Relevant bibliographies by topics / Glycosyltransferase (GT61)

Academic literature on the topic 'Glycosyltransferase (GT61)'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Glycosyltransferase (GT61).'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Glycosyltransferase (GT61)"

1

Wu, Ren, Meixian Zhou, and Hui Wu. "Purification and Characterization of an Active N-Acetylglucosaminyltransferase Enzyme Complex from Streptococci." Applied and Environmental Microbiology 76, no. 24 (October 22, 2010): 7966–71. http://dx.doi.org/10.1128/aem.01434-10.

Full text
Abstract:
ABSTRACT A new family of bacterial serine-rich repeat glycoproteins can function as adhesins required for biofilm formation and pathogenesis in streptococci and staphylococci. Biogenesis of these proteins depends on a gene cluster coding for glycosyltransferases and accessory secretion proteins. Previous studies show that Fap1, a member of this family from Streptococcus parasanguinis, can be glycosylated by a protein glycosylation complex in a recombinant heterogeneous host. Here we report a tandem affinity purification (TAP) approach used to isolate and study protein complexes from native streptococci. This method demonstrated that a putative glycosyltransferase (Gtf2), which is essential for Fap1 glycosylation, readily copurified with another glycosyltransferase (Gtf1) from native S. parasanguinis. This result and the similar isolation of a homologous two-protein complex from Streptococcus pneumoniae indicate the biological relevance of the complexes to the glycosylation in streptococci. Furthermore, novel N-acetylglucosaminyltransferase activity was discovered for the complexes. Optimal activity required heterodimer formation and appears to represent a novel type of glycosylation.
APA, Harvard, Vancouver, ISO, and other styles
2

Duncan, Samuel M., and Michael A. J. Ferguson. "Common and unique features of glycosylation and glycosyltransferases in African trypanosomes." Biochemical Journal 479, no. 17 (September 6, 2022): 1743–58. http://dx.doi.org/10.1042/bcj20210778.

Full text
Abstract:
Eukaryotic protein glycosylation is mediated by glycosyl- and oligosaccharyl-transferases. Here, we describe how African trypanosomes exhibit both evolutionary conservation and significant divergence compared with other eukaryotes in how they synthesise their glycoproteins. The kinetoplastid parasites have conserved components of the dolichol-cycle and oligosaccharyltransferases (OSTs) of protein N-glycosylation, and of glycosylphosphatidylinositol (GPI) anchor biosynthesis and transfer to protein. However, some components are missing, and they process and decorate their N-glycans and GPI anchors in unique ways. To do so, they appear to have evolved a distinct and functionally flexible glycosyltransferases (GT) family, the GT67 family, from an ancestral eukaryotic β3GT gene. The expansion and/or loss of GT67 genes appears to be dependent on parasite biology. Some appear to correlate with the obligate passage of parasites through an insect vector, suggesting they were acquired through GT67 gene expansion to assist insect vector (tsetse fly) colonisation. Others appear to have been lost in species that subsequently adopted contaminative transmission. We also highlight the recent discovery of a novel and essential GT11 family of kinetoplastid parasite fucosyltransferases that are uniquely localised to the mitochondria of Trypanosoma brucei and Leishmania major. The origins of these kinetoplastid FUT1 genes, and additional putative mitochondrial GT genes, are discussed.
APA, Harvard, Vancouver, ISO, and other styles
3

Bu, Su, Yirong Li, Meixian Zhou, Parastoo Azadin, Meiqin Zeng, Paula Fives-Taylor, and Hui Wu. "Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin." Journal of Bacteriology 190, no. 4 (December 14, 2007): 1256–66. http://dx.doi.org/10.1128/jb.01078-07.

