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Glycosyltransferase

Glycosyltransferases are a diverse group of enzymes that catalyze the transfer of glycosyl groups from activated donor molecules to acceptor molecules, resulting in the formation of glycosidic bonds.
These enzymes play crucial roles in the biosynthesis of complex carbohydrates, glycoproteins, and glycolipids, which are essential for a wide range of biological processes, including cell signaling, cell-cell interactions, and immune function.
Glycosyltransferases are involved in the synthesis of a variety of biologically important molecules, such as oligosaccharides, polysaccahrides, and glycoconjugates, and they are important targets for research and drug development in areas such as cancer, inflammation, and infectious diseases.
Thier study is crucial for understanding the fundamental mechanisms of glycosylation and for developing new therapeutic strategies.

Most cited protocols related to «Glycosyltransferase»

1
Comparative Genomics of Microbotryum Fungus
Cited 6 times
We compared M. lychnidis-dioicae to 18 other fungi (Additional file 13) that sample the three subphyla in Basidiomycota, including 5 other Pucciniomycotina, 7 Agaricomycotina, 3 Ustilaginomycotina, as well as 3 Ascomycota outgroups. For M. lychnidis-dioicae and the 18 other fungal genomes, we identified ortholog clusters using OrthoMCL [126 (link)] version 1.4 with a Markov inflation index of 1.5 and a maximum e-value of 1 × 10−5. Two genomes, R. glutinis and P. placenta, are missing more broadly conserved orthologs than the other genomes; examining the 961 Microbotryum gene clusters with an ortholog missing in just one other genome, the number of missing clusters in any one Basidiomycete genome ranged from 1 to 34 with the exception of R. glutinis and P. placenta, missing 410 and 393 of these highly conserved clusters, respectively. PFAM domains within each gene were identified using Hmmer3 [127 (link)], and gene ontology terms were assigned using BLAST2GO [128 (link)].
To examine gene duplication history, the phylome, or complete collection of phylogenetic trees for each gene in a genome, was reconstructed for Microbotryum lychnidis-dioicae and 19 other fungi, including those used for OrthoMCL (Additional file 13) and Serpula lacrymans. Phylomes were reconstructed using the previously described pipeline [129 (link)]. All trees and alignments have been deposited in PhylomeDB [129 (link)] and can be browsed on-line (www.phylomedb.org, phylome code 180). Trees were scanned to detect and date duplication events [130 ].
RNAi components from other other fungi were used as Blast queries to find homologs in M. lychnidis-dioicae; the queries used include U. hordei RdRp (CCF48827.1), C. neoformans Ago1 (XP_003194007), and N. crassa Dcl2 (Q75CC1.3) and Dcl1 (Q758J7.1). The putative function was confirmed by examining protein domains. The identified domains for each protein include: Piwi, PAZ and DUF1785 found in both copies of Argonaute (MVLG_06823, MVLG_06899); DEAD/DEAH helicase, double-stranded RNA binding, and RNAseIII (MVLG_01202). Sugar transporters were identified based on homology to the Ustillago maydis Srt1t transporter (Genbank: XP_758521) and the Uromyces viciae-fabae Hxt1 (Genbank: CAC41332).
The M. lychnidis-dioicae protein models corresponding to carbohydrate-active enzymes were assigned to families of glycoside hydrolases (GH), polysaccharide lyases (PL), carbohydrate esterases (CE), carbohydrate-binding modules (CBM), auxiliary activities (AA) and glycosyltransferases (GT) listed by the CAZy database [64 (link)], exactly as previously done for the analyses of dozens of fungal genomes [39 (link), 66 (link), 131 (link), 132 (link)].
Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J., Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E., Badouin H., Andrews J., Razeeq D., Gabaldón T., Quesneville H., Giraud T., Hood M.E., Schultz D.J, & Cuomo C.A. (2015). Sex and parasites: genomic and transcriptomic analysis of Microbotryum lychnidis-dioicae, the biotrophic and plant-castrating anther smut fungus. BMC Genomics, 16(1), 461.
