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Journal articles on the topic 'C-glycosyltransferase'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Pelzer, S., R. Süßmuth, D. Heckmann, J. Recktenwald, P. Huber, G. Jung, and W. Wohlleben. "Identification and Analysis of the Balhimycin Biosynthetic Gene Cluster and Its Use for Manipulating Glycopeptide Biosynthesis in Amycolatopsis mediterranei DSM5908." Antimicrobial Agents and Chemotherapy 43, no. 7 (July 1, 1999): 1565–73. http://dx.doi.org/10.1128/aac.43.7.1565.

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ABSTRACT Seven complete genes and one incomplete gene for the biosynthesis of the glycopeptide antibiotic balhimycin were isolated from the producer, Amycolatopsis mediterranei DSM5908, by a reverse-cloning approach and characterized. Using oligonucleotides derived from glycosyltransferase sequences, a 900-bp glycosyltransferase gene fragment was amplified and used to identify a DNA fragment of 9,882 bp. Of the identified open reading frames, three (oxyA to -C) showed significant sequence similarities to cytochrome P450 monooxygenases and one (bhaA) showed similarities to halogenase, and the genesbgtfA to -C showed similarities to glycosyltransferases. Glycopeptide biosynthetic mutants were created by gene inactivation experiments eliminating oxygenase and glycosyltransferase functions. Inactivation of the oxygenase gene(s) resulted in a balhimycin mutant (SP1-1) which was not able to synthesize an antibiotically active compound. Structural analysis by high-performance liquid chromatography–mass spectrometry, fragmentation studies, and amino acid analysis demonstrated that these oxygenases are involved in the coupling of the aromatic side chains of the unusual heptapeptide. Mutant strain HD1, created by inactivation of the glycosyltransferase gene bgtfB, produced at least four different compounds which were not glycosylated but still antibiotically active.

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2

Birch, Helen L., Luke J. Alderwick, Doris Rittmann, Karin Krumbach, Helga Etterich, Anna Grzegorzewicz, Michael R. McNeil, Lothar Eggeling, and Gurdyal S. Besra. "Identification of a Terminal Rhamnopyranosyltransferase (RptA) Involved in Corynebacterium glutamicum Cell Wall Biosynthesis." Journal of Bacteriology 191, no. 15 (May 29, 2009): 4879–87. http://dx.doi.org/10.1128/jb.00296-09.

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ABSTRACT A bioinformatics approach identified a putative integral membrane protein, NCgl0543, in Corynebacterium glutamicum, with 13 predicted transmembrane domains and a glycosyltransferase motif (RXXDE), features that are common to the glycosyltransferase C superfamily of glycosyltransferases. The deletion of C. glutamicum NCgl0543 resulted in a viable mutant. Further glycosyl linkage analyses of the mycolyl-arabinogalactan-peptidoglycan complex revealed a reduction of terminal rhamnopyranosyl-linked residues and, as a result, a corresponding loss of branched 2,5-linked arabinofuranosyl residues, which was fully restored upon the complementation of the deletion mutant by NCgl0543. As a result, we have now termed this previously uncharacterized open reading frame, rhamnopyranosyltransferase A (rptA). Furthermore, an analysis of base-stable extractable lipids from C. glutamicum revealed the presence of decaprenyl-monophosphorylrhamnose, a putative substrate for the cognate cell wall transferase.

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3

Fan, Jing, Chunxian Chen, Qibin Yu, Zheng-Guo Li, and Frederick G. Gmitter. "Characterization of three terpenoid glycosyltransferase genes in ‘Valencia’ sweet orange (Citrus sinensis L. Osbeck)." Genome 53, no. 10 (October 2010): 816–23. http://dx.doi.org/10.1139/g10-068.

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Three putative terpenoid UDP-glycosyltransferase (UGT) genes, designated CsUGT1, CsUGT2, and CsUGT3, were isolated and characterized in ‘Valencia’ sweet orange ( Citrus sinensis L. Osbeck). CsUGT1 consisted of 1493 nucleotides with an open reading frame encoding 492 amino acids, CsUGT2 consisted of 1727 nucleotides encoding 504 amino acids, and CsUGT3 consisted of 1705 nucleotides encoding 468 amino acids. CsUGT3 had a 145 bp intron at 730–874, whereas CsUGT1 and CsUGT2 had none. The three deduced glycosyltransferase proteins had a highly conserved plant secondary product glycosyltransferase motif in the C terminus. Phylogenetic analysis showed that CsUGT1 and CsUGT3 were classified into group L of glycosyltransferase family 1, and CsUGT2 was classified into group D. Through Southern blotting analysis, CsUGT1 was found to have two copies in the sweet orange genome, whereas CsUGT2 and CsUGT3 had at least seven and nine copies, respectively. CsUGT1, CsUGT2, and CsUGT3 were constitutively expressed in leaf, flower, and fruit tissues. The results facilitate further investigation of the function of terpenoid glycosyltransferases in citrus and the biosynthesis of terpenoid glycosides in vitro.

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4

Tegl, Gregor, and Bernd Nidetzky. "Leloir glycosyltransferases of natural product C-glycosylation: structure, mechanism and specificity." Biochemical Society Transactions 48, no. 4 (July 13, 2020): 1583–98. http://dx.doi.org/10.1042/bst20191140.

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A prominent attribute of chemical structure in microbial and plant natural products is aromatic C-glycosylation. In plants, various flavonoid natural products have a β-C-d-glucosyl moiety attached to their core structure. Natural product C-glycosides have attracted significant attention for their own unique bioactivity as well as for representing non-hydrolysable analogs of the canonical O-glycosides. The biosynthesis of natural product C-glycosides is accomplished by sugar nucleotide-dependent (Leloir) glycosyltransferases. Here, we provide an overview on the C-glycosyltransferases of microbial, plant and insect origin that have been biochemically characterized. Despite sharing basic evolutionary relationships, as evidenced by their common membership to glycosyltransferase family GT-1 and conserved GT-B structural fold, the known C-glycosyltransferases are diverse in the structural features that govern their reactivity, selectivity and specificity. Bifunctional glycosyltransferases can form C- and O-glycosides dependent on the structure of the aglycon acceptor. Recent crystal structures of plant C-glycosyltransferases and di-C-glycosyltransferases complement earlier structural studies of bacterial enzymes and provide important molecular insight into the enzymatic discrimination between C- and O-glycosylation. Studies of enzyme structure and mechanism converge on the view of a single displacement (SN2)-like mechanism of enzymatic C-glycosyl transfer, largely analogous to O-glycosyl transfer. The distinction between reactions at the O- or C-acceptor atom is achieved through the precise positioning of the acceptor relative to the donor substrate in the binding pocket. Nonetheless, C-glycosyltransferases may differ in the catalytic strategy applied to induce nucleophilic reactivity at the acceptor carbon. Evidence from the mutagenesis of C-glycosyltransferases may become useful in engineering these enzymes for tailored reactivity.

