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  2. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum. Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4 ...

  3. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Similar functionality is also presented in serine and threonine, whose side chains have a hydroxy group, but are alcohols. Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, that is greater than the negative charge of the only negatively charged aspartic and glutamic acids ...

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life. [3] [4]

  5. Secondary amino acid - Wikipedia

    en.wikipedia.org/wiki/Secondary_amino_acid

    Secondary amino acids can be classified to cyclic acids, such as proline, and acyclic N-substituted amino acids. [1] [2] In nature, proline, hydroxyproline, pipecolic acid and sarcosine are well-known secondary amino acids. Proline is the only proteinogenic secondary amino acids. Other secondary amino acids are non-proteinogenic amino acids. In ...

  6. 4-Hydroxyphenylglycine - Wikipedia

    en.wikipedia.org/wiki/4-Hydroxyphenylglycine

    4-Hydroxyphenylglycine (HPG) is a non-proteogenic amino acid found in vancomycin and related glycopeptides. HPG is synthesized from the shikimic acid pathway and requires four enzymes to synthesize: [1] Both L- and D-HPG are used in the vancomycin class of antibiotics.

  7. Threonine - Wikipedia

    en.wikipedia.org/wiki/Threonine

    Threonine was the last of the 20 common proteinogenic amino acids to be discovered. It was discovered in 1935 by William Cumming Rose, [7] collaborating with Curtis Meyer. The amino acid was named threonine because it was similar in structure to threonic acid, a four-carbon monosaccharide with molecular formula C 4 H 8 O 5 [8]

  8. Hydroxy group - Wikipedia

    en.wikipedia.org/wiki/Hydroxy_group

    The hydroxy group is pervasive in chemistry and biochemistry. Many inorganic compounds contain hydroxyl groups, including sulfuric acid, the chemical compound produced on the largest scale industrially. [2] Hydroxy groups participate in the dehydration reactions that link simple biological molecules into long chains.

  9. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...