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Publication 2015
Argonaute Proteins Ascomycetes Basidiomycota Carbohydrate Binding Modules Carbohydrates Cryptococcus neoformans DNA Helicases Enzymes Esterases Fungi Gene Duplication Genes Genome Genome, Fungal Glycoside Hydrolases Glycosyltransferase Membrane Transport Proteins Microbotryum lychnidis-dioicae M protein, multiple myeloma Placenta Polysaccharide-Lyases Protein Domain Rhodotorula glutinis RNA, Double-Stranded RNA Interference Serpula lacrymans Trees Uromyces viciae-fabae
2
Optimized Dual-Luciferase Reporter System
Cited 6 times
All constructs were based on the vector pUC18 supplemented by several restriction sites (EcoRV, NaeI, NotI, NheI, BglII, XhoI, NcoI and SpeI). For this purpose, the vector pUC18 was cut inside the multiple cloning site (SalI and HindIII) and a double-stranded oligonucleotide containing the additional restriction sites was inserted.
The sequence of the firefly luciferase and the CaMV 35S terminator from plasmid pGN35S-luc+ (kindly provided by Prof. Gunther Neuhaus, Freiburg University) was introduced into the modified pUC18 vector via NcoI (providing the ATG luciferase start codon) and PstI.
A synthetic polyadenylation (polyA) signal for background reduction was inserted into the EcoRI site upstream of the additionally introduced restriction sites. The signal was PCR-amplified from the plasmid pGL3-basic (Promega, Mannheim, Germany) (primers: polyA-a and polyA-b; all oligonucleotides used as primers are shown in Tab. 1, see Additional file 3) and subcloned into the vector pCR®4-TOPO® (Invitrogen, Karlsruhe, Germany) out of which it was cut with EcoRI for further cloning. This yielded the firefly luciferase construct pluc into which the transcriptional and translational enhancer elements were introduced afterwards (Fig. 1A).
The TMV (tobacco mosaic virus) omega translation enhancer [49 (link)] was cut out of pGN35S-luc+ and inserted into the basic vector pluc using the restriction sites XhoI and NcoI to yield pluc-Ω (Fig. 1A). With the aim of changing the sequence precisely in front of the translation initiation codon ATG, in accordance to Kozak [33 (link)] and Luetcke et al. [34 (link)], the five nucleotides CTCAA were inserted between the restriction sites XhoI and NcoI (NcoI including the translation initiation codon) of pluc to give pluc-enh (Fig. 1A).
All of the promoter sequences were PCR-amplified and the amplification products subcloned into the vector pCR®4-TOPO® (Invitrogen, Karlsruhe, Germany). Fragments of the heterologous promoters, except CaMV 35S(long), were excised with SalI and XhoI and subsequently inserted between the SalI and XhoI sites of the three basic vectors pluc, pluc-Ω and pluc-enh, respectively. The CaMV 35S(long) promoter was inserted into the basic vectors using the restriction sites EcoRI and XhoI. The 5'-sequences of the Physcomitrella glycosyltransferases fuc-t and xyl-t were introduced into pluc using the restriction sites SalI and NcoI. To avoid background activity resulting from the vector backbone, all firefly luciferase promoter plasmids were linearized using restriction enzyme EcoRI, which cuts 33 bp upstream the start of the corresponding promoter sequence, at the 5'-end of the multiple cloning site.
The sequence of the CaMV 35S(1x) promoter was amplified by PCR from the vector pRT101 [50 (link)] using the primers 35S(1x)-a and 35S(1x)-b. For the amplification of CaMV 35S(long) promoter sequence, the vector mAV4 [51 (link)] was used as a PCR-template with the primers 35S(long)-a and 35S(long)-b. PGN35S-luc+ employed for amplification of the CaMV 35S(2x) promoter sequence using the primers 35S(2x)-a and 35S(2x)-b. For the construction of plasmids carrying the rice Act1 promoter [43 (link)], the Act1 5'region was PCR-amplified from the vector pDM302 [[52 ], kindly provided by Pof. Ray Wu, Cornell University Ithaca, New York], using the primers Act1-a and Act1-b. PEGFP-N1 (BD Biosciences Clontech, Heidelberg, Germany) served as template for the amplification of the human cytomegalo virus (CMV) promoter with the primers CMV-a and CMV-b. The nos promoter sequence was PCR-amplified with the primers nos-a and nos-b using plasmid pBSNNN [8 (link)] as a template. Amplification of the simian virus (SV) 40 promoter sequence from the vector pSG5 (Stratagene, Amsterdam, The Netherlands) was carried out with the primers SV40-a and SV40-b.