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5

Kus, Julianne V., John Kelly, Luc Tessier, Hanjeong Harvey, Dennis G. Cvitkovitch, and Lori L. Burrows. "Modification of Pseudomonas aeruginosa Pa5196 Type IV Pilins at Multiple Sites with d-Araf by a Novel GT-C Family Arabinosyltransferase, TfpW." Journal of Bacteriology 190, no. 22 (September 19, 2008): 7464–78. http://dx.doi.org/10.1128/jb.01075-08.

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ABSTRACT Pseudomonas aeruginosa Pa5196 produces type IV pilins modified with unusual α1,5-linked d-arabinofuranose (α1,5-d-Araf) glycans, identical to those in the lipoarabinomannan and arabinogalactan cell wall polymers from Mycobacterium spp. In this work, we identify a second strain of P. aeruginosa, PA7, capable of expressing arabinosylated pilins and use a combination of site-directed mutagenesis, electrospray ionization mass spectrometry (MS), and electron transfer dissociation MS to identify the exact sites and extent of pilin modification in strain Pa5196. Unlike previously characterized type IV pilins that are glycosylated at a single position, those from strain Pa5196 were modified at multiple sites, with modifications of αβ-loop residues Thr64 and Thr66 being important for normal pilus assembly. Trisaccharides of α1,5-d-Araf were the principal modifications at Thr64 and Thr66, with additional mono- and disaccharides identified on Ser residues within the antiparallel beta sheet region of the pilin. TfpW was hypothesized to encode the pilin glycosyltransferase based on its genetic linkage to the pilin, weak similarity to membrane-bound GT-C family glycosyltransferases (which include the Mycobacterium arabinosyltransferases EmbA/B/C), and the presence of characteristic motifs. Loss of TfpW or mutation of key residues within the signature GT-C glycosyltransferase motif completely abrogated pilin glycosylation, confirming its involvement in this process. A Pa5196 pilA mutant complemented with other Pseudomonas pilins containing potential sites of modification expressed nonglycosylated pilins, showing that TfpW's pilin substrate specificity is restricted. TfpW is the prototype of a new type IV pilin posttranslational modification system and the first reported gram-negative member of the GT-C glycosyltransferase family.

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6

Hsieh, Yin-Cheng, Hsi-Ho Chiu, Yen-Chieh Huang, Hoong-Kun Fun, Chia-Yu Lu, Yaw-Kuen Li, and Chun-Jung Chen. "Purification, crystallization and preliminary X-ray crystallographic analysis of glycosyltransferase-1 fromBacillus cereus." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (August 27, 2014): 1228–31. http://dx.doi.org/10.1107/s2053230x14014629.

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Glycosyltransferases (GTs), which are distributed widely in various organisms, including bacteria, fungi, plants and animals, play a role in synthesizing biological compounds. Glycosyltransferase-1 fromBacillus cereus(BcGT-1), which is capable of transferring glucose to small molecules such as kaempferol and quercetin, has been identified as a member of the family 1 glycosyltransferases which utilize uridine diphosphate glucose (UDP-glucose) as the sugar donor.BcGT-1 (molecular mass 45.5 kDa) has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction ofBcGT-1 crystals to 2.10 Å resolution, the crystal belonged to space groupP1, with unit-cell parametersa= 54.56,b= 84.81,c= 100.12 Å, α = 78.36, β = 84.66, γ = 84.84°. Preliminary analysis indicates the presence of fourBcGT-1 molecules in the asymmetric unit with a solvent content of 50.27%.

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7

Chen, Dawei, Ridao Chen, Kebo Xie, Tian Yue, Xiaolin Zhang, Fei Ye, and Jungui Dai. "Biocatalytic C-Glucosylation of Coumarins Using an Engineered C-Glycosyltransferase." Organic Letters 20, no. 6 (February 22, 2018): 1634–37. http://dx.doi.org/10.1021/acs.orglett.8b00378.

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8

Gutmann, Alexander, and Bernd Nidetzky. "Enzymatic C-glycosylation: Insights from the study of a complementary pair of plant O- and C-glucosyltransferases." Pure and Applied Chemistry 85, no. 9 (September 1, 2013): 1865–77. http://dx.doi.org/10.1351/pac-con-12-11-24.

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C-Glycosylation presents a rare mode of sugar attachment to the core structure of natural products and is catalyzed by a special type of Leloir C-glycosyltransferases (C-GTs). Elucidation of mechanistic principles for these glycosyltransferases (GTs) is of fundamental interest, and it could also contribute to the development of new biocatalysts for the synthesis of valuable C-glycosides, potentially serving as analogues of the highly hydrolysis-sensitive O‑glycosides. Enzymatic glucosylation of the natural dihydrochalcone phloretin from UDP‑D-glucose was applied as a model reaction in the study of a structurally and functionally homologous pair of plant glucosyltransferases, where the enzyme from rice (Oryza sativa) was specific for C-glycosylation and the enzyme from pear (Pyrus communis) was specific for O-glycosylation. We show that distinct active-site motifs are used by the two enzymes to differentiate between C- and O-glucosylation of the phloretin acceptor. An enzyme design concept is therefore developed where exchange of active-site motifs results in a reversible switch between C/O-glycosyltransferase (C/O-GT) activity. Mechanistic proposal for enzymatic C-glycosylation involves a single nucleophilic displacement at the glucosyl anomeric carbon, proceeding through an oxocarbenium ion-like transition state. Alternatively, the reaction could be described as Friedel–Crafts-like direct alkylation of the phenolic acceptor.