Full text
Abstract:
ABSTRACT Fap1, a serine-rich glycoprotein, is essential for fimbrial biogenesis and biofilm formation of Streptococcus parasanguinis (formerly S. parasanguis). Fap1-like proteins are conserved in many streptococci and staphylococci and have been implicated in bacterial virulence. Fap1 contains two serine-rich repeat regions that are modified by O-linked glycosylation. A seven-gene cluster has been identified, and this cluster is implicated in Fap1 biogenesis. In this study, we investigated the initial step of Fap1 glycosylation by using a recombinant Fap1 as a model. This recombinant molecule has the same monosaccharide composition profile as the native Fap1 protein. Glycosyl linkage analyses indicated that N-acetylglucosamine (GlcNAc) is among the first group of sugar residues transferred to the Fap1 peptide. Two putative glycosyltransferases, Gtf1 and Gtf2, were essential for the glycosylation of Fap1 with GlcNAc-containing oligosaccharide(s) in both S. parasanguinis as well as in the Fap1 glycosylation system in Escherichia coli. Yeast two-hybrid analysis as well as in vitro and in vivo glutathione S-transferase pull-down assays demonstrated the two putative glycosyltransferases interacted with each other. The interaction domain was mapped to an N-terminal region of Gtf1 that was required for the Fap1 glycosylation. The data in this study suggested that the formation of the Gtf1 and Gtf2 complex was required for the initiation of the Fap1 glycosylation and that the N-terminal region of Gtf1 was necessary.
APA, Harvard, Vancouver, ISO, and other styles
4

Mendoza, Fernanda, and Gonzalo A. Jaña. "The inverting mechanism of the metal ion-independent LanGT2: the first step to understand the glycosylation of natural product antibiotic precursors through QM/MM simulations." Organic & Biomolecular Chemistry 19, no. 26 (2021): 5888–98. http://dx.doi.org/10.1039/d1ob00544h.

Full text
Abstract:
Glycosyltransferases (GTs) from the GT1 family are responsible for the glycosylation of various important organic structures such as terpenes, steroids and peptide antibiotics, making it one of the most intensely studied families of GTs.
APA, Harvard, Vancouver, ISO, and other styles
5

Evanovich, Eliane, Patricia Jeanne de Souza Mendonça-Mattos, and Maria Lúcia Harada. "Molecular Evolution of the Glycosyltransferase 6 Gene Family in Primates." Biochemistry Research International 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/9051727.

Full text
Abstract:
Glycosyltransferase 6 gene family includes ABO, Ggta1, iGb3S, and GBGT1 genes and by three putative genes restricted to mammals, GT6m6, GTm6, and GT6m7, only the latter is found in primates. GT6 genes may encode functional and nonfunctional proteins. Ggta1 and GBGT1 genes, for instance, are pseudogenes in catarrhine primates, while iGb3S gene is only inactive in human, bonobo, and chimpanzee. Even inactivated, these genes tend to be conversed in primates. As some of the GT6 genes are related to the susceptibility or resistance to parasites, we investigated (i) the selective pressure on the GT6 paralogs genes in primates; (ii) the basis of the conservation of iGb3S in human, chimpanzee, and bonobo; and (iii) the functional potential of the GBGT1 and GT6m7 in catarrhines. We observed that the purifying selection is prevalent and these genes have a low diversity, though ABO and Ggta1 genes have some sites under positive selection. GT6m7, a putative gene associated with aggressive periodontitis, may have regulatory function, but experimental studies are needed to assess its function. The evolutionary conservation of iGb3S in humans, chimpanzee, and bonobo seems to be the result of proximity to genes with important biological functions.
APA, Harvard, Vancouver, ISO, and other styles
6

Terrak, Mohammed, and Martine Nguyen-Distèche. "Kinetic Characterization of the Monofunctional Glycosyltransferase from Staphylococcus aureus." Journal of Bacteriology 188, no. 7 (April 1, 2006): 2528–32. http://dx.doi.org/10.1128/jb.188.7.2528-2532.2006.