The 5'-sequences of the Physcomitrella glycosyltransferases identified by inverse PCR were amplified using the primers FT-P-a and FT-P-b in the case of the fucosyltransferase promoter and XT-P-a and XT-P-b for the xylosyltransferase promoter, respectively. The promoter region of deletion construct plucFTP-Δ1 was amplified with the primers FTP-Δ1 and FT-P-b. PlucFTP-Δ1 served as a template for the amplification of the promoter sequences of plucFTP-Δ2, plucFTP-Δ3 and plucFTP-Δ4 with the forward primers FTP-Δ2, FTP-Δ3 or FTP-Δ4, respectively, and the reverse primer FT-P-b. The promoter regions of the xylosyltransferase deletion constructs were amplified with the forward primers XTP-Δ1, XTP-Δ2, XTP-Δ3 or XTP-Δ4, respectively, and XT-P-b as reverse primer, using plucXTP as template. The resulting amplification products were inserted into pluc using restriction sites SalI and XhoI.
Taken together, the XT fusion contains the sequence upstream of position -1 relative to the translation start codon. For cloning reasons the G at position -1 was replaced by the nucleotides CC followed by the luciferase coding sequence. The FT fusion contains the 5'-untranslated sequence upstream of position -2. The nucleotides A and T at positions -2 and -1 were replaced by CC followed by the luciferase coding sequence.
For the creation of the Renilla luciferase control plasmid (pRluc) the firefly luciferase sequence was exchanged with the Renilla luciferase sequence in the vector pluc-35S(long), using XhoI and XbaI (Fig. 1B). The sequence of the luciferase control reporter gene was amplified from the plasmid pRL-CMV (Promega), using the primers Rluc-a and Rluc-b.
Horstmann V., Huether C.M., Jost W., Reski R, & Decker E.L. (2004). Quantitative promoter analysis in Physcomitrella patens: a set of plant vectors activating gene expression within three orders of magnitude. BMC Biotechnology, 4, 13.
Publication 2004
Cloning Vectors Codon, Initiator Deletion Mutation Deoxyribonuclease EcoRI Enhancer Elements, Genetic Fucosyltransferase Genes, Reporter Glycosyltransferase Herpesvirus 1, Cercopithecine Homo sapiens Inverse PCR Luciferases Luciferases, Firefly Luciferases, Renilla Nucleotides Oligonucleotide Primers Oligonucleotides Open Reading Frames Paragangliomas 3 Physcomitrella Plasmids Polyadenylation Promega Rice Simian virus 40 Tobacco Mosaic Virus Topotecan Transcription, Genetic Vertebral Column Virus xylosyltransferase
3
Recombinant Expression and Characterization of UDP-Glycosyltransferases
Cited 5 times
The full cDNA of UGTs from Nipponbare (O. sativa L. spp. japonica) were cloned into the pGEX-6p-1 expression vector (Novagen) with a glutathione S-transferase tag. Recombinant proteins were expressed in BL21 (DE3) cells (Novagen) following induction by addition of 0.1 mM isopropy-β-D-thiogalactoside (IPTG) and growing continually for 16 h at 20 °C. Cells were collected and pellets were resuspended in lysis buffer (50 mM Tris-HCl, pH 8.0, 400 mM NaCl). The cells were disrupted by the high pressure cracker and cell debris was removed by centrifugation (14000 g, 1 h). Glutathione Sepharose 4B agarose (GE Healthcare) was added to the supernatant containing the target proteins. After incubation for 1 h, the mixture was transferred into a disposable column and washed extensively with lysis buffer (5 column volumes). Target proteins in collections were confirmed by SDS-PAGE and purified recombinant proteins were selected for enzyme assays and kinetics determination.
