Search results for "Glycosyltransferase"

showing 10 items of 22 documents

Expression of xyloglucan endotransglucosylase/hydrolase (XTH) genes and XET activity in ethylene treated apple and tomato fruits.

2013

[EN] Xyloglucan endotransglucosylase/hydrolase (XTHs: EC 2.4.1.207 and/or EC 3.2.1.151), a xyloglucan modifying enzyme, has been proposed to have a role during tomato and apple fruit ripening by loosening the cell wall. Since the ripening of climacteric fruits is controlled by endogenous ethylene biosynthesis, we wanted to study whether XET activity was ethylene-regulated, and if so, which specific genes encoding ripening-regulated XTH genes were indeed ethylene-regulated. XET specific activity in tomato and apple fruits was significantly increased by the ethylene treatment, as compared with the control fruits, suggesting an increase in the XTH gene expression induced by ethylene. The 25 Sl…

0106 biological sciencesEthylenePhysiologyPlant ScienceBiologyTransglucosylation and xyloglucan01 natural sciencesCell wall03 medical and health scienceschemistry.chemical_compoundSolanum lycopersicumPlant Growth RegulatorsGene Expression Regulation PlantGene expressionBIOQUIMICA Y BIOLOGIA MOLECULARGenePhylogeny030304 developmental biology2. Zero hunger0303 health sciencesSequence Homology Amino AcidCell wallAgriculturaGlycosyltransferasesfood and beveragesRipeningSequence Analysis DNAXyloglucan endotransglucosylaseEthylenesFruit ripeningXyloglucanMalus domesticachemistryBiochemistryFruitMalusClimactericAgronomy and Crop Science010606 plant biology & botany
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Xyloglucan endotransglucosylase/hydrolase (XTH) overexpression affects growth and cell wall mechanics in etiolated Arabidopsis hypocotyls.

2013

Abstract: Growth and biomechanics of etiolated hypocotyls from Arabidopsis thaliana lines overexpressing xyloglucan endotransglucosylase/hydrolase AtXTH18, AtXTH19, AtXTH20, and PttXET16-34 were studied. Overexpression of AtXTH18, AtXTH19, and AtXTH20 stimulated growth of hypocotyls, while PttXET16-34 overexpression did not show this effect. In vitro extension of frozen/thawed hypocotyls measured by a constant-load extensiometer started from a high-amplitude initial deformation followed by a slow time-dependent creep. Creep of growing XTH-overexpressing (OE) hypocotyls was more linear in time compared with the wild type at pH 5.0, reflecting their higher potential for long-term extension. X…

0106 biological sciencesPhysiologyArabidopsisPlant ScienceBiologyReal-Time Polymerase Chain Reaction01 natural sciencesHypocotylCell wall03 medical and health sciencesCell WallGene Expression Regulation PlantTensile StrengthArabidopsisArabidopsis thalianaXyloglucan:xyloglucosyl transferaseBiology030304 developmental biology0303 health sciencesAgriculturafungiWild typeGlycosyltransferasesfood and beveragesXyloglucan endotransglucosylasebiology.organism_classificationHypocotylBiochemistryEtiolationBiophysics010606 plant biology & botany
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Xyloglucan endotransglucosylase and cell wall extensibility

2011

Transgenic tomato hypocotyls with altered levels of an XTH gene were used to study how XET activity could affect the hypocotyl growth and cell wall extensibility. Transgenic hypocotyls showed significant over-expression (line 13) or co-suppression (line 33) of the SlXTH1 in comparison with the wild type, with these results being correlated with the results on specific soluble XET activity, suggesting that SlXTH1 translates mainly for a soluble XET isoenzyme. A relationship between XET activity and cell wall extensibility was found, and the highest total extensibility was located in the apical hypocotyl segment of the over-expressing SlXTH1 line, where the XET-specific activity and hypocotyl…

