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  2. Asparagine - Wikipedia

    en.wikipedia.org/wiki/Asparagine

    Asparagine (symbol Asn or N [2]) is an α-amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic ...

  3. Potassium asparaginate - Wikipedia

    en.wikipedia.org/wiki/Potassium_asparaginate

    Potassium asparaginate is a potassium salt of L-asparagine amino acid. [2] [3] [4] [5]Potassium asparaginate can be considered both a salt and a coordination complex. [6] [3] As a salt, potassium asparaginate is formed when the potassium ion (K +) replaces the hydrogen ion (H +) in the carboxyl group of L-asparagine, an amino acid; in this process, the carboxyl group (–COOH) in L-asparagine ...

  4. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group. Typically, asparagine is converted to aspartic acid or isoaspartic acid. Glutamine is converted to glutamic acid or pyroglutamic acid (5-oxoproline).

  5. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH), and a side chain (CH 2) 4 NH 2 (which ...

  6. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The anionic carboxylate groups behave as Brønsted bases in most circumstances. [32] Enzymes in very low pH environments, like the aspartic protease pepsin in mammalian stomachs, may have catalytic aspartate or glutamate residues that act as Brønsted acids. Functional groups found in histidine (left), lysine (middle) and arginine (right)

  7. Asparagine synthetase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_synthetase

    This depletion of serum asparagine leads to a subsequent rapid efflux of cellular asparagine, which is immediately acted upon and destroyed by the L-asparaginase as well. [5] Due to the transient response from these susceptible cancers in reaction to the asparagine depletion, tumor growth is significantly inhibited due to nutritional deficiency.

  8. Asparagine peptide lyase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_peptide_lyase

    Asparagine peptide lyase are one of the seven groups in which proteases, also termed proteolytic enzymes, peptidases, or proteinases, are classified according to their catalytic residue. The catalytic mechanism of the asparagine peptide lyases involves an asparagine residue acting as nucleophile to perform a nucleophilic elimination reaction ...

  9. 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 ...