The enzyme reactions in vitro assay for glycosyltransferases were performed in a total volume of 100 μl containing 200 μM flavonoid substrates, 1.5 mM UDP-glucose, 5 mM MgCl2 and totally 500 ng purified protein in Tris-HCl buffer (100 mM, pH 7.4) was incubated at 37 °C. After incubating for 20 min, the reaction was stopped by adding 300 μl of ice-cold methanol. The reaction mixture was then filtered through a 0.2 μm filter (Millipore) before being used for LC-MS analysis. HPLC conditions for the analysis of flavonoids were as follows: column, shim-pack VP-ODS (150 L × 4.6); flow rate, 0.8 mL min−1; solvent A, 0.04% (by volume) acetic acid in water; solvent B, 0.04% acetic acid in acetonitrile. After injection (40 μL) into a column that had been equilibrated with 5% solvent B (by volume), the column was initially developed isocratically with 5% solvent B, followed by a linear gradient from 5 to 95% solvent B for 20 min. The column was then washed isocratically with 95% solvent B for 2 min, followed by a linear gradient from 95 to 5% solvent B for 0.1 min. The column was isocratically with 5% solvent B for 5 min. The chromatograms were obtained with detection at 330 nm. Peak identification of each component was confirmed using authentic samples and post-run by LC-MS/MS analysis. The amounts of flavonoids were determined from peak integration using authentic samples for calibration.
Peng M., Shahzad R., Gul A., Subthain H., Shen S., Lei L., Zheng Z., Zhou J., Lu D., Wang S., Nishawy E., Liu X., Tohge T., Fernie A.R, & Luo J. (2017). Differentially evolved glucosyltransferases determine natural variation of rice flavone accumulation and UV-tolerance. Nature Communications, 8, 1975.
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Publication 2017
Acetic Acid acetonitrile Buffers Cells Centrifugation Cloning Vectors Cold Temperature DNA, Complementary Enzyme Assays Flavonoids Glutathione Glutathione S-Transferase Glycosyltransferase High-Performance Liquid Chromatographies Kinetics Magnesium Chloride Methanol Pellets, Drug Pressure Proteins Protein Targeting, Cellular Recombinant Proteins SDS-PAGE Sepharose Sepharose 4B SHIMS Sodium Chloride Solvents Tandem Mass Spectrometry Tromethamine Uridine Diphosphate Glucose
4
Comprehensive Genomic Profiling of Streptococcus
Cited 5 times
Bioinformatics methods are described and updated at https://github.com/BenJamesMetcalf. emm subtypes were obtained on the basis of a database of defined 180-bp sequences maintained at the CDC (ftp://ftp.cdc.gov/pub/infectious_diseases/biotech/tsemm/). This subtyping scheme is based on a sequence that consists of 10 codons corresponding to the C-terminal end of the M protein signal sequence and 50 codons corresponding to the N terminus of the mature M protein (46 (link)). The WGS emm typing scheme employs de novo assembly and queries sequences closely linked to 21-bp emm typing primer 1 (27 (link)) situated adjacent to the emm type-specific region.
A PBP2x transpeptidase amino acid sequence type was generated for each isolate as described for GBS PBP2x for detection of first-step mutations leading to β-lactam resistance (17 (link)). Additionally, the ARG-ANNOT and ResFinder databases were incorporated (23 (link), 24 (link)). Sequence targets for detection of the presence/absence of 21 T antigen backbone (tee) genes (29 (link)), the gacI glycosyl transferase specific for the group A antigen (28 (link)), the hyaluronic acid synthetic locus hasA (47 (link)), emm-like genes that flank emm (9 (link)), four different fibronectin-binding domain repeat proteins (48 (link)), the R28 surface antigen (30 (link)), the sda1-encoded DNase (49 (link)), sequence polymorphisms associated with the ngo operon (4 (link), 5 (link)), two conserved rocA null mutations (50 (link), 51 (link)), 12 exotoxin genes (speA to speC, speG to speM, ssa, smeZ) (52 (link)), and the streptococcal inhibitor of complement (31 (link), 32 (link)) were obtained through the references indicated.