Full text
Abstract:
ABSTRACT The glycosyltransferase (GT) module of class A penicillin-binding proteins (PBPs) and monofunctional GTs (MGTs) belong to the GT51 family in the sequence-based classification of GTs. They both possess five conserved motifs and use lipid II precursor (undecaprenyl-pyrophosphate-N-acetylglucosaminyl-N-acetylmuramoyl- pentapeptide) to synthesize the glycan chain of the bacterial wall peptidoglycan. MGTs appear to be dispensable for growth of some bacteria in vitro. However, new evidence shows that they may be essential for the infection process and development of pathogenic bacteria in their hosts. Only a small number of class A PBPs have been characterized so far, and no kinetic data are available on MGTs. In this study, we present the principal enzymatic properties of the Staphylococcus aureus MGT. The enzyme catalyzes glycan chain polymerization with an efficiency of ∼5,800 M−1 s−1 and has a pH optimum of 7.5, and its activity requires metal ions with a maximum observed in the presence of Mn2+. The properties of S. aureus MGT are distinct from those of S. aureus PBP2 and Escherichia coli MGT, but they are similar to those of E. coli PBP1b. We examined the role of the conserved Glu100 of S. aureus MGT (equivalent to the proposed catalytic Glu233 of E. coli PBP1b) by site-directed mutagenesis. The Glu100Gln mutation results in a drastic loss of GT activity. This shows that Glu100 is also critical for catalysis in S. aureus MGT and confirms that the conserved glutamate of the first motif EDXXFXX(H/N)X(G/A) is likely the key catalytic residue in the GT51 active site.
APA, Harvard, Vancouver, ISO, and other styles
7

Chang, Te-Sheng, Jiumn-Yih Wu, Tzi-Yuan Wang, Kun-Yuan Wu, and Chien-Min Chiang. "Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A." International Journal of Molecular Sciences 19, no. 11 (November 5, 2018): 3469. http://dx.doi.org/10.3390/ijms19113469.

Full text
Abstract:
Bacillus subtilis ATCC (American type culture collection) 6633 was found to biotransform ganoderic acid A (GAA), which is a major lanostane triterpenoid from the medicinal fungus Ganoderma lucidum. Five glycosyltransferase family 1 (GT1) genes of this bacterium, including two uridine diphosphate-dependent glycosyltransferase (UGT) genes, BsUGT398 and BsUGT489, were cloned and overexpressed in Escherichia coli. Ultra-performance liquid chromatography confirmed the two purified UGT proteins biotransform ganoderic acid A into a metabolite, while the other three purified GT1 proteins cannot biotransform GAA. The optimal enzyme activities of BsUGT398 and BsUGT489 were at pH 8.0 with 10 mM of magnesium or calcium ion. In addition, no candidates showed biotransformation activity toward antcin K, which is a major ergostane triterpenoid from the fruiting bodies of Antrodia cinnamomea. One biotransformed metabolite from each BsUGT enzyme was then isolated with preparative high-performance liquid chromatography. The isolated metabolite from each BsUGT was identified as ganoderic acid A-15-O-β-glucoside by mass and nuclear magnetic resonance spectroscopy. The two BsUGTs in the present study are the first identified enzymes that catalyze the 15-O-glycosylation of triterpenoids.
APA, Harvard, Vancouver, ISO, and other styles
8

Zhang, Peng, Zheng Zhang, Lijuan Zhang, Jingjing Wang, and Changsheng Wu. "Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features." Computational and Structural Biotechnology Journal 18 (2020): 1383–90. http://dx.doi.org/10.1016/j.csbj.2020.06.003.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Forget, Stephanie M., Sydney B. Shepard, Ebrahim Soleimani, and David L. Jakeman. "On the Catalytic Activity of a GT1 Family Glycosyltransferase from Streptomyces venezuelae ISP5230." Journal of Organic Chemistry 84, no. 18 (August 20, 2019): 11482–92. http://dx.doi.org/10.1021/acs.joc.9b01130.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Miyamoto, Yuji, Tetsu Mukai, Noboru Nakata, Yumi Maeda, Masanori Kai, Takashi Naka, Ikuya Yano, and Masahiko Makino. "Identification and Characterization of the Genes Involved in Glycosylation Pathways of Mycobacterial Glycopeptidolipid Biosynthesis." Journal of Bacteriology 188, no. 1 (January 1, 2006): 86–95. http://dx.doi.org/10.1128/jb.188.1.86-95.2006.

