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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. Asparagine (data page) - Wikipedia

    en.wikipedia.org/wiki/Asparagine_(data_page)

    Chemical formula: C 4 H 8 N 2 O 3 Molar mass: 132.118 g·mol −1 Systematic name: (2S)-2-amino-3-carbamoyl-propanoic acid Abbreviations: N, Asn Synonyms: (S)-2-aminosuccinic acid 4-amide {α/2}-aminosuccinamic acid Agedoite Altheine Asparagine acid Asparamide Asparatamine Aspartamic acid Aspartamine Aspartic acid β-amide Aspartic acid amide ...

  4. 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 ...

  5. Asparaginase - Wikipedia

    en.wikipedia.org/wiki/Asparaginase

    By adding asparaginase before baking or frying the food, asparagine is converted into another common amino acid, aspartic acid, and ammonium. As a result, asparagine cannot take part in the Maillard reaction, and therefore the formation of acrylamide is significantly reduced.

  6. Asparagine synthetase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_synthetase

    Escherichia coli derived asparagine synthetase is a dimeric protein with each subunit folding into two distinct domains. [4] The N-terminal region consists of two layers of six-stranded antiparallel β-sheets between which is the active site responsible for the hydrolysis of glutamine. [4]

  7. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are protonated, resulting in a cation.

  8. Glutamin-(asparagin-)ase - Wikipedia

    en.wikipedia.org/wiki/Glutamin-(asparagin-)ase

    In enzymology, a glutamin-(asparagin-)ase (EC 3.5.1.38) is an enzyme that catalyzes the chemical reaction. L-glutamine + H 2 O L-glutamate + NH 3. Thus, the two substrates of this enzyme are L-glutamine and H 2 O, whereas its two products are L-glutamate and NH 3.

  9. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    In both cases, the acceptor substrate is an asparagine residue. The asparagine residue linked to an N-linked oligosaccharide usually occurs in the sequence Asn-X-Ser/Thr, [7] where X can be any amino acid except for proline, although it is rare to see Asp, Glu, Leu, or Trp in this position. [citation needed]