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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 ...
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 ...
The first few amino acids were discovered in the early 1800s. [8] [9] In 1806, French chemists Louis-Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound from asparagus that was subsequently named asparagine, the first amino acid to be discovered.
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During heating the amino acid asparagine, naturally present in starchy foods, undergoes a process called the Maillard reaction, which is responsible for giving baked or fried foods their brown color, crust, and toasted flavor. Suspected carcinogens such as acrylamide and some heterocyclic amines are also generated in the Maillard reaction.
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3-Hydroxyasparagine also known as β-hydroxyasparagine (beta-hydroxyasparagine) is a modified asparagine amino acid. It appears in posttranslational modification of cbEGF-like domains which can occur in humans and other Eukaryotes. The amino acid code used for this is Hyn. The modified amino acid residue is found in fibrillin-1. [1]
These two active sites are connected by a tunnel lined primarily with backbone atoms and hydrophobic, nonpolar amino acid residues. [4] Structural characterization of asparagine synthetase from mammalian sources have been difficult due to the low abundance and instability of the enzyme during purification procedures. [5]
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