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  2. 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).

  3. Transaminase - Wikipedia

    en.wikipedia.org/wiki/Transaminase

    Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for oxaloacetate or alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to aspartate and glutamate for conversion to urea for excretion of nitrogen.

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. 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 ...

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The incorporation of these nonstandard amino acids is rare. For example, 25 human proteins include selenocysteine in their primary structure, [64] and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic moiety in their active sites. [65] Pyrrolysine and selenocysteine are encoded via variant codons.

  6. Branched-chain amino acid aminotransferase - Wikipedia

    en.wikipedia.org/wiki/Branched-chain_amino_acid...

    This reaction regulates metabolism of amino acids and is a crucial step in nitrogen shuttling throughout the whole body. [14] Branched-chain amino acids (BCAA) are ubiquitous in many organisms, comprising 35% of all proteins and 40% of the amino acids required in all mammals. [13]

  7. Stable isotope composition of amino acids - Wikipedia

    en.wikipedia.org/wiki/Stable_isotope_composition...

    Repeated transamination by consumers results in a predictable increase in the abundance of 15 N as amino acids are transferred up food chains. [4] Together, these application, among others in ecology, demonstrate the utility of stable isotopes as tracers of environmental processes that are difficult to measure directly.

  8. Biogenic amine - Wikipedia

    en.wikipedia.org/wiki/Biogenic_amine

    They are basic nitrogenous compounds formed mainly by decarboxylation of amino acids or by amination and transamination of aldehydes and ketones. Biogenic amines are organic bases with low molecular weight and are synthesized by microbial, vegetable and animal metabolisms. In food and beverages they are formed by the enzymes of raw material or ...

  9. Serine hydroxymethyltransferase - Wikipedia

    en.wikipedia.org/wiki/Serine_hydroxymethyl...

    The mechanism commonly ascribed to SHMT enzymatic activity is a transamidation followed by a cleavage of amino acid side chain from the backbone. [7] The N-terminal amine of serine makes a nucleophilic attack on the aldimine between the SHMT lysine (Internal Aldimine) and the PLP aldehyde to form a gem-diamine, and then the N-terminal amine lone pair comes down to displace the lysine, forming ...