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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. Oxidative deamination - Wikipedia

    en.wikipedia.org/wiki/Oxidative_deamination

    Glutamate can then be regenerated from α-KG via the action of transaminases or aminotransferase, which catalyze the transfer of an amino group from an amino acid to an α-keto acid. In this manner, an amino acid can transfer its amine group to glutamate, after which GDH can then liberate ammonia via oxidative deamination. This is a common ...

  4. 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).

  5. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and ...

  6. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In nature, the process of making proteins encoded by RNA genetic material is called translation and involves the step-by-step addition of amino acids to a growing protein chain by a ribozyme that is called a ribosome. [64]

  7. Coenzyme A - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_A

    Its acetyl-coenzyme A form is the primary input in the citric acid cycle and is obtained from glycolysis, amino acid metabolism, and fatty acid beta oxidation. This process is the body's primary catabolic pathway and is essential in breaking down the building blocks of the cell such as carbohydrates, amino acids, and lipids. [20]

  8. Amine oxide - Wikipedia

    en.wikipedia.org/wiki/Amine_oxide

    Almost all amine oxides are prepared by the oxidation of either tertiary aliphatic amines or aromatic N-heterocycles. Hydrogen peroxide is the most common reagent both industrially and in academia, however peracids are also important. [6] More specialised oxidising agents can see niche use, for instance Caro's acid or mCPBA. Spontaneous or ...

  9. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    In mammals, this metabolic pathway is important in beta oxidation of fatty acids and catabolism of amino acids and choline, as it accepts electrons from multiple acetyl-CoA dehydrogenases. [32] [33] In plants, ETF-Q oxidoreductase is also important in the metabolic responses that allow survival in extended periods of darkness. [34]