Chochua S., Metcalf B.J., Li Z., Rivers J., Mathis S., Jackson D., Gertz RE J.r., Srinivasan V., Lynfield R., Van Beneden C., McGee L, & Beall B. (2017). Population and Whole Genome Sequence Based Characterization of Invasive Group A Streptococci Recovered in the United States during 2015. mBio, 8(5), e01422-17.
Publication 2017
Amino Acid Sequence Arterial calcification of infancy Base Sequence Binding Proteins Codon Communicable Diseases Complement Inactivating Agents Deoxyribonuclease I Exotoxins Fibronectins Gene Products, gag Genes Genetic Polymorphism Glycosyltransferase Hyaluronic acid Lactams M protein, multiple myeloma Mutation Null Mutation Oculocutaneous Albinism, Type III Oligonucleotide Primers Operon Peptidyltransferase Pursuit, Smooth Signal Peptides SpeA protein, Streptococcus pyogenes Speg beta protein, human Streptococcus Surface Antigens Vertebral Column Viral Tumor Antigens
5
Enzymatic Modulation of Antibody Glycosylation
Cited 5 times
Where indicated, galactose substrate, D-galactose (Sigma, G0750-5G), was added to the medium before transfection. The decoy substrates for fucosylation, 2-deoxy-2-fluoro-l-fucose (2FF) (Carbosynth, MD06089) and galactosylation 2-deoxy-2-fluoro-D-galactose (2FG) (Carbosynth, MD04718) were added 4 hours post transfection. All carbohydrates were diluted in distilled sterile water and filtered using a 0.2 nm puradisc syringe filter (Whatmann, GE Healthcare, 10462200). Percentages of co-transfection of enzyme (glycosyltransferase or RMD) vectors ware calculated relative to total DNA, keeping the amount of antibody-encoding vector constant, and adding an empty expression vector to keep the amount of total DNA constant. In vitro sialylation was performed with recombinant human α-2,6-sialyltransferase (Roche, 07012250103) and cytidine-5′-monophospho-N-acetylneuraminic acid (CMP-NANA) (Roche, 05974003103).
Antibody, enzyme and substrate were mixed in a 20:1:10 w/w ratio in PBS at pH 7.4, incubated for 12 hours at 37 °C, subsequently additional CMP-NANA was added to the mixture to a final ratio of 20:1:20 for antibody, enzyme and substrate respectively and further incubated for 12 hours at 37 °C. After in vitro sialylation to remove the excess enzyme and CMP-NANA, the antibodies were re-purified on a protein A (WT IgG1) HiTrap HP column (GE Life Sciences) as described below.
Dekkers G., Plomp R., Koeleman C.A., Visser R., von Horsten H.H., Sandig V., Rispens T., Wuhrer M, & Vidarsson G. (2016). Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans. Scientific Reports, 6, 36964.
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Publication 2016
2-deoxy-2-fluoro-L-fucose Antibodies Carbohydrates Cloning Vectors cytidine-5'-monophosphosialic acid Cytidine Monophosphate N-Acetylneuraminic Acid Enzymes Galactose Glycosyltransferase Homo sapiens IgG1 Immunoglobulins oxytocin, 1-desamino-(O-Et-Tyr)(2)- Sialyltransferases Staphylococcal Protein A Sterility, Reproductive Syringes Transfection

Most recents protocols related to «Glycosyltransferase»

1
Rapid Screening Strain for RebA to RebD Conversion
Not available on PMC !

Example 3

To make a screening strain to rapidly screen for RebA to RebD conversion in vivo, a landing pad was inserted into the RebA strain described above. The landing pad consisted of 500 bp of locus-targeting DNA sequences on either end of the construct to the genomic region downstream of the ALG1 open reading frame (FIG. 4). Internally, the landing pad contained a PGAL1 promoter and a yeast terminator flanking an endonuclease recognition site (F-CphI).

