When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Echinocandin - Wikipedia

    en.wikipedia.org/wiki/Echinocandin

    Beta-glucan destruction prevents resistance against osmotic forces, which leads to cell lysis. [12] They have fungistatic activity against Aspergillus species and fungicidal activity against most Candida spp., including strains that are resistant to fluconazole. [6] In vitro and mouse models show echinocandins may also enhance host immune ...

  3. Mixed-linkage glucan - Wikipedia

    en.wikipedia.org/wiki/Mixed-linkage_glucan

    Mixed-linkage glucan (MLG), sometimes incorrectly referred to as beta-glucan, is a hemicellulosic polysaccharide consisting of β-D(1-3) and β-D(1-4) linked glucosyl residues. MLG is highly prevalent within the Poales , where it has important properties in the diet .

  4. Glucan - Wikipedia

    en.wikipedia.org/wiki/Glucan

    A glucan is a polysaccharide derived from D-glucose, [1] linked by glycosidic bonds. Glucans are noted in two forms: alpha glucans and beta glucans. Many beta-glucans are medically important. They represent a drug target for antifungal medications of the echinocandin class.

  5. Beta-glucan - Wikipedia

    en.wikipedia.org/wiki/Beta-glucan

    In general, β-1,3 linkages are created by 1,3-beta-glucan synthase, and β-1,4 linkages are created by cellulose synthase. The process leading to β-1,6 linkages is poorly understood: although genes important in the process have been identified, not much is known about what each of them do. [9]

  6. Hemicellulose - Wikipedia

    en.wikipedia.org/wiki/Hemicellulose

    Given that mixed-linkage glucan is a non-branched homopolymer of glucose, there is no side-chain synthesis, only the addition of glucose to the backbone in two linkages, β1-3 and β1-4. [10] Backbone synthesis is mediated by enzymes in cellulose synthase-like protein families F and H (CSLF and CSLH), specifically glucan synthase.

  7. Glucanase - Wikipedia

    en.wikipedia.org/wiki/Glucanase

    The first step of his proposed mechanism is rate-limiting step independent of the concentration of the substrate and involves an amino acid nucleophile and an acid/base catalyst. [4] In this step, the nucleophile, with help from the acid residue, displaces the aglycone and forms a covalent glycosyl-enzyme intermediate.

  8. Glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glycosyltransferase

    Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...

  9. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    The binding mechanisms of receptors to the oligosaccharides depends on the composition of the oligosaccharides that are exposed or presented above the surface of the membrane. There is great diversity in the binding mechanisms of glycolipids, which is what makes them such an important target for pathogens as a site for interaction and entrance ...