Biosynthesis of food constituents: Amino acids. 3. Modified proteinogenic amino acids - a review

Jan Velíšek and Karel Cejpek
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Jan Velíšek: Department of Food Chemistry and Analysis, Faculty of Food and Biochemical Technology, Institute of Chemical Technology Prague, Prague, Czech Republic
Karel Cejpek: Department of Food Chemistry and Analysis, Faculty of Food and Biochemical Technology, Institute of Chemical Technology Prague, Prague, Czech Republic

Czech Journal of Food Sciences, 2006, vol. 24, issue 2, 59-61

Abstract: 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.

Keywords: biosynthesis; amino acids; cystine; hydroxyproline; hydroxylysine; methylhistidine; phosphoserine (search for similar items in EconPapers)
Date: 2006
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Persistent link: https://EconPapers.repec.org/RePEc:caa:jnlcjf:v:24:y:2006:i:2:id:3300-cjfs

DOI: 10.17221/3300-CJFS

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