US11866738B2. UDP-dependent glycosyltransferase for high efficiency production of rebaudiosides (2024-01-09). AMYRIS, INC. [US]. Inventors: Lishan Zhao [US], Wenzong Li [US], Gale Wichmann [US], Aditi Khankhoje [US], Chantal Garcia De Gonzalo [US], Tina Mahatdejkul-Meadows [US], Shaina Jackson [US], Michael Leavell [US], Darren Platt [US].
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Patent 2024
DNA Sequence Endonuclease Enzymes Genome Glycosyltransferase Saccharomyces cerevisiae Strains
2
Screening Protein Interactions in E. coli
Plasmids encoding fusions of glycosyltransferases and proteins involved in the transport and polymerization of EPS (PssT, PssP, PssL, and PssP2) were previously constructed [26 (link),76 (link),78 (link)] and are listed in Supplementary Table S8. Plasmids were co-transformed into E. coli DHM1 strain and interaction screening was performed using agar plates containing 40 μg/mL 5-bromo-4-chloro-3-indolyl-β-D-galactoside (X-Gal, A&A Biotechnology, Gdańsk, Poland), 0.5 mM IPTG (A&A Biotechnology, Gdańsk, Poland), ampicillin, and kanamycin. Quantitative measurement of β-galactosidase activity was performed in a plate format as described earlier [26 (link)].
Żebracki K., Horbowicz A., Marczak M., Turska-Szewczuk A., Koper P., Wójcik K., Romańczuk M., Wójcik M, & Mazur A. (2023). Exopolysaccharide Biosynthesis in Rhizobium leguminosarum bv. trifolii Requires a Complementary Function of Two Homologous Glycosyltransferases PssG and PssI. International Journal of Molecular Sciences, 24(4), 4248.
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Publication 2023
5-bromo-4-chloro-3-indolyl beta-galactoside Agar Ampicillin Escherichia coli Galactosides GLB1 protein, human Glycosyltransferase Isopropyl Thiogalactoside Kanamycin Plasmids Polymerization Proteins Strains
3
Glycosyltransferase Kinetics for Flavonoids
The kinetic constants of glycosyltransferase were determined for flavonoid and tomatidine compounds. The activity was determined with 0–200 μM quercetin and tomatine, and a fixed concentration of 15 mM UDP-galactose was used as the glycosyl donor [42 (link)].
Zhao X., Zhang Y., Lai J., Deng Y., Hao Y., Wang S, & Yang J. (2023). The SlDOG1 Affect Biosynthesis of Steroidal Glycoalkaloids by Regulating GAME Expression in Tomato. International Journal of Molecular Sciences, 24(4), 3360.
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Publication 2023
Flavonoids Glycosyltransferase Kinetics Quercetin Tissue Donors tomatidine Tomatine Uridine Diphosphate Galactose
4
UDP-Glo Assay for Glycosyltransferase Activity
The UDP-Glo assay quantifies the amount of UDP product formed from a glycosyltransferase reaction. The principle of the assay is to convert UDP to ATP to generate light in a luciferase reaction. A white 96-well microplate (Ref. 655074, Greiner Bio-One) containing the nucleotide detection reagent was used to stop the glycosyltransferase reaction and initiate luminescence. Luminescence was read using the Spark microplate reader (TECAN). The enzymatic rate was determined using a UDP standard curve, and activity was expressed, depending on the data analysis, as relative light units (RLU), as specific enzyme activity (nmol/min/mg protein) or as a reaction rate (μM/min). Assays were carried out in triplicates. Control reactions were performed in the absence of an acceptor.
