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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 ...
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).
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 ...
Glutaminase (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction: Glutamine + H 2 O → glutamate + NH + 4
Glutamine is the most abundant amino acid in the plasma and an additional energy source in tumor cells especially when glycolytic energy production is low due to a high amount of the dimeric form of M2-PK. Glutamine and its degradation products glutamate and aspartate are precursors for nucleic acid and serine synthesis.
Theanine / ˈ θ iː ən iː n /, also known as L-theanine, L-gamma-glutamylethylamide, or N 5-ethyl-L-glutamine, is a non-proteinogenic amino acid similar to L-glutamate and L-glutamine. It is produced by certain plants such as Camellia sinensis (the tea plant), and by some fungi .
Isoglutamine or α-glutamine is a gamma amino acid derived from glutamic acid by substituting the carboxyl group in position 1 with an amide group. [1] This is in contrast to the proteinogenic amino acid glutamine , which is the 5-amide of glutamic acid.
Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. [1] Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). [2] The reaction is [1]