Found 19 structures.
Displayed structures from 1 to 15
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1. Compound ID: 70
Structure type: oligomer
Trivial name: raffinose
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_164059,IEDB_190606,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 17
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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2. Compound ID: 71
Structure type: oligomer
Trivial name: stachyose
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_164059,IEDB_190606,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 17
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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3. Compound ID: 4932
Structure type: oligomer
Trivial name: trehalulose
Contained glycoepitopes: IEDB_142488,IEDB_144998,IEDB_146664,IEDB_164059,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 1898
Miyata Y, Sugitani T, Tsuyuki KI, Ebashi T, Nakajima Y "Isolation and characterization of Pseudomonas mesoacidophila producing trehalulose" -
Bioscience, Biotechnology, and Biochemistry 56 (1992) 1680-1681
no abstract
Publication DOI: 10.1271/bbb.56.1680Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Research and Development Department, Mitsui Sugar Co., Ltd
- Article ID: 1899
Nagai-Miyata Y, Tsuyuki KI, Sugitani T, Ebashi T, Nakajima Y "Isolation and characterization of a trehalulose-producing strain of Agrobacterium" -
Bioscience, Biotechnology, and Biochemistry 57 (1993) 2049-2053
A novel strain, MX-232, which produced much trehalulose (1-O-α-D-glucopyranosyl-D-fructose), was isolated from a soil sample in Udonthani, Thailand. The isolate was a Gram-negative aerobic rod, motile with peritrichous flagella, and had a high ability to convert sucrose into trehalulose and isomaltulose (palatinose, 6-O-α-D-glucopyranosyl-D-fructose) with α-glucosyltransferase. The results of physiological characterization, G+C content, and pathogenicity tests on several plants showed that MX-232 is a strain of Agrobacterium radiobacter. When free cells and 20% (w/v) sucrose solution were used in the reaction, the yield of trehalulose was 88-90% (w/w). And with immobilized cells, the yield was about 85% when 40-50% (w/w) sucrose solution was used as the substrate. Using immobilized cells in a column reaction was good for producing trehalulose. This report suggests MX-232 has the highest ability to produce trehalulose from sucrose.
Publication DOI: 10.1271/bbb.57.2049Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Research and Development Department, Mitsui Sugar Co., Ltd.
- Article ID: 1900
Nagai Y, Sugitani T, Tsuyuki KI "Characterization of a-glucosyltransferase from Pseudomonas mesoacidophila MX-45" -
Bioscience, Biotechnology, and Biochemistry 58 (1994) 1789-1793
α-Glucosyltransferase was purified from Pseudomonas mesoacidophila MX-45. The molecular weight was estimated to be 63,000 by SDS-PAGE, and the isoelectric point was pI 5.4. For enzyme activity based on sucrose decomposition, the optimum pH and the optimum temperature were pH 5.8 and 40 degrees C, respectively. The ranges of stable pH and temperature were pH 5.1-6.7 and below 40 degrees C, respectively. The purified enzyme of MX-45 converted sucrose into trehalulose (1-O-α-D-glucopyranosyl- D-fructose) and isomaltulose (palatinose, 6-O-α-D-glucopyranosyl-D-fructose) simultaneously, and the ratio of trehalulose to isomaltulose increased at lower reaction temperatures. Therefore, optimum conditions for trehalulose production were pH 5.5-6.5 at 20 degrees C. The yield of trehalulose from sucrose (20-40% solution) was 91%. The Km for sucrose was 19.2 +/- 3.3 mM estimated by the Hanes-Woolf plot. Product inhibition was observed, and the product inhibition constant was 0.17 M. Hg2+, Fe3+, Cu2+, Mg2+, Ag+, Pb2+, glucono-1,5-lactone, and Tris(hydroxymethyl)aminomethane inhibited the reaction.
