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  2. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.

  3. Dehydroamino acid - Wikipedia

    en.wikipedia.org/wiki/Dehydroamino_acid

    Dehydroamino acids do not feature amino-alkene groups, but the corresponding N-acylated derivatives are known. These derivatives, also known as N-acylamino acrylates, are prochiral substrates for asymmetric hydrogenation. The 2001 Nobel Prize in Chemistry was awarded to William S. Knowles for his synthesis of L-DOPA from the N-acylacrylate. [4] [5]

  4. Condensation reaction - Wikipedia

    en.wikipedia.org/wiki/Condensation_reaction

    The addition of the two molecules typically proceeds in a step-wise fashion to the addition product, usually in equilibrium, and with loss of a water molecule (hence the name condensation). [3] The reaction may otherwise involve the functional groups of the molecule, and is a versatile class of reactions that can occur in acidic or basic ...

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human body. These intermediates must be ingested, mostly from eating other organisms. [6]

  6. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are asymmetrical molecules. For all standard amino acids, except glycine, the α-carbon is a chiral center. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this ...

  7. Reductive amination - Wikipedia

    en.wikipedia.org/wiki/Reductive_amination

    In biochemistry, dehydrogenase enzymes can catalyze the reductive amination of α-keto acids and ammonia to yield α-amino acids. Reductive amination is predominantly used for the synthesis of the amino acid glutamate starting from α-ketoglutarate, while biochemistry largely relies on transamination to introduce nitrogen in the other amino ...

  8. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  9. Amphibolic - Wikipedia

    en.wikipedia.org/wiki/Amphibolic

    Anabolism has two classes of reactions. The first are dehydration synthesis reactions; these involve the joining of smaller molecules together to form larger, more complex molecules. These include the formation of carbohydrates, proteins, lipids and nucleic acids.