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  2. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    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.

  3. Glutamine (data page) - Wikipedia

    en.wikipedia.org/wiki/Glutamine_(data_page)

    The complete data for Glutamine ... Structure. Crystal data: Spectral data. UV-Vis: IR: NMR: MS - Masses of main fragments: GMD MS Spectrum: Phase behavior. Solid ...

  4. Glutamine synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutamine_synthetase

    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

  5. Glutaminase - Wikipedia

    en.wikipedia.org/wiki/Glutaminase

    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

  6. Glutamic acid - Wikipedia

    en.wikipedia.org/wiki/Glutamic_acid

    Glutamic acid (symbol Glu or E; [4] the anionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins.It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use.

  7. Glutamate synthase (NADH) - Wikipedia

    en.wikipedia.org/wiki/Glutamate_synthase_(NADH)

    Glutamine will be produced because of the introduction of ammonium in the carbon backbone, which can be converted into glutamate by glutamate synthase of another pathway. [ 2 ] These processes are common in plant roots due to the fact that if the nitrogen deficient conditions exist (with access to ammonium and nitrate ions), there will be a ...

  8. Glutamic protease - Wikipedia

    en.wikipedia.org/wiki/Glutamic_protease

    The first structure of this group of protease was scytalidoglutamic peptidase, the active site of which contains a catalytic dyad, glutamic acid (E) and glutamine (Q), which give rise to the name eqolisin. This group of proteases are found primarily in pathogenic fungi affecting plant and human. [2]

  9. Transglutaminase - Wikipedia

    en.wikipedia.org/wiki/Transglutaminase

    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]

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