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  2. Alanine - Wikipedia

    en.wikipedia.org/wiki/Alanine

    L-alanine is second only to L-leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. [5] The right-handed form, D -alanine, occurs in peptides in some bacterial cell walls [ 6 ] : 131 (in peptidoglycan ) and in some peptide antibiotics , and occurs in the tissues of many crustaceans and ...

  3. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Alanine is produced by the transamination of one molecule of pyruvate using two alternate steps: 1) conversion of glutamate to α-ketoglutarate using a glutamate-alanine transaminase, and 2) conversion of valine to α-ketoisovalerate via Transaminase C. Not much is known about the regulation of alanine synthesis.

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids are formally named by the IUPAC-IUBMB Joint Commission on Biochemical Nomenclature in terms of the fictitious "neutral" structure shown in the illustration. For example, the systematic name of alanine is 2-aminopropanoic acid, based on the formula CH 3 −CH(NH 2)−COOH. The Commission justified this approach as follows: [7]

  5. β-Alanine - Wikipedia

    en.wikipedia.org/wiki/Β-Alanine

    β-Alanine (beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon (i.e. the carbon two carbon atoms away from the carboxylate group) instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid.

  6. Cahill cycle - Wikipedia

    en.wikipedia.org/wiki/Cahill_cycle

    The Cahill cycle, also known as the alanine cycle or glucose-alanine cycle, [1] is the series of reactions in which amino groups and carbons from muscle are transported to the liver. [2] It is quite similar to the Cori cycle in the cycling of nutrients between skeletal muscle and the liver. [ 1 ]

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  8. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Indeed, phosphorylation replaces neutral hydroxyl groups on serines, threonines, or tyrosines with negatively charged phosphates with pKs near 1.2 and 6.5. Thus, below pH 5.5, phosphates add a single negative charge; near pH 6.5, they add 1.5 negative charges; above pH 7.5, they add 2 negative charges.

  9. Costco's Healthiest Prepared Foods to Start the New Year Right

    www.aol.com/costcos-healthiest-prepared-foods...

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