0106 biological sciencesPhysiologyBiologíaPlant ScienceBiologyPolysaccharidePolymerase Chain Reaction01 natural sciencesHypocotylCell wall03 medical and health scienceschemistry.chemical_compoundTransformation GeneticSolanum lycopersicumCell WallSpectroscopy Fourier Transform InfraredXyloglucan:xyloglucosyl transferaseGenetically modified tomatoPlant Proteins030304 developmental biologychemistry.chemical_classification0303 health sciencesfungiWild typeGlycosyltransferasesfood and beveragesXyloglucan endotransglucosylaseBlotting NorthernXyloglucanchemistryBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationAgronomy and Crop Science010606 plant biology & botany
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Evaluation of an amino acid residue critical for the specificity and activity of human Gb3/CD77 synthase

2016

Human Gb3/CD77 synthase (α1,4-galactosyltransferase) is the only known glycosyltransferase that changes acceptor specificity because of a point mutation. The enzyme, encoded by A4GALT locus, is responsible for biosynthesis of Gal(α1–4)Gal moiety in Gb3 (CD77, Pk antigen) and P1 glycosphingolipids. We showed before that a single nucleotide substitution c.631C > G in the open reading frame of A4GALT, resulting in replacement of glutamine with glutamic acid at position 211 (substitution p. Q211E), broadens the enzyme acceptor specificity, so it can not only attach galactose to another galactose but also to N-acetylgalactosamine. The latter reaction leads to synthesis of NOR antigens, which are…

0301 basic medicineAcetylgalactosamineMutation MissenseBiochemistryGlycosphingolipidsSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundGb3/CD77 synthaseBiosynthesisCell Line TumorGlycosyltransferaseAspartic acidHumansAsparagineSite-directed mutagenesisMolecular BiologySite-directed mutagenesisbiologyAntigens NuclearGlutamic acidCell BiologyGalactosyltransferasesMolecular biologyEnzyme assayGlutamineP1PK blood group system030104 developmental biologyAmino Acid SubstitutionBiochemistrychemistryGlycopshingolipidsbiology.proteinNOR polyagglutinationOriginal ArticleGlycoconjugate Journal
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Single nucleotide polymorphisms in A4GALT spur extra products of the human Gb3/CD77 synthase and underlie the P1PK blood group system.

2018

Contrary to the mainstream blood group systems, P1PK continues to puzzle and generate controversies over its molecular background. The P1PK system comprises three glycosphingolipid antigens: Pk, P1 and NOR, all synthesised by a glycosyltransferase called Gb3/CD77 synthase. The Pk antigen is present in most individuals, whereas P1 frequency is lesser and varies regionally, thus underlying two common phenotypes: P1, if the P1 antigen is present, and P2, when P1 is absent. Null and NOR phenotypes are extremely rare. To date, several single nucleotide polymorphisms (SNPs) have been proposed to predict the P1/P2 status, but it has not been clear how important they are in general and in relation …

0301 basic medicinePhysiologyCell Membraneslcsh:MedicineArtificial Gene Amplification and ExtensionBiochemistryPolymerase Chain Reactionchemistry.chemical_compoundSpectrum Analysis TechniquesTranscription (biology)GenotypeMedicine and Health Scienceslcsh:ScienceGeneticsMultidisciplinaryGlobosidesHomozygoteGlycosphingolipidFlow CytometryGalactosyltransferasesPhenotypeLipidsBody FluidsElectrophysiologyCholesterolBloodPhenotypeSpectrophotometryBlood Group AntigensCytophotometryAnatomyCellular Structures and OrganellesResearch ArticleGenotypeSingle-nucleotide polymorphismBiologyResearch and Analysis MethodsReal-Time Polymerase Chain ReactionMembrane PotentialPolymorphism Single NucleotideAntibodiesGlycosphingolipids03 medical and health sciencesAntigenGlycosyltransferaseHumansMolecular Biology TechniquesMolecular BiologyBlood typeSphingolipidslcsh:RBiology and Life SciencesCell Biology030104 developmental biologychemistrybiology.proteinlcsh:QBlood GroupsPLoS ONE
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Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus…

