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Asparagine synthetase uses ATP to activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP. [22] The biosynthesis of asparagine from oxaloacetate. In reaction that is the reverse of its biosynthesis, asparagine is hydrolyzed to aspartate by asparaginase ...
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 (–COOH) of L-asparagine, an amino acid. [3]
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)
Lysine ball and stick model spinning. 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 ...
Arginine ball and stick model spinning. 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.
The reactivity of a functional group can be modified by other functional groups nearby. Functional group interconversion can be used in retrosynthetic analysis to plan organic synthesis. A functional group is a group of atoms in a molecule with distinctive chemical properties, regardless of the other atoms in the molecule. The atoms in a ...
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).
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 ...
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