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  2. Leucines - Wikipedia

    en.wikipedia.org/wiki/Leucines

    The leucines are primarily the four isomeric amino acids: leucine, isoleucine, tert-leucine (terleucine, pseudoleucine) and norleucine. [1] Being compared with the four butanols, they could be classified as butyl-substituted glycines; they represent all four possible variations.

  3. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    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 chain isobutyl group, making it a non ...

  4. Isoleucine - Wikipedia

    en.wikipedia.org/wiki/Isoleucine

    Isoleucine (symbol Ile or I) [1] is an α-amino acid that is used in the biosynthesis of proteins.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 hydrocarbon side chain with a branch (a central carbon atom bound to three other ...

  5. Stable isotope composition of amino acids - Wikipedia

    en.wikipedia.org/wiki/Stable_isotope_composition...

    Some amino acids have carbon isotope compositions that reflect the organism that produced them. The x axis is the difference in δ 13 C between isoleucine and leucine, while the y axis shows this difference for isolecuine and lysine. There are clear clusters of points corresponding to bacteria, fungi, and plants.

  6. Branched-chain amino acid - Wikipedia

    en.wikipedia.org/wiki/Branched-chain_amino_acid

    A deficiency of this complex leads to a buildup of the branched-chain amino acids (leucine, isoleucine, and valine) and their toxic by-products in the blood and urine, giving the condition the name maple syrup urine disease. On the other hand, unchecked activity of this complex causes branched-chain keto acid dehydrogenase kinase deficiency.

  7. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Isoleucine: I Ile Ile is essential for humans. Isoleucine, leucine, and valine have large aliphatic hydrophobic side chains. Their molecules are rigid, and their mutual hydrophobic interactions are important for the correct folding of proteins, as these chains tend to be located inside of the protein molecule. Leucine or isoleucine: J Xle

  8. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Feedback inhibition of final products is the main method of inhibition, and, in E. coli, the ilvEDA operon also plays a part in this regulation. This diagram shows the biosynthesis (anabolism) of amino acids alanine, valine, isoleucine, and leucine from the precursor pyruvate.

  9. Conservative replacement - Wikipedia

    en.wikipedia.org/wiki/Conservative_replacement

    For example, leucine and isoleucine are both aliphatic, branched hydrophobes. Similarly, aspartic acid and glutamic acid are both small, negatively charged residues. Although there are many ways to classify amino acids, they are often sorted into six main classes on the basis of their structure and the general chemical characteristics of their ...

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