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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. Strecker amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Strecker_amino_acid_synthesis

    The Strecker amino acid synthesis, also known simply as the Strecker synthesis, is a method for the synthesis of amino acids by the reaction of an aldehyde with cyanide in the presence of ammonia. The condensation reaction yields an α-aminonitrile, which is subsequently hydrolyzed to give the desired amino acid.

  4. Erlenmeyer–Plöchl azlactone and amino-acid synthesis

    en.wikipedia.org/wiki/Erlenmeyer–Plöchl...

    The Erlenmeyer–Plöchl azlactone and amino acid synthesis, named after Friedrich Gustav Carl Emil Erlenmeyer who partly discovered the reaction, is a series of chemical reactions which transform an N-acyl glycine to various other amino acids via an oxazolone (also known as an azlactone). [1] [2] Azlactone chemistry: step 2 is a Perkin variation

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. 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.

  6. 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 ...

  7. Arndt–Eistert reaction - Wikipedia

    en.wikipedia.org/wiki/Arndt–Eistert_reaction

    In organic chemistry, the Arndt–Eistert reaction is the conversion of a carboxylic acid to its homologue. It is named for the German chemists Fritz Arndt (1885–1969) and Bernd Eistert (1902–1978). The method entails treating an acid chlorides with diazomethane. It is a popular method of producing β-amino acids from α-amino acids. [1]

  8. Seminars in Cell & Developmental Biology

    images.huffingtonpost.com/2013-04-11-Molecular...

    of the acid-induced sweetness of MCL using a cell-based assay system. The results strongly suggested that MCL binds hT1R2–hT1R3 as an antagonist at neutral pH and functionally changes into an agonist at acidic pH. Since sweet-tasting proteins may be used as low-calorie sweeteners because they contain

  9. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.