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  2. 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.

  3. Glucagon - Wikipedia

    en.wikipedia.org/wiki/Glucagon

    n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Glucagon is a peptide hormone, produced by alpha cells of the pancreas. It raises the concentration of glucose and fatty acids in the bloodstream and is considered to be the main catabolic hormone of the body. It is also used as a medication ...

  4. Glutaminolysis - Wikipedia

    en.wikipedia.org/wiki/Glutaminolysis

    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.

  5. Glutamate (neurotransmitter) - Wikipedia

    en.wikipedia.org/wiki/Glutamate_(neurotransmitter)

    Glutamate is a very major constituent of a wide variety of proteins; consequently it is one of the most abundant amino acids in the human body. [1] Glutamate is formally classified as a non-essential amino acid, because it can be synthesized (in sufficient quantities for health) from α-ketoglutaric acid, which is produced as part of the citric acid cycle by a series of reactions whose ...

  6. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels. Being a major degradative aminoacid pathway, lysine , proline and threonine are the only three amino acids that do not always undergo transamination and rather use respective dehydrogenase.

  7. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...

  8. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    Protein synthesis, as any other of the 20 proteinogenic amino acids; Lipid synthesis, especially by cancer cells. [8] Regulation of acid-base balance in the kidney by producing ammonium [9] Cellular energy, as a source, next to glucose [10] Nitrogen donation for many anabolic processes, including the synthesis of purines [7]

  9. Glutamine synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutamine_synthetase

    Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. [4] The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. [5] Other reactions may take place via GS.