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Biosynthesis of the α chains of collagen
Author(s) -
Piez Karl A.
Publication year - 1970
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040760317
Subject(s) - hydroxylysine , aldehyde , hydroxylation , amino acid , chemistry , side chain , biosynthesis , biochemistry , stereochemistry , lysine , organic chemistry , catalysis , polymer , gene , enzyme
The α chains of collagen are synthesized like other proteins by the sequential addition of amino acids beginning at the amino‐terminal end and continuing for over 1000 amino acids. In addition to amino acid assembly, hydroxylation of certain prolyl and lysyl residues is required to complete the molecule. Approximately 4.8 minutes is necessary for the entire process. After extrusion from the cell, specific lysyl residues are oxidatively deaminated to the aldehyde allysine. An analogous conversion probably occurs with hydroxylysine. Cross‐linking results from the condensation of an aldehyde on one chain with an aldehyde or an ϵ‐amino group on another chain.