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9

Geshi, Naomi. "Arabinogalactan Glycosyltransferases: Enzyme Assay, Protein-Protein Interaction, Subcellular Localization, and Perspectives for Application." Advances in Botany 2014 (September 10, 2014): 1–7. http://dx.doi.org/10.1155/2014/434979.

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Arabinogalactan proteins (AGPs) are abundant extracellular proteoglycans that are found in most plant species and involved in many cellular processes, such as cell proliferation and survival, pattern formation, and growth, and in plant microbe interaction. AGPs are synthesized by posttranslational O-glycosylation of proteins and attached glycan part often constitutes greater than 90% of the molecule. Subtle altered glycan structures during development have been considered to function as developmental markers on the cell surface, but little is known concerning the molecular mechanisms. My group has been working on glycosylation enzymes (glycosyltransferases) of AGPs to investigate glycan function of the molecule. This review summarizes the recent findings from my group as for AtGalT31A, AtGlcAT14A-C, and AtGalT29A of Arabidopsis thaliana with a specific focus on the (i) biochemical enzyme activities; (ii) subcellular compartments targeted by the glycosyltransferases; and (iii) protein-protein interactions. I also discuss application aspect of glycosyltransferase in improving AGP-based product used in industry, for example, gum arabic.

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10

Zou, Wei. "C-Glycosides and Aza-C-Glycosides as Potential Glycosidase and Glycosyltransferase Inhibitors." Current Topics in Medicinal Chemistry 5, no. 14 (November 1, 2005): 1363–91. http://dx.doi.org/10.2174/156802605774642999.

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11

Cai, Xiaofeng, Takaaki Taguchi, Huili Wang, Megumi Yuki, Megumi Tanaka, Kai Gong, Jinghua Xu, Yiming Zhao, Koji Ichinose, and Aiying Li. "Identification of a C-Glycosyltransferase Involved in Medermycin Biosynthesis." ACS Chemical Biology 16, no. 6 (June 3, 2021): 1059–69. http://dx.doi.org/10.1021/acschembio.1c00227.

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12

Zhang, Ya-Qun, Zi-Long Wang, Zhuo Chen, Zheng-Tong Jin, Aobulikasimu Hasan, Hai-Dong Wang, Yu-Wei Sun, Xue Qiao, Yong Wang, and Min Ye. "A highly selective 2′′-O-glycosyltransferase from Ziziphus jujuba and De novo biosynthesis of isovitexin 2′′-O-glucoside." Chemical Communications 58, no. 15 (2022): 2472–75. http://dx.doi.org/10.1039/d1cc06949g.

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13

Gutmann, Alexander, Corinna Krump, Linda Bungaruang, and Bernd Nidetzky. "A two-step O- to C-glycosidic bond rearrangement using complementary glycosyltransferase activities." Chem. Commun. 50, no. 41 (2014): 5465–68. http://dx.doi.org/10.1039/c4cc00536h.

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A 2′-O- to 3′-C-glucosidic bond rearrangement on the flavonoid-like aglycon phloretin was catalysed with perfect atom economy by coupled uridine 5′-diphosphate dependent O- and C-glycosyltransferase activities.

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14

Blanco, K. C., F. F. de Moraes, N. S. Bernardi, M. H. P. B. Vettori, R. Monti, and J. Contiero. "Cyclodextrin production by Bacillus lehensis isolated from cassava starch: Characterisation of a novel enzyme." Czech Journal of Food Sciences 32, No. 1 (February 18, 2014): 48–53. http://dx.doi.org/10.17221/432/2012-cjfs.

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The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using β-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cyclodextrin glycosyltransferase were 55°C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.  

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15

Amoah, Obed Jackson, Hue Thi Nguyen, and Jae Kyung Sohng. "N-Glucosylation in Corynebacterium glutamicum with YdhE from Bacillus lichenformis." Molecules 27, no. 11 (May 25, 2022): 3405. http://dx.doi.org/10.3390/molecules27113405.

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Corynebacterium glutamicum is traditionally known as a food-grade microorganism due to its high ability to produce amino acids and its endotoxin-free recombinant protein expression factory. In recent years, studies to improve the activities of useful therapeutics and pharmaceutical compounds have led to the engineering of the therapeutically advantageous C. glutamicum cell factory system. One of the well-studied ways to improve the activities of useful compounds is glucosylation with glycosyltransferases. In this study, we successfully and efficiently glycosylated therapeutic butyl-4-aminobenzoate and other N-linked compounds in C. glutamicum using a promiscuous YdhE, which is a glycosyltransferase from Bacillus lichenformis. For efficient glucosylation, components, such as promoter, codons sequence, expression temperatures, and substrate and glucose concentrations were optimized. With glucose as the sole carbon source, we achieved a conversion rate of almost 96% of the glycosylated products in the culture medium. The glycosylated product of high concentration was successfully purified by a simple purification method, and subjected to further analysis. This is a report of the in vivo cultivation and glucosylation of N-linked compounds in C. glutamicum.

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16

Sun, Y., L. M. Willis, H. R. Batchelder, and M. Nitz. "Site specific protein O-glucosylation with bacterial toxins." Chemical Communications 52, no. 88 (2016): 13024–26. http://dx.doi.org/10.1039/c6cc06223g.

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17

He, Junbin, Kuan Chen, Zhi-min Hu, Kai Li, Wei Song, Li-yan Yu, Chung-Hang Leung, Dik-Lung Ma, Xue Qiao, and Min Ye. "UGT73F17, a new glycosyltransferase from Glycyrrhiza uralensis, catalyzes the regiospecific glycosylation of pentacyclic triterpenoids." Chemical Communications 54, no. 62 (2018): 8594–97. http://dx.doi.org/10.1039/c8cc04215b.

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18

Chen, Dawei, Ridao Chen, Kebo Xie, Yangyang Duan, and Jungui Dai. "Production of acetophenone C-glucosides using an engineered C-glycosyltransferase in Escherichia coli." Tetrahedron Letters 59, no. 19 (May 2018): 1875–78. http://dx.doi.org/10.1016/j.tetlet.2018.04.006.