Full text
Abstract:
ABSTRACT Glycopeptidolipids (GPLs) are major components present on the outer layers of the cell walls of several nontuberculous mycobacteria. GPLs are antigenic molecules and have variant oligosaccharides in mycobacteria such as Mycobacterium avium. In this study, we identified four genes (gtf1, gtf2, gtf3, and gtf4) in the genome of Mycobacterium smegmatis. These genes were independently inactivated by homologous recombination in M. smegmatis, and the structures of GPLs from each gene disruptant were analyzed. Thin-layer chromatography, gas chromatography-mass spectrometry, and matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analyses revealed that the mutants Δgtf1 and Δgtf2 accumulated the fatty acyl-tetrapeptide core having O-methyl-rhamnose and 6-deoxy-talose as sugar residues, respectively. The mutant Δgtf4 possessed the same GPLs as the wild type, whereas the mutant Δgtf3 lacked two minor GPLs, consisting of 3-O-methyl-rhamnose attached to O-methyl-rhamnose of the fatty acyl-tetrapeptide core. These results indicate that the gtf1 and gtf2 genes are responsible for the early glycosylation steps of GPL biosynthesis and the gtf3 gene is involved in transferring a rhamnose residue not to 6-deoxy-talose but to an O-methyl-rhamnose residue. Moreover, a complementation experiment showed that M. avium gtfA and gtfB, which are deduced glycosyltransferase genes of GPL biosynthesis, restore complete GPL production in the mutants Δgtf1 and Δgtf2, respectively. Our findings propose that both M. smegmatis and M. avium have the common glycosylation pathway in the early steps of GPL biosynthesis but differ at the later stages.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Glycosyltransferase (GT61)"

1

Herliana, Lina. "Heterologous Expression and Functional Analysis of Plantago GT61 and DUF579 Genes in Arabidopsis thaliana." Thesis, 2017. http://hdl.handle.net/2440/121634.

Full text
Abstract:
Mucilage released from Plantago ovata seed (psyllium) has been used for maintaining human health as a dietary fibre supplement. Heteroxylan is the main component, and its substitution affects solubility and viscosity of the end product. However, little is known about genes involved in xylan substitution so phylogenetic and transcript information were used to identify candidate genes in the GT61 and DUF579 families and their functions were tested in the model plant Arabidopsis thaliana. Plantago GT61_7, driven by a seed-coat promoter (ProDP1) was transformed into Arabidopsis using a floral dip and spray method. Ruthenium red staining of wild-type and T2 seeds from multiple independent transgenic lines showed a significant difference in the thickness of the adherent mucilage layer. The difference in mucilage phenotype suggests that GT61_7 may have a role in xylan substitution that affects seed coat adherence. This preliminary result needs to be examined using immunolabeling and monosaccharide analysis. For the DUF579 gene AT1G71690, a genome editing approach was adopted. Three single guide RNAs were designed using online tools and in silico analysis was performed to predict any changes in coding and protein sequences by each guide RNA. To test them in vitro, the CRISPR/Cas9 constructs were successfully delivered to protoplast cells using the Transient Expression in Arabidopsis Mesophyll Protoplast (TEAMP) method. However, an analysis using Tracking of Indels by Decomposition(TIDE) showed no evidence of edits in the DUF569 genomic DNA extracted from the protoplasts. Increasing the transfection efficiency or redesigning the sgRNA could lead to improved CRISPR/Cas9 activity.
Thesis (M.Bio.(PB)) -- University of Adelaide, Masters of Biotechnology (Plant Biotechnology), School of Agriculture, Food and Wine, 2017.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Glycosyltransferase (GT61)"

1

Edvardsson, Ellinor, Sunil Kumar Singh, Min-Soo Yun, Agata Mansfeld, Marie-Theres Hauser, and Alan Marchant. "The Plant Glycosyltransferase Family GT64: In Search of a Function." In Annual Plant Reviews, 285–303. Oxford, UK: Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9781444391015.ch11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Egelund, Jack, Miriam Ellis, Monika Doblin, Yongmei Qu, and Antony Bacic. "Genes and Enzymes of the GT31 Family: Towards Unravelling the Function(s) of the Plant Glycosyltransferase Family Members." In Annual Plant Reviews, 213–34. Oxford, UK: Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9781444391015.ch7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Glycosyltransferase (GT61)' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography