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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Nonstandard amino acids are usually formed through modifications to standard amino acids. For example, homocysteine is formed through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosylmethionine, [114] while hydroxyproline is made by a post translational modification of proline. [115]

  3. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids ...

  4. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    Some amino acids have functions by themselves or in a modified form; for instance, glutamate functions as an important neurotransmitter. Amino acids can be joined via a peptide bond . In this dehydration synthesis, a water molecule is removed and the peptide bond connects the nitrogen of one amino acid's amino group to the carbon of the other's ...

  5. List of amino acids - Wikipedia

    en.wikipedia.org/wiki/List_of_amino_acids

    Amino acids are listed by type: Proteinogenic amino acid; Non-proteinogenic amino acids This page was last edited on 5 January 2020, at 17:16 (UTC). Text is ...

  6. Hypothetical types of biochemistry - Wikipedia

    en.wikipedia.org/wiki/Hypothetical_types_of...

    In known Earth-based life, amino acids are almost universally of the L form and sugars are of the D form. Molecules using D amino acids or L sugars may be possible; molecules of such a chirality, however, would be incompatible with organisms using the opposing chirality molecules. Amino acids whose chirality is opposite to the norm are found on ...

  7. 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).

  8. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Modified amino acids are sometimes observed in proteins; this is usually the result of enzymatic modification after translation (protein synthesis). For example, phosphorylation of serine by kinases and dephosphorylation by phosphatases is an important control mechanism in the cell cycle .

  9. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    The essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine (i.e. H, I, L, K, M, F, T, W, V). [3] The proteinogenic amino acids have been found to be related to the set of amino acids that can be recognized by ribozyme autoaminoacylation systems. [4]