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19

Tao, Yehui, Ping Sun, Ruxin Cai, Yan Li, and Honghua Jia. "Exploring the Strategy of Fusing Sucrose Synthase to Glycosyltransferase UGT76G1 in Enzymatic Biotransformation." Applied Sciences 12, no. 8 (April 13, 2022): 3911. http://dx.doi.org/10.3390/app12083911.

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Uridine diphosphate glycosyltransferases (UGTs) as fine catalysts of glycosylation are increasingly used in the synthesis of natural products. Sucrose synthase (SuSy) is recognized as a powerful tool for in situ regenerating sugar donors for the UGT-catalyzed reaction. It is crucial to select the appropriate SuSy for cooperation with UGT in a suitable way. In the present study, eukaryotic SuSy from Arabidopsisthaliana (AtSUS1) helped stevia glycosyltransferase UGT76G1 achieve the complete conversion of stevioside (30 g/L) into rebaudioside A (RebA). Position of the individual transcription units containing the genes encoding AtSUS1 and UGT76G1 in the expression plasmid has an effect, but less than that of the fusion order of these genes on RebA yield. Fusion of the C-terminal of AtSUS1 and the N-terminal of UGT76G1 with rigid linkers are conducive to maintaining enzyme activities. When the same fusion strategy was applied to a L637M-T640V double mutant of prokaryotic SuSy from Acidithiobacillus caldus (AcSuSym), 18.8 ± 0.6 g/L RebA (a yield of 78.2%) was accumulated in the reaction mixture catalyzed by the fusion protein Acm-R3-76G1 (the C-terminal of AcSuSym and the N-terminal of UGT76G1 were linked with (EAAAK)3). This work would hopefully reveal the potential of UGT-SuSy fusion in improving the cascade enzymatic glycosylation.

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20

Wang, Bo, Shang-Hui Jin, Hong-Qun Hu, Yan-Guo Sun, Yan-Wen Wang, Ping Han, and Bing-Kai Hou. "UGT87A2, an Arabidopsis glycosyltransferase, regulates flowering time viaFLOWERING LOCUS C." New Phytologist 194, no. 3 (March 9, 2012): 666–75. http://dx.doi.org/10.1111/j.1469-8137.2012.04107.x.

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21

Plewe, Michael, Konrad Sandhoff, and Richard R. Schmidt. "Synthesis of 4-Epoxy-4-c-methyleneglycosylceramides, Potential Glycosyltransferase Inhibitors." Liebigs Annalen der Chemie 1992, no. 7 (July 24, 1992): 699–708. http://dx.doi.org/10.1002/jlac.1992199201118.

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22

Arbeloa, Ana, Heidi Segal, Jean-Emmanuel Hugonnet, Nathalie Josseaume, Lionnel Dubost, Jean-Paul Brouard, Laurent Gutmann, Dominique Mengin-Lecreulx, and Michel Arthur. "Role of Class A Penicillin-Binding Proteins in PBP5-Mediated β-Lactam Resistance in Enterococcus faecalis." Journal of Bacteriology 186, no. 5 (March 1, 2004): 1221–28. http://dx.doi.org/10.1128/jb.186.5.1221-1228.2004.

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ABSTRACT Peptidoglycan polymerization complexes contain multimodular penicillin-binding proteins (PBP) of classes A and B that associate a conserved C-terminal transpeptidase module to an N-terminal glycosyltransferase or morphogenesis module, respectively. In Enterococcus faecalis, class B PBP5 mediates intrinsic resistance to the cephalosporin class of β-lactam antibiotics, such as ceftriaxone. To identify the glycosyltransferase partner(s) of PBP5, combinations of deletions were introduced in all three class A PBP genes of E. faecalis JH2-2 (ponA, pbpF, and pbpZ). Among mutants with single or double deletions, only JH2-2 ΔponA ΔpbpF was susceptible to ceftriaxone. Ceftriaxone resistance was restored by heterologous expression of pbpF from Enterococcus faecium but not by mgt encoding the monofunctional glycosyltransferase of Staphylococcus aureus. Thus, PBP5 partners essential for peptidoglycan polymerization in the presence of β-lactams formed a subset of the class A PBPs of E. faecalis, and heterospecific complementation was observed with an ortholog from E. faecium. Site-directed mutagenesis of pbpF confirmed that the catalytic serine residue of the transpeptidase module was not required for resistance. None of the three class A PBP genes was essential for viability, although deletion of the three genes led to an increase in the generation time and to a decrease in peptidoglycan cross-linking. As the E. faecalis chromosome does not contain any additional glycosyltransferase-related genes, these observations indicate that glycan chain polymerization in the triple mutant is performed by a novel type of glycosyltransferase. The latter enzyme was not inhibited by moenomycin, since deletion of the three class A PBP genes led to high-level resistance to this glycosyltransferase inhibitor.

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23

Khairullina, Alfia, Nikola Micic, Hans J. Lyngs Jørgensen, Nanna Bjarnholt, Leif Bülow, David B. Collinge, and Birgit Jensen. "Biocontrol Effect of Clonostachys rosea on Fusarium graminearum Infection and Mycotoxin Detoxification in Oat (Avena sativa)." Plants 12, no. 3 (January 21, 2023): 500. http://dx.doi.org/10.3390/plants12030500.

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Oat (Avena sativa) is susceptible to Fusarium head blight (FHB). The quality of oat grain is threatened by the accumulation of mycotoxins, particularly the trichothecene deoxynivalenol (DON), which also acts as a virulence factor for the main pathogen Fusarium graminearum. The plant can defend itself, e.g., by DON detoxification by UGT-glycosyltransferases (UTGs) and accumulation of PR-proteins, even though these mechanisms do not deliver effective levels of resistance. We studied the ability of the fungal biocontrol agent (BCA) Clonostachys rosea to reduce FHB and mycotoxin accumulation. Greenhouse trials showed that C. rosea-inoculation of oat spikelets at anthesis 3 days prior to F. graminearum inoculation reduced both the amount of Fusarium DNA (79%) and DON level (80%) in mature oat kernels substantially. DON applied to C. rosea-treated spikelets resulted in higher conversion of DON to DON-3-Glc than in mock treated plants. Moreover, there was a significant enhancement of expression of two oat UGT-glycosyltransferase genes in C. rosea-treated oat. In addition, C. rosea treatment activated expression of genes encoding four PR-proteins and a WRKY23-like transcription factor, suggesting that C. rosea may induce resistance in oat. Thus, C. rosea IK726 has strong potential to be used as a BCA against FHB in oat as it inhibits F. graminearum infection effectively, whilst detoxifying DON mycotoxin rapidly.