NCBI PubMed ID: 7765505Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Food Laboratory, Mitsui Sugar Co., Ltd., Kanagawa, Japan
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4. Compound ID: 4934
Structure type: oligomer
Trivial name: isomaltulose, palatinose
Contained glycoepitopes: IEDB_142488,IEDB_144998,IEDB_146664,IEDB_164059,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 1900
Nagai Y, Sugitani T, Tsuyuki KI "Characterization of a-glucosyltransferase from Pseudomonas mesoacidophila MX-45" -
Bioscience, Biotechnology, and Biochemistry 58 (1994) 1789-1793
α-Glucosyltransferase was purified from Pseudomonas mesoacidophila MX-45. The molecular weight was estimated to be 63,000 by SDS-PAGE, and the isoelectric point was pI 5.4. For enzyme activity based on sucrose decomposition, the optimum pH and the optimum temperature were pH 5.8 and 40 degrees C, respectively. The ranges of stable pH and temperature were pH 5.1-6.7 and below 40 degrees C, respectively. The purified enzyme of MX-45 converted sucrose into trehalulose (1-O-α-D-glucopyranosyl- D-fructose) and isomaltulose (palatinose, 6-O-α-D-glucopyranosyl-D-fructose) simultaneously, and the ratio of trehalulose to isomaltulose increased at lower reaction temperatures. Therefore, optimum conditions for trehalulose production were pH 5.5-6.5 at 20 degrees C. The yield of trehalulose from sucrose (20-40% solution) was 91%. The Km for sucrose was 19.2 +/- 3.3 mM estimated by the Hanes-Woolf plot. Product inhibition was observed, and the product inhibition constant was 0.17 M. Hg2+, Fe3+, Cu2+, Mg2+, Ag+, Pb2+, glucono-1,5-lactone, and Tris(hydroxymethyl)aminomethane inhibited the reaction.
NCBI PubMed ID: 7765505Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Food Laboratory, Mitsui Sugar Co., Ltd., Kanagawa, Japan
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5. Compound ID: 4991
Structure type: oligomer
Trivial name: levan
Compound class: EPS
Contained glycoepitopes: IEDB_164059,IEDB_923066
The structure is contained in the following publication(s):
- Article ID: 1938
Kasapis S, Morris ER, Gross M, Rudolph K "Solution properties of levan polysaccharide from Pseudomonas syringae pv. phaseolicola, and its possible primary role as a blocker of recognition during pathogenesis" -
Carbohydrate Polymers 23(1) (1994) 55-64
Bacterial levan, a highly branched, high molecular weight polymer of fructose, was purified from culture supernatants of Pseudomonas syringaepv.phaseolicola grown in a liquid high-sucrose medium, and the predominance of β-(2 → 6) linkages was confirmed by 13C NMR. The solution properties of this material resembled those of disordered linear polysaccharides in the response to low-amplitude oscillatory shear (frequency dependence of G′ and G″); the absence of any detectable conformational change with temperature (as monitored by optical rotation); close superposition of steady-shear viscosity (η) and complex dynamic viscosity (gh*) at equivalent values of shear-rate (γs-1) and frequency (ωrad s-1); a similar form of shear-thinning (giving linear plots of η versus ηγ0.76); and the onset of semi-dilute behaviour at a closely comparable degree of space-occupancy (c[η] ≈ 3·6). The intrinsic viscosity, however, was unusually low ([η] ≈ 0·17 dl g−1) and the concentration dependence of ‘zero-shear’ viscosity in the semi-dilute regime unusually high (η0 ∼ c9·3), as anticipated from the densely packed, branched molecular structure. Solutions of levan and pectin, matched to approximately the same initial viscosity, showed a substantial reduction in viscosity when mixed. Similar behaviour was observed for mixed solutions of levan with locust bean gum (LBG), chosen for its structural similarity to cellulose and hemicelluloses of the plant cell wall. Viscosity reduction was eliminated at low concentrations (indicating that it does not arise from heterologous association), but became very pronounced at high concentrations, and was then accompanied by resolution into levan-rich and LBG-rich solution phases. This evidence of strong thermodynamic incompatibility and exclusion behaviour with (1 → 4)-linked plant polysaccharides suggests that the primary role of levan during pathogenesis may be as a barrier to intimate morphological contact (recognition) between plant cell walls and those of the parasite, thus inhibiting initiation of a hypersensitive response by the host.