1992

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Bacterial ToxinsMolecular Sequence DataEnterotoxinMicrobiologyMicrobiologyStreptococcus mutanschemistry.chemical_compoundEnterotoxinsGlucosyltransferasesBacterial ProteinsGlycosyltransferaseConsensus SequenceConsensus sequenceAromatic amino acidsAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding SitesbiologySequence Homology Amino AcidClostridioides difficileCytotoxinsClostridium difficilechemistryBiochemistryGlucosyltransferasesbiology.proteinCarbohydrate MetabolismResearch ArticleJournal of bacteriology
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Effects of streptozotocin-induced diabetes, physical training and their combination on collagen biosynthesis in rat skeletal muscle.

1995

The effects of streptozotocin-induced diabetes, physical training and their combination on the activities of prolyl 4-hydroxylase (PH) and galactosylhydroxylysyl glucosyl-transferase (GGT), both marker enzymes of collagen biosynthesis, and on the concentration of hydroxyproline (Hyp) were studied in vastus lateralis, rectus femoris and gastrocnemius muscles in rats. The experimental period was 12-16 weeks. Diabetes had an overall decreasing effect on specific PH activity in all muscles studied, whereas specific GGT activity remained at control level. Total PH and GGT activities decreased in all three muscles in the diabetic animals (P < 0.001). Training caused an increase in PH and GGT acti…

Blood GlucoseMalemedicine.medical_specialtyPhysiologyProcollagen-Proline DioxygenasePhysical exerciseProcollagen glucosyltransferaseDiabetes Mellitus ExperimentalRats Sprague-DawleyHydroxyprolinechemistry.chemical_compoundInternal medicineDiabetes mellitusPhysical Conditioning AnimalGlycosyltransferasemedicineAnimalsInsulinMuscle Skeletalchemistry.chemical_classificationbiologyBody WeightSkeletal musclemedicine.diseaseStreptozotocinRatsHydroxyprolineEnzymemedicine.anatomical_structureEndocrinologychemistryGlucosyltransferasesbiology.proteinCollagenmedicine.drugActa physiologica Scandinavica
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Large clostridial cytotoxins — a family of glycosyltransferases modifying small GTP-binding proteins

1996

Some Clostridium species produce AB x -type protein cytotoxins of high molecular weight. These toxins constitute the group of large clostridial cytotoxins (LCTs), which have homologous protein sequences, exert glycosyltransferase activity and modify GTP-binding proteins of the Ras-superfamily. These characteristics render the LCTs valuable tools for developmental and cell biologists.

ClostridiumMicrobiology (medical)Clostridium speciesMicrobial toxinsCytotoxinsBacterial ToxinsCellGlycosyltransferasesProtein superfamilyBiologyGlycosyltransferase activityMicrobiologyInfectious DiseasesGTP-binding protein regulatorsmedicine.anatomical_structureBiochemistryVirologyGlycosyltransferaseras Proteinsbiology.proteinmedicineCytotoxicityTrends in Microbiology
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The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.

2008

Abstract Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, t…

DNA ComplementaryGlycosylationCell SurvivalLysyl hydroxylaseCellhydroxylysyl glycosylationFluorescent Antibody Techniquelysyl hydroxylaseMicrotubulesPermeabilityCell LineGlycosyltransferasemedicineExtracellularAnimalsHumanscell growthViability assayRNA Small InterferingCell Shapecell viabilityCell ProliferationbiologyCell DeathCell growthProcollagen-Lysine 2-Oxoglutarate 5-Dioxygenasecollagen biosynthesisGlycosyltransferasesCell BiologyArticlesGalactosyltransferasesMolecular biologyPeptide FragmentsCulture MediaActin Cytoskeletonmedicine.anatomical_structurepost-translational modificationCell culturebiology.proteinMolecular MedicineGlucosyltransferaseExtracellular Spacehydroxylysyl glycosyltransferaseJournal of cellular and molecular medicine
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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 &amp; Medicinal Chemistry
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