycogeninPeriod (gene)Circadian clockGene ExpressionBiochemistry03 medical and health sciencesCryptochromeComplementary DNAAnimalsRNA Messenger14. Life underwaterMolecular BiologyDNA PrimersGlycoproteins030304 developmental biology0303 health sciencesBase SequencebiologyCircadian Rhythm Signaling Peptides and Proteins030302 biochemistry & molecular biologyNuclear ProteinsCell Biologybiology.organism_classificationCircadian RhythmSuberites domunculaCLOCKBiochemistryGlucosyltransferasesSuberitesTranscription FactorsBiochem. J.
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Separation by FPLC chromatofocusing of UDP-glucosyltransferases from three developmental stages of Drosophila melanogaster.

1997

Variation of UDP-glucosyltransferase activity, during Drosophila melanogaster development, was analyzed. The endogenous metabolite xanthurenic acid and the xenobiotic compounds 1-naphthol and 2-naphthol were used as substrates. Developmentally regulated differences were observed for the three substrates, suggesting the presence of UDP-glucosyltransferase isoenzymes. This was further confirmed by FPLC chromatofocusing on a Mono P column: seven peaks of UDP-glucosyltransferase activity (pHs: ≥6.3, 5.8, 5.5, 4.9, 4.5, 4.2, ≤4.0) with either single or overlapping substrate specificity were detected. A single xanthurenic acid:UDP-glucosyltransferase activity (pl 5.8) was found throughout develop…

PhysiologyMetaboliteOvipositionBiochemistryIsozymeGene Expression Regulation EnzymologicSubstrate Specificitychemistry.chemical_compoundGlucosyltransferasesAnimalsXanthurenic acidChromatography High Pressure LiquidbiologyChromatofocusingGene Expression Regulation DevelopmentalFast protein liquid chromatographyGeneral Medicinebiology.organism_classificationIsoenzymesDrosophila melanogasterchemistryBiochemistryGlucosyltransferasesInsect ScienceChromatography GelFemaleDrosophila melanogasterXenobioticArchives of insect biochemistry and physiology
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Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences.

2000

Plant cell suspension cultures of Rauvolfia are able to produce a high amount of arbutin by glucosylation of exogenously added hydroquinone. A four step purification procedure using anion exchange, hydrophobic interaction, hydroxyapatite-chromatography and chromatofocusing delivered in a yield of 0.5%, an approximately 390 fold enrichment of the involved glucosyltransferase. SDS-PAGE showed a M(r) for the enzyme of 52 kDa. Proteolysis of the pure enzyme with endoproteinase LysC revealed six peptide fragments with 9-23 amino acids which were sequenced. Sequence alignment of the six peptides showed high homologies to glycosyltransferases from other higher plants.

RauvolfiaStereochemistryMolecular Sequence DataPeptidePlant ScienceHorticultureBiochemistryRauwolfiachemistry.chemical_compoundRauvolfia serpentinaAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChromatographyPlants MedicinalbiologyChromatofocusingArbutinGeneral Medicinebiology.organism_classificationChromatography Ion ExchangePeptide FragmentsAmino acidMolecular WeightKineticsEnzymeDurapatitechemistryBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseElectrophoresis Polyacrylamide GelPhytochemistry
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