Publication DOI: 10.1016/0144-8617(94)90090-6Journal NLM ID: 8307156Publisher: Elsevier
Institutions: Department of Food Research and Technology, Cranfield University, Silsoe College, Silsoe, Bedford MK45 4DT, UK, Institut für Pflanzenpathologie und Pflanzenschutz der Universität Göttingen, Grisebachstr.6, D-3400 Göttingen, Germany
Methods: optical rotation measurement, rheological measurements, chiroptical measurements, viscosity measurements
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6. Compound ID: 6048
Structure type: oligomer
Contained glycoepitopes: IEDB_164059,IEDB_923066
The structure is contained in the following publication(s):
- Article ID: 2694
Tanaka K, Karigane T, Yamaguchi F "Isolation of levanoligosaccharides from a partial acid hydrolyzate of levan by cellulose column chromatography" -
Journal of Chromatography 265 (1983) 374-377
no abstract
Publication DOI: 10.1016/S0021-9673(01)96736-6Journal NLM ID: 0427043Publisher: Amsterdam: Elsevier
Institutions: Department of Biology, Osaka Kyoiku University, Tennoji-ku, Osaka, Osaka 543 Japan
Methods: TLC, acid hydrolysis, carbon-celite CC
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7. Compound ID: 6049
Structure type: oligomer
Contained glycoepitopes: IEDB_164059,IEDB_923066
The structure is contained in the following publication(s):
- Article ID: 2694
Tanaka K, Karigane T, Yamaguchi F "Isolation of levanoligosaccharides from a partial acid hydrolyzate of levan by cellulose column chromatography" -
Journal of Chromatography 265 (1983) 374-377
no abstract
Publication DOI: 10.1016/S0021-9673(01)96736-6Journal NLM ID: 0427043Publisher: Amsterdam: Elsevier
Institutions: Department of Biology, Osaka Kyoiku University, Tennoji-ku, Osaka, Osaka 543 Japan
Methods: TLC, acid hydrolysis, carbon-celite CC
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8. Compound ID: 6050
|
b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-D-Fru |
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Structure type: oligomer
Contained glycoepitopes: IEDB_164059,IEDB_923066
The structure is contained in the following publication(s):
- Article ID: 2694
Tanaka K, Karigane T, Yamaguchi F "Isolation of levanoligosaccharides from a partial acid hydrolyzate of levan by cellulose column chromatography" -
Journal of Chromatography 265 (1983) 374-377
no abstract
Publication DOI: 10.1016/S0021-9673(01)96736-6Journal NLM ID: 0427043Publisher: Amsterdam: Elsevier
Institutions: Department of Biology, Osaka Kyoiku University, Tennoji-ku, Osaka, Osaka 543 Japan
Methods: TLC, acid hydrolysis, carbon-celite CC
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9. Compound ID: 6051
|
b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-b-D-Fruf-(2-6)-D-Fru |
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Structure type: oligomer
Contained glycoepitopes: IEDB_164059,IEDB_923066
The structure is contained in the following publication(s):
- Article ID: 2694
Tanaka K, Karigane T, Yamaguchi F "Isolation of levanoligosaccharides from a partial acid hydrolyzate of levan by cellulose column chromatography" -
Journal of Chromatography 265 (1983) 374-377
no abstract
Publication DOI: 10.1016/S0021-9673(01)96736-6Journal NLM ID: 0427043Publisher: Amsterdam: Elsevier
Institutions: Department of Biology, Osaka Kyoiku University, Tennoji-ku, Osaka, Osaka 543 Japan
Methods: TLC, acid hydrolysis, carbon-celite CC
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10. Compound ID: 6137
Structure type: oligomer
Trivial name: inulotetraose
Contained glycoepitopes: IEDB_164059,IEDB_923067
The structure is contained in the following publication(s):
- Article ID: 2736
Kishimoto M, Kobayashi S, Nagata K, Honbo K, Kadoma M, Kainuma K "Inulotetraose-producing Bacillus KK-4645" -
Kokai Tokkyo Koho = unexamined Japanese Patent Applications [Japanese] (1987) 1-3
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11. Compound ID: 7231
Structure type: monomer
Contained glycoepitopes: IEDB_164059
The structure is contained in the following publication(s):
- Article ID: 3271
De Leon GP, Elowe NH, Koteva KP, Valvano MA, Wright GD "An In Vitro Screen of Bacterial Lipopolysaccharide Biosynthetic Enzymes Identifies an Inhibitor of ADP-Heptose Biosynthesis" -