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24

Nguyen, Hai P., and Kenichi Yokoyama. "Characterization of Acyl Carrier Protein-Dependent Glycosyltransferase in Mitomycin C Biosynthesis." Biochemistry 58, no. 25 (June 7, 2019): 2804–8. http://dx.doi.org/10.1021/acs.biochem.9b00379.

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25

Dürr, Clemens, Dirk Hoffmeister, Sven-Eric Wohlert, Koji Ichinose, Monika Weber, Ursula von Mulert, Jon S. Thorson, and Andreas Bechthold. "The Glycosyltransferase UrdGT2 Catalyzes Both C- and O-Glycosidic Sugar Transfers." Angewandte Chemie International Edition 43, no. 22 (May 24, 2004): 2962–65. http://dx.doi.org/10.1002/anie.200453758.

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26

Dürr, Clemens, Dirk Hoffmeister, Sven-Eric Wohlert, Koji Ichinose, Monika Weber, Ursula von Mulert, Jon S. Thorson, and Andreas Bechthold. "Die Glycosyltransferase UrdGT2 katalysiert sowohl C- als auch O-glycosidischen Zuckertransfer." Angewandte Chemie 116, no. 22 (May 24, 2004): 3022–25. http://dx.doi.org/10.1002/ange.200453758.

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27

Chen, Dawei, Shuai Fan, Ridao Chen, Kebo Xie, Sen Yin, Lili Sun, Jimei Liu, et al. "Probing and Engineering Key Residues for Bis-C-glycosylation and Promiscuity of a C-Glycosyltransferase." ACS Catalysis 8, no. 6 (April 23, 2018): 4917–27. http://dx.doi.org/10.1021/acscatal.8b00376.

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28

Shepherd, Micah D., Tao Liu, Carmen Méndez, Jose A. Salas, and Jürgen Rohr. "Engineered Biosynthesis of Gilvocarcin Analogues with Altered Deoxyhexopyranose Moieties." Applied and Environmental Microbiology 77, no. 2 (November 12, 2010): 435–41. http://dx.doi.org/10.1128/aem.01774-10.

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ABSTRACTA combinatorial biosynthetic approach was used to interrogate the donor substrate flexibility of GilGT, the glycosyltransferase involved inC-glycosylation during gilvocarcin biosynthesis. Complementation of gilvocarcin mutantStreptomyces lividansTK24 (cosG9B3-U−), in which the biosynthesis of the natural sugar donor substrate was compromised, with various deoxysugar plasmids led to the generation of six gilvocarcin analogues with altered saccharide moieties. Characterization of the isolated gilvocarcin derivatives revealed five new compounds, including 4-β-C-d-olivosyl-gilvocarcin V (d-olivosyl GV), 4-β-C-d-olivosyl-gilvocarcin M (d-olivosyl GM), 4-β-C-d-olivosyl-gilvocarcin E (d-olivosyl GE), 4-α-C-l-rhamnosyl-gilvocarcin M (polycarcin M), 4-α-C-l-rhamnosyl-gilvocarcin E (polycarcin E), and the recently characterized 4-α-C-l-rhamnosyl-gilvocarcin V (polycarcin V). Preliminary anticancer assays showed thatd-olivosyl-gilvocarcin and polycarcin V exhibit antitumor activities comparable to that of their parent drug congener, gilvocarcin V, against human lung cancer (H460), murine lung cancer (LL/2), and breast cancer (MCF-7) cell lines. Our findings demonstrate GilGT to be a moderately flexibleC-glycosyltransferase able to transfer bothd- andl-hexopyranose moieties to the unique angucyclinone-derived benzo[d]naphtho[1,2b]pyran-6-one backbone of the gilvocarcins.

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Scherman, Hataichanok, Devinder Kaur, Ha Pham, Henrieta Škovierová, Mary Jackson, and Patrick J. Brennan. "Identification of a Polyprenylphosphomannosyl Synthase Involved in the Synthesis of Mycobacterial Mannosides." Journal of Bacteriology 191, no. 21 (August 28, 2009): 6769–72. http://dx.doi.org/10.1128/jb.00431-09.

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ABSTRACT We report on the identification of a glycosyltransferase (GT) from Mycobacterium tuberculosis H37Rv, Rv3779, of the membranous GT-C superfamily responsible for the direct synthesis of polyprenyl-phospho-mannopyranose and thus indirectly for lipoarabinomannan, lipomannan, and the higher-order phosphatidyl-myo-inositol mannosides.

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Voitsekhovskaia, Irina, Constanze Paulus, Charlotte Dahlem, Yuriy Rebets, Suvd Nadmid, Josef Zapp, Denis Axenov-Gribanov, et al. "Baikalomycins A-C, New Aquayamycin-Type Angucyclines Isolated from Lake Baikal Derived Streptomyces sp. IB201691-2A." Microorganisms 8, no. 5 (May 7, 2020): 680. http://dx.doi.org/10.3390/microorganisms8050680.

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Natural products produced by bacteria found in unusual and poorly studied ecosystems, such as Lake Baikal, represent a promising source of new valuable drug leads. Here we report the isolation of a new Streptomyces sp. strain IB201691-2A from the Lake Baikal endemic mollusk Benedictia baicalensis. In the course of an activity guided screening three new angucyclines, named baikalomycins A–C, were isolated and characterized, highlighting the potential of poorly investigated ecological niches. Besides that, the strain was found to accumulate large quantities of rabelomycin and 5-hydroxy-rabelomycin, known shunt products in angucyclines biosynthesis. Baikalomycins A–C demonstrated varying degrees of anticancer activity. Rabelomycin and 5-hydroxy-rabelomycin further demonstrated antiproliferative activities. The structure elucidation showed that baikalomycin A is a modified aquayamycin with β-d-amicetose and two additional hydroxyl groups at unusual positions (6a and 12a) of aglycone. Baikalomycins B and C have alternating second sugars attached, α-l-amicetose and α-l-aculose, respectively. The gene cluster for baikalomycins biosynthesis was identified by genome mining, cloned using a transformation-associated recombination technique and successfully expressed in S. albus J1074. It contains a typical set of genes responsible for an angucycline core assembly, all necessary genes for the deoxy sugars biosynthesis, and three genes coding for the glycosyltransferase enzymes. Heterologous expression and deletion experiments allowed to assign the function of glycosyltransferases involved in the decoration of baikalomycins aglycone.

