Biosynthesis of food constituents: Amino acids. 3. Modified proteinogenic amino acids - a review
2006
Jan Velíšek | Karel Cejpek
This review article gives a survey of principal pathways that lead to the biosynthesis of the modified principal proteinogenic amino acids, i.e. cystine, 4-hydroxyproline, 5-hydroxylysine, 3-methylhistidine, and O-phosphoserine. Except the proteinogenic amino acids, peptides and proteins often contain several unusual amino acids arising by specific modifications (e.g. oxidation or esterification) of amino acid residues present in the already synthesised polypeptide chain. The post-translational products include, e.g., the oxidation of the thiol groups of two cysteine residues to form a disulfide bridge (cystine), thus allowing cross-linking of polypeptide chains; the hydroxylation of proline to 4-hydroxyproline and of lysine to 5-hydroxylysine; N-methylation of histidine to 3-methylhistidine; and the phosphorylation of serine to O-phosphoserine. There also exist several other modified proteinogenic amino acids that are of minor significance to foods.
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