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At least 19 recordsLinked to original sources
PubMed1978

Identification of amino sugars from bacterial lipopolysaccharides by gas chromatography electron impact and chemical ionization mass spectrometry.

Amino sugars isolated from lipopolysaccharides of Brucella suis, Brucella abortus and Neisseria gonorrhoeae colony types 1 and 4 were identified using gas chromatography electron impact and chemical ionization mass spectrometry. Lipopolysaccharides were obtained by aqueous ether or aqueous phenol extraction. Isolated lipopolysaccharides were hydrolyzed in 1% acetic acid followed by hydrolysis of the polysaccharide moiety in 2 NHCl for 6 h at 100 degrees C. Amino sugars were first isolated by elution from Dowex 50 H+ and then N-acetylated, followed by trimethylsilylation. Trimethylsilyl ethers of 2-acetamido-2-deoxysugars; N-acetylglucosamine, N-acetylmannosamine, N-acetylgalactosamine, and a 2-acetamido-2.6-dideoxysugar, N-acetylquinovosamine, were identified by their fragmentation patterns. In the electron impact mode, N-acetylglucosamine and N-acetyl-galactosamine were distinguished from one another by comparing peak intensities at m/e 233 and 305. However, N-acetylglucosamine and N-acetylmannosamine could not be differentiated by electron impact mass spectrometry. In the chemical ionization mode, N-acetylglucosamine and N-acetylmannosamine both with base peaks at m/e 494, could be distinguished from N-acetylgalactosamine and N-acetylquinovosamine by their base peaks at m/e 420 and 332, respectively. N-Acetylglucosamine and N-acetylmannosamine were differentiated from one another by comparing peak intensities at m/e 330, 404, 420, and 510 [MH]+. This is the first report of chemical ionization mass spectrometry applied to the identification of amino sugars in bacterial lipopolysaccharides and shows that some 2-amino-2-deoxysugars can be differentiated by both electron impact and chemical ionization mass spectrometry.

Amino Sugars↗
PubMed1977

Relationship between Habs serotypes and 2-amino sugar composition of Pseudomonas aeruginosa.

Thirteen Habs-serotype strains could be classified into 11 groups depending on the characteristic patterns of 2-amino sugar composition; strains of serotypes 2, 5, and 7 had the same pattern, and each other serotype strain had its own distinctive pattern. In our classification, fucosamine and quinovosamine were of importance. We found that fucosamine from strain P14 (Habs serotype 1) was of the D configuration only, unlike DL-fucosamine from strain N10 (Habs serotype 11).

Amino Sugars↗
PubMed1978

Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: N-deacetylation of Escherichia coli peptidoglycan amino sugars.

During intraperiplasmic growth of Bdellovibrio bacteriovorus on Escherichia coli, the substrate cell peptidoglycan is extensively modified as it is converted to bdelloplast peptidoglycan. The initially lysozyme-sensitive peptidoglycan of E. coli was rapidly converted to a lysozyme-resistant form. The conversion was due to the N-deacetylation of a large portion of the peptidoglycan amino sugars. Chemically acetylating the isolated peptidoglycan restored its sensitivity to lysozyme digestion. However, approximately half of the products of lysozyme digestion exhibited hydrophobic interactions that were shown not to be due to the presence of protein. This suggests that a molecule capable of hydrophobic interactions, other than protein, becomes linked to the bdelloplast peptidoglycan. The data also suggest that much of the Braun lipoprotein is removed from the E. coli peptidoglycan early during bdellovibrio development.

Amidohydrolases↗
PubMed1979

A reaction for the simple sensitive fluorimetric assay of heparin and 2-amino sugars.