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PLEWE, M., K. SANDHOFF, and R. R. SCHMIDT. "ChemInform Abstract: Synthesis of 4-Epoxy-4-C-methyleneglycosylceramides, Potential Glycosyltransferase Inhibitors." ChemInform 23, no. 46 (August 21, 2010): no. http://dx.doi.org/10.1002/chin.199246237.

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Tam, Heng Keat, Johannes Härle, Stefan Gerhardt, Jürgen Rohr, Guojun Wang, Jon S. Thorson, Aurélien Bigot, et al. "Strukturelle Charakterisierung von O- und C-glycosylierenden Varianten der Landomycin-Glycosyltransferase LanGT2." Angewandte Chemie 127, no. 9 (January 7, 2015): 2853–57. http://dx.doi.org/10.1002/ange.201409792.

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33

Wang, Fengbin, Maoquan Zhou, Shanteri Singh, Ragothaman M. Yennamalli, Craig A. Bingman, Jon S. Thorson, and George N. Phillips. "Crystal structure of SsfS6, the putative C -glycosyltransferase involved in SF2575 biosynthesis." Proteins: Structure, Function, and Bioinformatics 81, no. 7 (April 20, 2013): 1277–82. http://dx.doi.org/10.1002/prot.24289.

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34

He, Jun‐Bin, Peng Zhao, Zhi‐Min Hu, Shuang Liu, Yi Kuang, Meng Zhang, Bin Li, Cai‐Hong Yun, Xue Qiao, and Min Ye. "Molecular and Structural Characterization of a Promiscuous C ‐Glycosyltransferase from Trollius chinensis." Angewandte Chemie International Edition 58, no. 33 (August 12, 2019): 11513–20. http://dx.doi.org/10.1002/anie.201905505.

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35

Kelly, Steven D., Bradley R. Clarke, Olga G. Ovchinnikova, Ryan P. Sweeney, Monica L. Williamson, Todd L. Lowary, and Chris Whitfield. "Klebsiella pneumoniae O1 and O2ac antigens provide prototypes for an unusual strategy for polysaccharide antigen diversification." Journal of Biological Chemistry 294, no. 28 (May 28, 2019): 10863–76. http://dx.doi.org/10.1074/jbc.ra119.008969.

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A limited range of different structures is observed in O-antigenic polysaccharides (OPSs) from Klebsiella pneumoniae lipopolysaccharides. Among these, several are based on modifications of a conserved core element of serotype O2a OPS, which has a disaccharide repeat structure [→3)-α-d-Galp-(1→3)-β-d-Galf-(1→]. Here, we describe the enzymatic pathways for a highly unusual modification strategy involving the attachment of a second glycan repeat-unit structure to the nonreducing terminus of O2a. This occurs by the addition of the O1 [→3)-α-d-Galp-(1→3)-β-d-Galp-(1→] or O2c [→3)-β-d-GlcpNAc-(1→5)-β-d-Galf-(1→] antigens. The organization of the enzyme activities performing these modifications differs, with the enzyme WbbY possessing two glycosyltransferase catalytic sites solely responsible for O1 antigen polymerization and forming a complex with the O2a glycosyltransferase WbbM. In contrast, O2c polymerization requires glycosyltransferases WbmV and WbmW, which interact with one another but apparently not with WbbM. Using defined synthetic acceptors and site-directed mutants to assign the activities of the WbbY catalytic sites, we found that the C-terminal WbbY domain is a UDP-Galp–dependent GT-A galactosyltransferase adding β-(1→3)–linked d-Galp, whereas the WbbY N terminus includes a GT-B enzyme adding α-(1→3)–linked d-Galp. These activities build the O1 antigen on a terminal Galp in the O2a domain. Using similar approaches, we identified WbmV as the UDP-GlcNAc transferase and noted that WbmW represents a UDP-Galf–dependent enzyme and that both are GT-A members. WbmVW polymerizes the O2c antigen on a terminal Galf. Our results provide mechanistic and conceptual insights into an important strategy for polysaccharide antigen diversification in bacteria.

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Jungui, Dai. "Biocatalytic bis-C-alkylation of phenolics using one-pot cascades with promiscuous C-glycosyltransferase and prenyltransferase." Journal of Chinese Pharmaceutical Sciences 2018, no. 4 (April 15, 2018): 241–50. http://dx.doi.org/10.5246/jcps.2018.04.025.

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37

GUÉRARDEL, Yann, Luis BALANZINO, Emmanuel MAES, Yves LEROY, Bernadette CODDEVILLE, Rafael ORIOL, and Gérard STRECKER. "The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides." Biochemical Journal 357, no. 1 (June 25, 2001): 167–82. http://dx.doi.org/10.1042/bj3570167.

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The free-living nematode Caenorhabditis elegans is a relevant model for studies on the role of glycoconjugates during development of multicellular organisms. Several genes coding for glycosyltransferases involved in the synthesis of N- and O-linked glycans have already been isolated, but, apart from repetitive dimers of glycosaminoglycans, no detailed structure of either type of component has been published so far. This study aimed to establish the structures of the major O-glycans synthesized by C. elegans to give an insight into the endogenous glycosyltransferase activities expressed in this organism. By the use of NMR and MS, we have resolved the sequence of seven of these components that present very unusual features. Most of them were characterized by the type-1 core substituted on Gal and/or GalNAc by (β1–4)Glc and (β1–6)Glc residues. Another compound exhibited the GalNAc(β1–4)N-acetylglucosaminitol sequence in the terminal position, to which was attached a tetramer of β-Gal substituted by both Fuc and 2-O-methyl-fucose residues. Our experimental procedure led also to the isolation of glycosaminoglycan-like components and oligomannosyl-type N-glycans. In particular, the data confirmed that C. elegans synthesizes the ubiquitous linker sequence GlcA(β1–3)Gal(β1–3)Gal(β1–4)Xyl.

