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  2. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...

  3. 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 ...

  4. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    It is the covalent attachment between the carbonil group of a reducing sugar (mainly glucose and fructose) and the amino acid side chain of the protein. In this process the intervention of an enzyme is not needed. It takes place across and close to the water channels and the protruding tubules. [21]

  5. Reactive nitrogen - Wikipedia

    en.wikipedia.org/wiki/Reactive_nitrogen

    Reactive nitrogen ("Nr"), also known as fixed nitrogen [1], refers to all forms of nitrogen present in the environment except for molecular nitrogen (N 2 ). [ 2 ] While nitrogen is an essential element for life on Earth, molecular nitrogen is comparatively unreactive, and must be converted to other chemical forms via nitrogen fixation before it ...

  6. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    These glycans link themselves to specific areas of the protein amino acid chain. The two most common linkages in glycoproteins are N-linked and O-linked glycoproteins. [3] An N-linked glycoprotein has glycan bonds to the nitrogen containing an asparagine amino acid within the protein sequence. [4]

  7. SN2 reaction - Wikipedia

    en.wikipedia.org/wiki/SN2_reaction

    Competition experiment between SN2 and E2. With ethyl bromide, the reaction product is predominantly the substitution product. As steric hindrance around the electrophilic center increases, as with isobutyl bromide, substitution is disfavored and elimination is the predominant reaction. Other factors favoring elimination are the strength of the ...

  8. Carbohydrate synthesis - Wikipedia

    en.wikipedia.org/wiki/Carbohydrate_synthesis

    That is the reason why the hydroxyl group at OH-4 in pyranosides is unreactive. Hyperconjugation is involved when OH-4 is anti-periplanar to the ring oxygen, which can also reduce its reactivity. (Scheme 3) Furthermore, acyl protecting groups can reduce the reactivity of the acceptors compared with alkyl protecting groups because of their ...

  9. Glycan - Wikipedia

    en.wikipedia.org/wiki/Glycan

    N-Linked glycans are attached in the endoplasmic reticulum to the nitrogen (N) in the side chain of asparagine (Asn) in the sequon.The sequon is an Asn-X-Ser or Asn-X-Thr sequence, where X is any amino acid except proline and the glycan may be composed of N-acetylgalactosamine, galactose, neuraminic acid, N-acetylglucosamine, fucose, mannose, and other monosaccharides.