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  2. Hydroxylysine - Wikipedia

    en.wikipedia.org/wiki/Hydroxylysine

    Hydroxylysine (Hyl) is an amino acid with the molecular formula C 6 H 14 N 2 O 3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form. [1] It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen. [2]

  3. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Serine (symbol Ser or S) [3] [4] 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), a carboxyl group (which is in the deprotonated − COO −

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  5. Hydroxy group - Wikipedia

    en.wikipedia.org/wiki/Hydroxy_group

    In chemistry, a hydroxy or hydroxyl group is a functional group with the chemical formula −OH and composed of one oxygen atom covalently bonded to one hydrogen atom. In organic chemistry, alcohols and carboxylic acids contain one or more hydroxy groups.

  6. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    Lysine ball and stick model spinning. Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH ...

  7. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Similar functionality is also presented in serine and threonine, whose side chains have a hydroxy group, but are alcohols. Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, that is greater than the negative charge of the only negatively charged aspartic and glutamic acids ...

  8. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum .

  9. Alkanolamine - Wikipedia

    en.wikipedia.org/wiki/Alkanolamine

    Most proteins and peptides contain both alcohols and amino groups. Two amino acids are alkanolamines, formally speaking: serine and hydroxyproline. Veratridine and veratrine; Tropane alkaloids such as atropine; hormones and neurotransmitters epinephrine (adrenaline) and norepinephrine (noradrenaline)