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Larson, Eric T., Dirk Reiter, Mark Young, and C. Martin Lawrence. "Structure of A197 from Sulfolobus Turreted Icosahedral Virus: a Crenarchaeal Viral Glycosyltransferase Exhibiting the GT-A Fold." Journal of Virology 80, no. 15 (August 1, 2006): 7636–44. http://dx.doi.org/10.1128/jvi.00567-06.

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ABSTRACT Sulfolobus turreted icosahedral virus (STIV) was the first icosahedral virus characterized from an archaeal host. It infects Sulfolobus species that thrive in the acidic hot springs (pH 2.9 to 3.9 and 72 to 92°C) of Yellowstone National Park. The overall capsid architecture and the structure of its major capsid protein are very similar to those of the bacteriophage PRD1 and eukaryotic viruses Paramecium bursaria Chlorella virus 1 and adenovirus, suggesting a viral lineage that predates the three domains of life. The 17,663-base-pair, circular, double-stranded DNA genome contains 36 potential open reading frames, whose sequences generally show little similarity to other genes in the sequence databases. However, functional and evolutionary information may be suggested by a protein's three-dimensional structure. To this end, we have undertaken structural studies of the STIV proteome. Here we report our work on A197, the product of an STIV open reading frame. The structure of A197 reveals a GT-A fold that is common to many members of the glycosyltransferase superfamily. A197 possesses a canonical DXD motif and a putative catalytic base that are hallmarks of this family of enzymes, strongly suggesting a glycosyltransferase activity for A197. Potential roles for the putative glycosyltransferase activity of A197 and their evolutionary implications are discussed.

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39

Rajesh, Y., K. Narayanan, V. M. Subrahmanyam, and J. Venkata Rao. "BIOPROSPECTING FOR CYCLODEXTRIN GLYCOSYLTRANSFERASE PRODUCING BACTERIA." INDIAN DRUGS 51, no. 06 (June 28, 2014): 44–48. http://dx.doi.org/10.53879/id.51.06.p0044.

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Cyclodextrin glycosyltransferase- (CGTase), (EC.2.4.1.19) producing micro-organisms were isolated from different sources of soil (paddy plantation, potato plantation, garden and Malpe beach) from places in and around Udupi, India. A potential isolate MBS 24 was identified as Virgibacillus pantothenticus. This organism was cultivated on modified Horikoshi medium at 130 rpm for 24 h at 32 °C. The maximum production of CGTase enzyme was observed (0.308μmol/ml β-CD units) after 36 h of incubation at 32°C and pH 10.0. CGTase was precipitated using ammonium sulphate at 60% saturation. Cyclodextrin (CD) produced by incubation of CGTase with starch was extracted using toluene and analyzed by thin layer chromatography. Rf values of the solvent extracted CD were similar to the standard α, β and γ CD confirming that all three types of CD’s were formed during enzymatic conversion. These CDs could be used as drug carrier for delivering BCS class II drugs.

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40

Liu, Meizi, Dandan Wang, Yang Li, Xuemiao Li, Guangning Zong, Shuang Fei, Xue Yang, Jianping Lin, Xiaoqiang Wang, and Yuequan Shen. "Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation." Plant Cell 32, no. 9 (July 22, 2020): 2917–31. http://dx.doi.org/10.1105/tpc.20.00002.

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41

Ying, Yanling, Xiaozhen Hong, Shu Chen, Ji He, and Faming Zhu. "c.518T > C missense mutation in the B glycosyltransferase gene responsible for a weak B variant." Transfusion 58, no. 1 (November 6, 2017): 269–70. http://dx.doi.org/10.1111/trf.14381.

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42

Fischbach, M. A., H. Lin, D. R. Liu, and C. T. Walsh. "From The Cover: In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase." Proceedings of the National Academy of Sciences 102, no. 3 (December 14, 2004): 571–76. http://dx.doi.org/10.1073/pnas.0408463102.

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43

Chen, Dawei, Ridao Chen, Ruishan Wang, Jianhua Li, Kebo Xie, Chuancai Bian, Lili Sun, et al. "Probing the Catalytic Promiscuity of a Regio- and Stereospecific C-Glycosyltransferase fromMangifera indica." Angewandte Chemie 127, no. 43 (September 10, 2015): 12869–73. http://dx.doi.org/10.1002/ange.201506505.

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44

Vidal, Sébastien, Isabelle Bruyère, Annie Malleron, Claudine Augé, and Jean-Pierre Praly. "Non-isosteric C-glycosyl analogues of natural nucleotide diphosphate sugars as glycosyltransferase inhibitors." Bioorganic & Medicinal Chemistry 14, no. 21 (November 2006): 7293–301. http://dx.doi.org/10.1016/j.bmc.2006.06.057.

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45

Chen, Dawei, Ridao Chen, Ruishan Wang, Jianhua Li, Kebo Xie, Chuancai Bian, Lili Sun, et al. "Probing the Catalytic Promiscuity of a Regio- and Stereospecific C-Glycosyltransferase fromMangifera indica." Angewandte Chemie International Edition 54, no. 43 (September 1, 2015): 12678–82. http://dx.doi.org/10.1002/anie.201506505.

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46

Tam, Heng Keat, Johannes Härle, Stefan Gerhardt, Jürgen Rohr, Guojun Wang, Jon S. Thorson, Aurélien Bigot, et al. "Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2." Angewandte Chemie International Edition 54, no. 9 (January 7, 2015): 2811–15. http://dx.doi.org/10.1002/anie.201409792.

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47

Ovchinnikova, Olga G., Evan Mallette, Akihiko Koizumi, Todd L. Lowary, Matthew S. Kimber, and Chris Whitfield. "Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99)." Proceedings of the National Academy of Sciences 113, no. 22 (May 19, 2016): E3120—E3129. http://dx.doi.org/10.1073/pnas.1603146113.