Enzyme activity with LacCer acceptor was performed as follows. We used a LacCer variant with a short C8 acyl chain, which is more soluble than naturally occurring LacCer [29 (link)]. The required amount of C8 LacCer in chloroform:methanol (2:1) was added to a glass tube and dried under nitrogen for 20 min. The lipid was resolubilized in 30 µL of reaction buffer (see below). The LacCer solution was sonicated at 35 kHz in an iced water bath sonicator (Bioblock Scientific) to form micelles for 10 min. LgtC was added to the reaction, and the addition of UDP-Gal initiated the enzyme reaction. The enzymatic reaction (30 µL final volume) contained 20 mM HEPES, 1 mM MnCl2, 1 mM DTT, 250 μM UDP-Gal, varying lactosylceramide concentrations and 10 ng/μL (0.29 μM) LgtC at pH 7.5. The enzyme reaction proceeded for 10 min or longer where appropriate. 25 μL of the reaction was mixed with 25 μL nucleotide detection reagent. The plate was covered with foil, shaken for 30 s and incubated for 1 h at room temperature before measuring the luminescence. Enzyme activity with the acceptor lactose was performed in the same buffer conditions in a final volume of 100 µL. At the end of the reaction, 25 μL was transferred into a 96-well plate and mixed with 25 μL nucleotide detection reagent, as described above. All enzyme reactions were performed in triplicates at room temperature.
Jabeguero D., Siukstaite L., Wang C., Mitrovic A., Pérez S., Makshakova O., Richter R.P., Römer W, & Breton C. (2023). Enzymatic Glyco-Modification of Synthetic Membrane Systems. Biomolecules, 13(2), 335.
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Publication 2023
Bath Biological Assay Buffers CDw17 antigen Chloroform enzyme activity Enzymes Glycosyltransferase HEPES Lactose lactosyl-beta1-1-N-octanoylsphingosine Light Lipids Luciferases Luminescence manganese chloride Methanol Micelles Nitrogen Nucleotides Proteins
5
Reconstitution of Lipid Membranes with Glycolipids
C8 lactosyl(β)-ceramide (LacCer), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and cholesterol were obtained from Avanti Polar Lipids (Alabaster, AL, USA). Atto 647N 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) was purchased from Sigma-Aldrich (Darmstadt, Germany). Globotriaosylceramide (Gb3) was obtained from Matreya (State College, PA, USA). Shiga toxin B-subunit (StxB) was kindly provided by enGenes Biotech (Vienna, Austria). UDP-Glo Glycosyltransferase assay kit and ultra-pure UDP-Galactose (UDP-Gal) were from Promega (Charbonnières-les-Bain, France). UDP-Gal for QCM-D analysis was purchased from Carbosynth (Compton, UK). HisTrap FF column was purchased from Cytiva (Marlborough, MA, USA) and Superdex 200 Increase 10/300 GL from GE Healthcare (Chicago, MA, USA). All other chemical reagents were of analytical or liquid chromatography grade.
Jabeguero D., Siukstaite L., Wang C., Mitrovic A., Pérez S., Makshakova O., Richter R.P., Römer W, & Breton C. (2023). Enzymatic Glyco-Modification of Synthetic Membrane Systems. Biomolecules, 13(2), 335.
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Publication 2023
1,2-oleoylphosphatidylcholine Alabaster Biological Assay Ceramides Cholesterol dioleoyl cephalin globotriaosylceramide Glycerylphosphorylcholine Glycosyltransferase Lipids Liquid Chromatography Promega Protein Subunits Shiga Toxin Uridine Diphosphate Galactose

Top products related to «Glycosyltransferase»

1
Udp glo glycosyltransferase assay by Promega
Sourced in United States
The UDP-Glo™ Glycosyltransferase Assay is a luminescence-based kit designed to measure the activity of glycosyltransferase enzymes. The assay quantifies the production of UDP, a byproduct of the glycosyltransferase-catalyzed reaction, using a coupled enzymatic detection system.
2
Glycosyltransferase activity kit by R&D Systems
Sourced in United States
The Glycosyltransferase Activity Kit is a laboratory tool designed to measure the enzymatic activity of glycosyltransferases, a class of enzymes responsible for the transfer of sugar moieties to various substrates. The kit provides the necessary reagents and protocols to quantify the activity of these enzymes, which play crucial roles in numerous biological processes.
3
Udp glo glycosyltransferase assay kit by Promega
Sourced in France, United States
The UDP-Glo Glycosyltransferase Assay kit is a luminescent-based assay that measures the activity of glycosyltransferase enzymes. The kit detects the production of UDP, a byproduct of the glycosyltransferase reaction, and provides a quantitative measurement of enzyme activity.
