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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea cycle. The other product of transamidation is a keto acid that enters the citric acid cycle. [85] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis. [86]

  3. 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 ...

  4. Amine - Wikipedia

    en.wikipedia.org/wiki/Amine

    Amine. In chemistry, amines (/ ə ˈ m iː n, ˈ æ m iː n /, [1] [2] UK also / ˈ eɪ m iː n / [3]) are compounds and functional groups that contain a basic nitrogen atom with a lone pair.Formally, amines are derivatives of ammonia (NH 3), wherein one or more hydrogen atoms have been replaced by a substituent such as an alkyl or aryl group [4] (these may respectively be called alkylamines ...

  5. Imino acid - Wikipedia

    en.wikipedia.org/wiki/Imino_acid

    proline. Secondary amino acids, amino acids containing a secondary amine group are sometimes named imino acids, [2] [3] though this usage is obsolescent. [1] The only proteinogenic amino acid of this type is proline, although the related non-proteinogenic amino acids hydroxyproline [4] [5] [6] and pipecolic acid [7] have often been included in studies of this class of compounds.

  6. Beta-peptide - Wikipedia

    en.wikipedia.org/wiki/Beta-peptide

    β-alanine, an example of a β-amino acid. The amino group attaches not to the α carbon but to the β-carbon, which in this case is a methylene group.. Beta-peptides (β-peptides) are peptides derived from β-amino acids, in which the amino group is attached to the β-carbon (i.e. the carbon two atoms away from the carboxylate group).

  7. 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).

  8. Indolamines - Wikipedia

    en.wikipedia.org/wiki/Indolamines

    A common example of an indolamine is the tryptophan derivative serotonin, a neurotransmitter involved in mood and sleep. [1] Another example of an indolamine is melatonin. In biochemistry, indolamines are substituted indole compounds that contain an amino group. Examples of indolamines include the lysergamides.

  9. Aminoaldehydes and aminoketones - Wikipedia

    en.wikipedia.org/wiki/Aminoaldehydes_and_aminoke...

    Aminoaldehydes and aminoketones are organic compounds that contain an amine functional group as well as either a aldehyde or ketone functional group. These compounds are important in biology and in chemical synthesis. Because of their bifunctional nature, they have attracted much attention from chemists.