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Kdo (3-deoxy-d-manno-oct-2-ulosonic acid) is an eight-carbon sugar mostly confined to Gram-negative bacteria. It is often involved in attaching surface polysaccharides to their lipid anchors. α-Kdo provides a bridge between lipid A and the core oligosaccharide in all bacterial LPSs, whereas an oligosaccharide of β-Kdo residues links “group 2” capsular polysaccharides to (lyso)phosphatidylglycerol. β-Kdo is also found in a small number of other bacterial polysaccharides. The structure and function of the prototypical cytidine monophosphate-Kdo–dependent α-Kdo glycosyltransferase from LPS assembly is well characterized. In contrast, the β-Kdo counterparts were not identified as glycosyltransferase enzymes by bioinformatics tools and were not represented among the 98 currently recognized glycosyltransferase families in the Carbohydrate-Active Enzymes database. We report the crystallographic structure and function of a prototype β-Kdo GT from WbbB, a modular protein participating in LPS O-antigen synthesis inRaoultella terrigena. The β-Kdo GT has dual Rossmann-fold motifs typical of GT-B enzymes, but extensive deletions, insertions, and rearrangements result in a unique architecture that makes it a prototype for a new GT family (GT99). The cytidine monophosphate-binding site in the C-terminal α/β domain closely resembles the corresponding site in bacterial sialyltransferases, suggesting an evolutionary connection that is not immediately evident from the overall fold or sequence similarities.

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48

Wang, Guohong, Jiaxi Li, Shuxin Xie, Zhengyuan Zhai, and Yanling Hao. "The N-terminal domain of rhamnosyltransferase EpsF influences exopolysaccharide chain length determination in Streptococcus thermophilus 05-34." PeerJ 8 (February 12, 2020): e8524. http://dx.doi.org/10.7717/peerj.8524.

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Glycosyltransferases are key enzymes involved in the assembly of repeating units of exopolysaccharides (EPS). A glycosyltransferase generally consists of the N-terminal and the C-terminal domain, however, the functional role of these domains in EPS biosynthesis remains largely unknown. In this study, homologous overexpression was employed to investigate the effects of EpsFN, a truncated form of rhamnosyltransferase EpsF with only the N-terminal domain, on EPS biosynthesis in Streptococcus thermophilus 05-34. Reverse transcription qPCR and Western blotting analysis confirmed the successful expression of epsFN in 05-34 at the transcription and translation level, respectively. Further analysis showed that the monosaccharide composition and yield of EPS were not affected by the overexpression of epsFN, whereas the molecular mass decreased by 5-fold. Accordingly, the transcription levels of genes involved in EPS biosynthesis, including chain-length determination gene epsC, were down-regulated by 5- to 6-fold. These results indicated that the N-terminal domain of EpsF alone could influence the molecular mass of EPS, probably via lowering the concentration of sugar precursors, which may lead to decreased expression of genes responsible for chain-length determination.

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Chang, Y. C., A. Jong, S. Huang, P. Zerfas, and K. J. Kwon-Chung. "CPS1, a Homolog of the Streptococcus pneumoniae Type 3 Polysaccharide Synthase Gene, Is Important for the Pathobiology of Cryptococcus neoformans." Infection and Immunity 74, no. 7 (July 2006): 3930–38. http://dx.doi.org/10.1128/iai.00089-06.

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ABSTRACT The polysaccharide capsule is known to be the major factor required for the virulence of Cryptococcus neoformans. We have cloned and characterized a gene, designated CPS1, that encodes a protein containing a glycosyltransferase moiety and shares similarity with the type 3 polysaccharide synthase encoded by the cap3B gene of Streptococcus pneumoniae. Cps1p also shares similarity with hyaluronan synthase of higher eukaryotes. Deletion of the CPS1 gene from a serotype D strain of C. neoformans resulted in a slight reduction of the capsule size as observed by using an India ink preparation. The growth at 37°C was impaired, and the ability to associate with human brain endothelial cells in vitro was also significantly reduced by the deletion of CPS1. Using site-specific mutagenesis, we showed that the conserved glycosyltransferase domains are critical for the ability of the strain to grow at elevated temperatures. A hyaluronan enzyme-linked immunosorbent assay method demonstrated that CPS1 is important for the synthesis of hyaluronan or its related polysaccharides in C. neoformans. Comparisons between the wild-type and the cps1Δ strains, using three different transmission electron microscopic methods, indicated that the CPS1 gene product is involved in the composition or maintenance of an electron-dense layer between the outer cell wall and the capsule. These and the virulence studies in a mouse model suggested that the CPS1 gene is important in the pathobiology of C. neoformans.

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50

Allison, Sarah E., Michael A. D'Elia, Sharif Arar, Mario A. Monteiro, and Eric D. Brown. "Studies of the Genetics, Function, and Kinetic Mechanism of TagE, the Wall Teichoic Acid Glycosyltransferase in Bacillus subtilis 168." Journal of Biological Chemistry 286, no. 27 (May 10, 2011): 23708–16. http://dx.doi.org/10.1074/jbc.m111.241265.

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The biosynthetic enzymes involved in wall teichoic acid biogenesis in Gram-positive bacteria have been the subject of renewed investigation in recent years with the benefit of modern tools of biochemistry and genetics. Nevertheless, there have been only limited investigations into the enzymes that glycosylate wall teichoic acid. Decades-old experiments in the model Gram-positive bacterium, Bacillus subtilis 168, using phage-resistant mutants implicated tagE (also called gtaA and rodD) as the gene coding for the wall teichoic acid glycosyltransferase. This study and others have provided only indirect evidence to support a role for TagE in wall teichoic acid glycosylation. In this work, we showed that deletion of tagE resulted in the loss of α-glucose at the C-2 position of glycerol in the poly(glycerol phosphate) polymer backbone. We also reported the first kinetic characterization of pure, recombinant wall teichoic acid glycosyltransferase using clean synthetic substrates. We investigated the substrate specificity of TagE using a wide variety of acceptor substrates and found that the enzyme had a strong kinetic preference for the transfer of glucose from UDP-glucose to glycerol phosphate in polymeric form. Further, we showed that the enzyme recognized its polymeric (and repetitive) substrate with a sequential kinetic mechanism. This work provides direct evidence that TagE is the wall teichoic acid glycosyltransferase in B. subtilis 168 and provides a strong basis for further studies of the mechanism of wall teichoic acid glycosylation, a largely uncharted aspect of wall teichoic acid biogenesis.

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