Chemistry and Biology 13(4) (2006) 437-441
The lipopolysaccharide (LPS)-rich outer membrane of gram-negative bacteria provides a protective barrier that insulates these organisms from the action of numerous antibiotics. Breach of the LPS layer can therefore provide access to the cell interior to otherwise impermeant toxic molecules and can expose vulnerable binding sites for immune system components such as complement. Inhibition of LPS biosynthesis, leading to a truncated LPS molecule, is an alternative strategy for antibacterial drug development in which this vital cellular structure is weakened. A significant challenge for in vitro screens of small molecules for inhibition of LPS biosynthesis is the difficulty in accessing the complex carbohydrate substrates. We have optimized an assay of the enzymes required for LPS heptose biosynthesis that simultaneously surveys five enzyme activities by using commercially available substrates and report its use in a small-molecule screen that identifies an inhibitor of heptose synthesis
Lipopolysaccharide, biosynthesis, synthesis, LPS, structure, heptose, alternative, biosynthetic, Bacterial, carbohydrate, cell, molecule, Research, complex, bacteria, activity, biochemistry, Gram-negative bacteria, enzyme, gram negative bacteria, Gram-negative, cellular, inhibition, component, binding, binding site, site, Enzymes, action, membrane, substrate, heptose biosynthesis, protective, outer membrane, PDF, assay, immune, immune system, in vitro, use, challenge, development, drug, layer, complement, inhibitor, antibiotic, antimicrobial, antibacterial, toxic, Binding Sites, antibiotics, barrier
NCBI PubMed ID: 16632256Journal NLM ID: 9500160Publisher: Maryland Heights, MO: Elsevier
Correspondence: wrightge@mcmaster.ca
Institutions: Antimicrobial Research Centre Department of Biochemistry and Biomedical Sciences McMaster University Hamilton, Hamilton, ON, Canada, Infectious Diseases Research Group Siebens-Drake Research Institute Department of Microbiology and Immunology The University of Western Ontario London, Ontario N6A 5C1 Canada
Methods: biochemical methods
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12. Compound ID: 7731
Structure type: monomer
Trivial name: D-fructose-6-phosphate
Contained glycoepitopes: IEDB_164059
The structure is contained in the following publication(s):
- Article ID: 3454
Cook PD, Holden HM "GDP-Perosamine Synthase: Structural Analysis and Production of a Novel Trideoxysugar" -
Biochemistry 47(9) (2008) 2833-2840
Perosamine or 4-amino-4,6-dideoxy- d-mannose is an unusual sugar found in the O-antigens of some Gram-negative bacteria such as Vibrio cholerae O1 (the causative agent of cholera) or Escherichia coli O157:H7 (the leading cause of food-borne illnesses). It and similar deoxysugars are added to the O-antigens of bacteria via the action of glycosyltransferases that employ nucleotide-linked sugars as their substrates. The focus of this report is GDP-perosamine synthase, a PLP-dependent enzyme that catalyzes the last step in the formation of GDP-perosamine, namely, the amination of the sugar C-4'. Here we describe the three-dimensional structure of the enzyme from Caulobacter crescentus determined to a nominal resolution of 1.8 A and refined to an R-factor of 17.9%. The overall fold of the enzyme places it into the well-characterized aspartate aminotransferase superfamily. Each subunit of the dimeric enzyme contains a seven-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet, and 12 alpha-helices. Amino acid residues from both subunits form the active sites of the GDP-perosamine synthase dimer. Recently, the structure of another PLP-dependent enzyme, GDP-4-keto-6-deoxy- d-mannose-3-dehydratase (or ColD), was determined in our laboratory, and this enzyme employs the same substrate as GDP-perosamine synthase. Unlike GDP-perosamine synthase, however, ColD functions as a dehydratase that removes the sugar C-3' hydroxyl group. By purifying the ColD product and reacting it with purified GDP-perosamine synthase, we have produced a novel GDP-linked sugar, GDP-4-amino-3,4,6-trideoxy-d-mannose. Details describing the X-ray structural investigation of GDP-perosamine synthase and the enzymatic synthesis of GDP-4-amino-3,4,6-trideoxy-d-mannose are presented.
