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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 (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 ...
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.
Asparagine: Asn N Amide Polar Neutral −3.5 132.119 3.93 AAY Aspartate: Asp D Anion Brønsted base: Negative −3.5 133.104 5.49 GAY Cysteine: Cys C Thiol Brønsted acid Neutral 2.5 250 0.3 121.154 1.38 UGY Glutamine: Gln Q Amide Polar Neutral −3.5 146.146 3.9 CAR Glutamate: Glu E Anion Brønsted base Negative −3.5 147.131 6.32 GAR Glycine ...
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]
Glutamine can exist in either of two enantiomeric forms, L-glutamine and D-glutamine. The L-form is found in nature. Glutamine contains an α-amino group which is in the protonated −NH 3 + form under biological conditions and a carboxylic acid group which is in the deprotonated −COO − form, known as carboxylate, under physiological ...
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