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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 ...
This page was last edited on 18 May 2006, at 11:44 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply ...
In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction. L-glutamine + pyruvate 2-oxoglutaramate + L-alanine. Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate and L-alanine.
Theanine / ˈ θ iː ən iː n /, commonly known as L-theanine and sometimes L-gamma-glutamylethylamide or N 5-ethyl-L-glutamine, is an amino acid analogue of the proteinogenic amino acids L-glutamate and L-glutamine. It is produced by certain plants such as Camellia sinensis (the tea plant), and by some fungi.
Chemical formula: C 5 H 10 N 2 O 3 Molar mass: 146.15 g·mol −1 Systematic name: (2S)-2-amino-4-carbamoyl-butanoic acid Abbreviations: Q, Gln Synonyms: {γ/+/-/D/L}-Glutamine 2-amino-4-carbamoylbutanoic acid
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
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