X-ray, Escherichia coli O157:H7, O-antigens, glycosyltransferases, Vibrio cholerae O1, perosamine, enzymatic synthesis
NCBI PubMed ID: 18247575Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: Hazel_Holden@biochem.wisc.edu
Institutions: Department of Biochemistry, UniVersity of Wisconsin, Madison, Wisconsin 53706
Methods: 13C NMR, 1H NMR, X-ray, sugar analysis, ESI-MS, genetic methods, biochemical methods, HPLC, crystallization
- Article ID: 3524
Namboori SC, Graham DE "Acetamido sugar biosynthesis in the Euryarchaea" -
Journal of Bacteriology 190(8) (2008) 2987-2996
Archaea and eukaryotes share a dolichol phosphate-dependent system for protein N-glycosylation. In both domains, the acetamido sugar N-acetylglucosamine (GlcNAc) forms part of the core oligosaccharide. However, the archaeal Methanococcales produced GlcNAc using the bacterial biosynthetic pathway. Key enzymes in this pathway belong to large families of proteins with diverse functions; therefore the archaeal enzymes could not be identified solely using comparative sequence analysis. Genes encoding acetamido sugar biosynthetic proteins were identified in Methanococcus maripaludis using phylogenetic and gene cluster analyses. Proteins expressed in Escherichia coli were purified and assayed for the predicted activities. The MMP1680 protein encodes a universally conserved glucosamine-6-phosphate synthase. The MMP1077 phosphomutase converted α-D-glucosamine-6-phosphate to α-D-glucosamine-1-phosphate, although this protein is more closely related to archaeal pentose and glucose phosphomutases than to bacterial glucosamine phosphomutases. The thermostable MJ1101 protein catalyzed both the acetylation of glucosamine-1-phosphate and the uridylyltransferase reaction with uridine triphosphate to produce UDP-GlcNAc. The MMP0705 protein catalyzed the C-2 epimerization of UDP-GlcNAc, and the MMP0706 protein used NAD(+) to oxidize UDP-N-acetylmannosamine forming UDP-N-acetylmannosaminuronate (ManNAcA). These two proteins are similar to enzymes used for proteobacterial lipopolysaccharide biosynthesis and Gram-positive bacterial capsule production, suggesting a common evolutionary origin and a widespread distribution of ManNAcA. UDP-GlcNAc and UDP-ManNAcA biosynthesis evolved early in the euryarchaeal lineage, because most of their genomes contain orthologs of the five genes characterized here. These UDP-acetamido sugars are predicted to be precursors for flagellin and S-layer protein modifications, and for the biosynthesis of methanogenic coenzyme B
biosynthesis, core oligosaccharide, gene cluster, S-layer, archaea, phylogenetic
NCBI PubMed ID: 18263721Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: degraham@mail.utexas.edu
Institutions: Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, TX 78712
Methods: 1H NMR, SDS-PAGE, 31P NMR, genetic methods, biochemical methods, LC-ESI-MS
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13. Compound ID: 10920
Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_164059
The structure is contained in the following publication(s):
- Article ID: 4431
Ovodov YS "Bacterial capsular antigens. Structural patterns of capsular antigens" -
Biochemistry (Moscow) 71(9) (2006) 937-954
Structural patterns of bacterial capsular antigens including capsular polysaccharides and exoglycans are given in this review. In addition, the immunological activity of capsular antigens and their role in type specificity of bacteria are discussed.
structure, capsular polysaccharides, bacterial capsular antigens, bacterial exoglycans, immunological activity, type specificity
NCBI PubMed ID: 17009947Publication DOI: 10.1134/S000629790609001XJournal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: ovoys@physiol.komisc.ru
Institutions: Institute of Physiology, Komi Science Center, Urals Branch of the Russian Academy of Sciences, Syktyvkar 167982, Russia
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14. Compound ID: 15975
|
b-D-Xylp-(1-4)-+
|
a-D-Xylp-(1-2)-a-D-Glcp-(1-6)-b-D-Glcp-(1-5)-+ |
| |
-1)-b-D-Frup-(2-2)-b-D-Xylp-(1-6)-b-D-Fruf-(2-4)-b-D-Ribp-(1- |
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Structure type: polymer chemical repeating unit
Compound class: EPS
Contained glycoepitopes: IEDB_114701,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_164059,IEDB_167188,IEDB_174332,IEDB_581504,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 6195
Andrew M, Jayaraman G "Molecular Characterization and Biocompatibility of Exopolysaccharide Produced by Moderately Halophilic Bacterium Virgibacillus dokdonensis from the Saltern of Kumta Coast" -
Polymers 14(9) (2022) 3986