4
Udp glucose by Merck Group
Sourced in United States
UDP-glucose is a nucleotide sugar that serves as a substrate for various glycosyltransferase enzymes involved in the biosynthesis of carbohydrates and glycosylated molecules. It is an important intermediate in cellular metabolism and plays a crucial role in various biological processes.
5
Qiaamp dna mini kit by Qiagen
Sourced in Germany, United States, France, United Kingdom, Netherlands, Spain, Japan, China, Italy, Canada, Switzerland, Australia, Sweden, India, Belgium, Brazil, Denmark
The QIAamp DNA Mini Kit is a laboratory equipment product designed for the purification of genomic DNA from a variety of sample types. It utilizes a silica-membrane-based technology to efficiently capture and purify DNA, which can then be used for various downstream applications.
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Rneasy mini kit by Qiagen
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
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Synergy h1 microplate reader by Agilent Technologies
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The Synergy H1 microplate reader is a versatile instrument designed for a wide range of absorbance, fluorescence, and luminescence-based assays. It features a Take3 Micro-Volume Plate for precise measurements of small sample volumes, and a Quad4 Monochromator for flexible wavelength selection.
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High capacity cdna reverse transcription kit by Thermo Fisher Scientific
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The High-Capacity cDNA Reverse Transcription Kit is a laboratory tool used to convert RNA into complementary DNA (cDNA) molecules. It provides a reliable and efficient method for performing reverse transcription, a fundamental step in various molecular biology applications.
9
Udp glcnac by Merck Group
Sourced in United States
UDP-GlcNAc is a chemical compound that serves as a substrate for various enzymatic reactions involved in the biosynthesis of glycoproteins, glycolipids, and other glycosylated molecules. It is a key intermediate in the hexosamine biosynthetic pathway and plays a crucial role in cellular processes such as protein glycosylation and signaling.
10
Gdp azido fucose by R&D Systems
Sourced in United States
GDP-azido-fucose is a chemical compound used as a biochemical research tool. It is a synthetic derivative of the monosaccharide fucose, containing an azido group. This compound can be utilized in various biochemical applications, such as the study of protein-carbohydrate interactions and the labeling of glycoconjugates.

More about "Glycosyltransferase"

Glycosyltransferases are a diverse group of enzymes that play a crucial role in the biosynthesis of complex carbohydrates, glycoproteins, and glycolipids.
These enzymes catalyze the transfer of glycosyl groups from activated donor molecules, such as UDP-glucose, UDP-GlcNAc, and GDP-azido-fucose, to acceptor molecules, resulting in the formation of glycosidic bonds.
This process is essential for a wide range of biological processes, including cell signaling, cell-cell interactions, and immune function.
Glycosyltransferases are involved in the synthesis of a variety of biologically important molecules, such as oligosaccharides, polysaccharides, and glycoconjugates.
They are important targets for research and drug development in areas such as cancer, inflammation, and infectious diseases.
The study of glycosyltransferases is crucial for understanding the fundamental mechanisms of glycosylation and for developing new therapeutic strategies.
The UDP-Glo™ Glycosyltransferase Assay and the Glycosyltransferase Activity Kit are commonly used tools for measuring the activity of glycosyltransferases.
These assays utilize the UDP-Glo™ technology to detect the production of UDP, a byproduct of the glycosyltransferase reaction.
The Synergy H1 microplate reader can be used to measure the luminescent signal generated by these assays.
Additionally, the QIAamp DNA Mini Kit and the RNeasy Mini Kit can be used to extract and purify DNA and RNA, respectively, which may be necessary for studying the expression and regulation of glycosyltransferase genes.
The High-Capacity cDNA Reverse Transcription Kit can then be used to synthesize cDNA from the extracted RNA, enabling further analysis of glycosyltransferase gene expression.
In summary, glycosyltransferases are a diverse group of enzymes that play a crucial role in the biosynthesis of complex carbohydrates, glycoproteins, and glycolipids, and are important targets for research and drug development.
The tools and techniques mentioned, such as the UDP-Glo™ Glycosyltransferase Assay, Glycosyltransferase Activity Kit, and related products, can be utilized to study and understand the function and regulation of these enzymes.