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  2. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    Leucine ball and stick model spinning. Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side ...

  3. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).

  4. Template:Leucine metabolism in humans - Wikipedia

    en.wikipedia.org/wiki/Template:Leucine...

    To transclude this template as is, use: {{Leucine metabolism in humans | note=yes}} Important: If the note parameter is set to yes (|note=yes), the article receiving the transclusion from this template must have a reference group for "note" included in a "Notes" or "References" section at the end of the article (code: {{Reflist|group=note}}).

  5. Levacetylleucine - Wikipedia

    en.wikipedia.org/wiki/Levacetylleucine

    [1] [2] Levacetylleucine is a modified version of the amino acid leucine (N-Acetyl-L-Leucine). [1] It is the L form of acetylleucine. It is taken by mouth. [1] The most common side effects include abdominal pain, difficulty swallowing, upper respiratory tract infections, and vomiting. [1] [2]

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    This form of peptidase is a zinc metalloenzyme and it is inhibited by the transition state analog. This analog is similar to the actual transition state , so it can make the enzyme bind to it instead of the actual transition state, thus preventing substrate binding and decreasing reaction rates. [ 22 ]

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase. [18] Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its pathway also can inhibit the synthesis of leucine.

  8. Non-proteinogenic amino acids - Wikipedia

    en.wikipedia.org/wiki/Non-proteinogenic_amino_acids

    Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...

  9. β-Leucine - Wikipedia

    en.wikipedia.org/wiki/Β-Leucine

    β-Leucine (beta-leucine) is a beta amino acid and positional isomer of L-leucine which is naturally produced in humans via the metabolism of L-leucine by the enzyme leucine 2,3-aminomutase. [ 1 ] [ 2 ] [ 3 ] In cobalamin (vitamin B 12 ) deficient individuals, plasma concentrations of β-leucine are elevated.