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Glutamine ball and stick model spinning. Glutamine (symbol Gln or Q) [3] is an α-amino acid that is used in the biosynthesis of proteins.Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide.
Glutamine is converted to glutamic acid or pyroglutamic acid (5-oxoproline). In a protein or peptide, these reactions are important because they may alter its structure, stability or function and may lead to protein degradation. The net chemical change is the addition of a water group and removal of an ammonia group, which corresponds to a +1 ...
Glutamine synthetase (GS) (EC 6.3.1.2) [3] is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH 3 → Glutamine + ADP + phosphate
Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Usually, it is located on the outer surface of the protein, making it water-soluble. It binds to positively charged molecules and ions, and is often used in enzymes to fix the metal ion. When located inside of the protein, aspartate and glutamate are usually paired with arginine and lysine. Glutamic acid: E Glu
The adenylation activity is catalyzed by the bifunctional adenylyltransferase/adenylyl removal (AT/AR) enzyme. Glutamine and a regulatory protein called PII act together to stimulate adenylation. [3] This diagram shows the biosynthesis (anabolism) of amino acids glutamate, glutamine, proline, and arginine from the precursor alpha-ketoglutarate.