The use of natural polysaccharides as biomaterials is gaining importance in tissue engineering due to their inherent biocompatibility. In this direction, the present study aims to explore the structure and biocompatibility of the EPS produced by Virgibacillus dokdonensis VITP14. This marine bacterium produces 17.3 g/L of EPS at 96 h of fermentation. The EPS was purified using ion exchange and gel permeation chromatographic methods. The porous web-like structure and elemental composition (C, O, Na, Mg, P, S) of the EPS were inferred from SEM and EDX analysis. AFM analysis revealed spike-like lumps with a surface roughness of 84.85 nm. The zeta potential value of -10 mV indicates the anionic nature of the EPS. Initial molecular characterization showed that the EPS is a heteropolysaccharide composed of glucose (25.8%), ribose (18.6%), fructose (31.5%), and xylose (24%), which are the monosaccharide units in the HPLC analysis. The FTIR spectrum indicates the presence of functional groups/bonds typical of EPSs (O-H, C-H, C-O-H, C-O, S=O, and P=O). The polymer has an average molecular weight of 555 kDa. Further, NMR analysis revealed the monomer composition, the existence of two α- and six β-glycosidic linkages, and the branched repeating unit as →1)[α-D-Xylp-(1→2)-α-D-Glcp-(1→6)-β-D-Glcp-(1→5)]-β-D-Frup-(2→2)[β-D-Xylp-(1→4)]-β-D-Xylp-(1→6)-β-D-Fruf-(2→4)-β-D-Ribp-(1→. The EPS is thermally stable till 251.4 °C. X-ray diffraction analysis confirmed the semicrystalline (54.2%) nature of the EPS. Further, the EPS exhibits significant water solubility (76.5%), water-holding capacity (266.8%), emulsifying index (66.8%), hemocompatibility (erythrocyte protection > 87%), and cytocompatibility (cell viability > 80% on RAW264.7 and keratinocyte HaCaT cells) at higher concentrations and prolongs coagulation time in APTT and PT tests. Our research unveils the significant biocompatibility of VITP14 EPS for synthesizing a variety of biomaterials.
exopolysaccharides, fermentation, Marine bacteria, anticoagulant activity, Structural characterization, halophiles, biomaterial, cytocompatibility, hemocompatibility
NCBI PubMed ID: 36235941Publication DOI: 10.3390/polym14193986Journal NLM ID: 101545357Publisher: Basel: MDPI
Correspondence: G. Jayaraman
Institutions: School of Biosciences and Technology, Vellore Institute of Technology, Vellore 632014, Tamil Nadu, India
Methods: 13C NMR, 1H NMR, NMR-2D, X-ray, FTIR, HPLC, GPC, statistical analysis, zeta potential measurement, cell viability assay, SEM, AFM, emulsifying activity determination, TGA, WHC, X-ray EDX, hemolytic activity, hemolysis activity, anticoagulant activity
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15. Compound ID: 18692
Structure type: oligomer
; 527 [M+Na]+
Contained glycoepitopes: IEDB_142488,IEDB_144998,IEDB_146664,IEDB_164059,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 7328
Okada H, Fukushi E, Yamamori A, Kawazoe N, Onodera S, Kawabata J, Shiomi N "Isolation and structural confirmation of the oligosaccharides containing α-D-fructofuranoside linkages isolated from fermented beverage of plant extracts" -
Carbohydrate Research 346(16) (2011) 2633-2637
Fermented beverage of plant extracts was prepared from the extracts of approximately 50 types of vegetables and fruits. Natural fermentation was carried out mainly by lactic acid bacteria (Leuconostoc spp.) and yeast (Zygosaccharomyces spp. and Pichia spp.). Two oligosaccharides containing an α-fructofuranoside linkage were detected in this beverage and isolated using carbon-Celite column chromatography and preparative HPLC. The structural confirmation of the saccharides was determined by methylation analysis, MALDI-TOF-MS, and NMR measurements. These saccharides were identified as α-D-fructofuranosyl-(2→6)-D-glucopyranose, which was isolated from a natural source for the first time, and a novel saccharide β-D-fructopyranosyl-(2→6)-α-D-fructofuranosyl-(2↔1)-α-D-glucopyranoside
oligosaccharide, Fermented beverage of plant extracts, a-D-Fructofuranoside, Natural fructopyranoside
NCBI PubMed ID: 21996604Publication DOI: 10.1016/j.carres.2011.09.002Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: Okada H
Institutions: General Institute of Ohtakakohso Co., Otaru, Japan, Graduate School of Agriculture, Hokkaido University, Sapporo, Japan, Department of Food and Nutrition Sciences, Graduate School of Dairy Science Research, Rakuno Gakuen University, Ebetsu, Japan
Methods: 13C NMR, 1H NMR, methylation, acid hydrolysis, GLC, HPAEC, MALDI-TOF MS, methanolysis, HPLC, extraction, HMBC, COSY, HSQC-TOCSY
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