1. 3,5-Diaminobenzoic acid reacted rapidly with the product from HNO(2) deamination of heparin, heparan sulphate and 2-amino-2-deoxyhexoses under very mild conditions (pH3.0 and 37 degrees C) to give stable fluorescent derivatives. 2. The fluorescence yield was rectilinearly related to the concentration of heparin etc. Less than 0.1mug of 2-amino-2-deoxyhexose was easily measurable in standard cuvettes. 3. The deamination products of glucosamine and (particularly) galactosamine were labile in the HNO(2) reagent, with half-lives of 20-40min at room temperature. At 0 degrees C they were much more stable. The analogous product from heparin was not so labile. 4. Under the standard conditions, and at room temperature, relative fluorescence yields (d-glucosamine=1.0) were: d-galactosamine, 0.75; d-gulosamine, 0.38; d-mannosamine, approx. 0.20. 5. Neutral sugars, chondroitin sulphates, DNA and N-acetylneuraminic acids did not react, nor did N-acetylamino sugars or non-deaminated hexosamines. 6. It is suggested that the Dische-Borenfreund [Dische & Borenfreund (1950) J. Biol. Chem.184, 517-522] indole method, the Kissane-Robins [Kissane & Robins (1962) J. Biol. Chem.233, 184-188] DNA assay and the proposed amino sugar method are all examples of simple aldehyde reactions. The specificity of the proposed method is considerably greater than that of the Dische-Borenfreund procedure, partly because of the much milder reaction conditions. 7. The proposed method is very reproducible, about 50-100 times as sensitive as the Elson-Morgan reaction, and 10-50 times as sensitive as the Dische-Borenfreund procedures. It is also convenient; acid hydrolysates of amino sugar-containing compounds can be directly neutralized with sodium acetate solution.

Amino Sugars↗
PubMed1979

Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts.

1. The major hemorrhagic component (HR1) in the venom of Trimeresurus flavoviridis was purified further by gel filtration on Sephadex G-200, superfine, resulting in its resolution into two parts, 1A and 1B. 1A possessed proteolytic activity towards casein, while 1B was almost free from such activity. Both components were associated with lethal toxicity. 2. The purified preparations of 1A and 1B were homogeneous as judged by several criteria. The molecular weights of the purified principles determined by dodecyl sulfate gel electrophoresis were approximately 60 000. 1A shows anomalous behaviour on ultracentrifugation and gel filtration owing to concentration-dependent polymeric interaction. The purified components were acidic glycoproteins with isoelectric points of 4.4 and they contained neutral sugar, amino sugar and sialic acid altogether amounting to 17-18% on the total weight basis. 3. The two hemorrhagic components were closely related, if not identical, immunologically.

Animals↗
PubMed1979

Phage-related surface modifications of Pseudomonas aeruginosa: effects on the biological activity of viable cells.

Lysogenic [EI(8)3] and phage 8-resistant mutant (EI/8S17) strains of Pseudomonas aeruginosa EI were isolated. Besides lacking the capacity to adsorb phage 8, strains EI(8)3 and EI/8s17 did not contain surface substrate for the depolymerase that is produced de novo when phage 8 infects wild-type strain. EI. The glycolipoprotein (GLP) in the wild type contains phage 8 receptors and surface substrate for the depolymerase, as well as possesses characteristics of a virulence factor; therefore, the chemical and biological characteristics of the derived strains were investigated. The neutral-sugar, amino sugar, and protein content of the GLPs from the derived strains differed quantitatively from that of the wild type. In spite of some cross-reactivity, the GLPs from all strains were antigenically distinct in the indirect hemagglutination inhibition test. In mice, the toxicity of the GLP from strain EI(8)3 equaled that of the wild type, but the GLP of strain EI/8s17 was threefold less toxic. Significantly fewer viable EI(8)3 cells were required for the mouse 50% lethal dose than for the cells of either the wild type or the phage-resistant mutant.

Antigens, Bacterial↗
PubMed2026

Flux rewiring enables native D-glucosamine production in Escherichia coli.

D-Glucosamine is an industrially important amino sugar used in pharmaceuticals, nutraceuticals, and functional materials, yet its production remains dominated by chemical extraction from chitinous biomass, raising sustainability and allergen concerns. Escherichia coli natively synthesizes D-glucosamine directly from D-glucose through endogenous metabolism, revealing an underutilized amino sugar biosynthetic capability. Building on this native pathway, D-glucosamine production was enhanced through targeted genetic modifications and systematic optimization of nitrogen metabolism and cultivation conditions, reaching 9.2 g L-1 under shake-flask conditions. This work extends a phosphorylation-dephosphorylation strategy previously developed for neutral rare sugars to amino sugar biosynthesis, demonstrating the broader applicability of this metabolic design principle. Phosphatase identity emerged as a key control point for product formation: YbiV was the most effective phosphatase for selective D-glucosamine production, whereas alternative phosphatases redirected flux toward D-sedoheptulose. This enzyme-dependent flux partitioning further enabled tunable co-production of D-glucosamine and D-sedoheptulose. Native amino sugar biosynthesis in E. coli provides a controllable framework for producing chemically distinct sugars through endogenous metabolism and establishes a generalizable strategy for engineering amino sugar and other nitrogen-containing metabolite biosynthesis.

Escherichia coli↗