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  2. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Amino acid biosynthesis overview. The drawn molecules are in their neutral forms and do not fully correspond to their presented names. Humans can not synthesize all of these amino acids. Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced.

  3. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    Methylation is the reversible addition of a methyl group onto an amino acid catalyzed by methyltransferase enzymes. Methylation occurs on at least 9 of the 20 common amino acids, however, it mainly occurs on the amino acids lysine and arginine. One example of a protein which is commonly methylated is a histone. Histones are proteins found in ...

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Surface-based chemical metabolism of amino acids and very small compounds may have led to the build-up of amino acids, coenzymes and phosphate-based small carbon molecules. [ 119 ] [ additional citation(s) needed ] Amino acids and similar building blocks could have been elaborated into proto- peptides , with peptides being considered key ...

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in ...

  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. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    This is important in the biosynthesis of amino acids, as for many of the pathways, intermediates from other biochemical pathways are converted to the α-keto acid skeleton, and then an amino group is added, often via transamination. The amino acids may then be linked together to form a protein. A similar process is used to break down proteins ...

  8. Aminoacyl tRNA synthetase - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

    The synthetase first binds ATP and the corresponding amino acid (or its precursor) to form an aminoacyl-adenylate, releasing inorganic pyrophosphate (PPi).The adenylate-aaRS complex then binds the appropriate tRNA molecule's D arm, and the amino acid is transferred from the aa-AMP to either the 2'- or the 3'-OH of the last tRNA nucleotide (A76) at the 3'-end.

  9. α-Aminoadipate pathway - Wikipedia

    en.wikipedia.org/wiki/Α-aminoadipate_pathway

    The amino acid L-lysine The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L - lysine . In the eukaryotes , this pathway is unique to several species of yeast , higher fungi (containing chitin in their cell walls), and the euglenids .