The role of ascorbic acid in the hydroxylation of peptide-bound proline
1979
Experiments using the enzyme prolyl hydroxylase of high purity help to explain the role of ascorbic acid in the conversion of peptide-bound proline to hydroxyproline and other hydroxylation reactions. Prolyl hydroxylase, in the presence of O(sub2) ferrous iron, alpha-ketoglutarate and polypeptide, changes peptide-bound proline to hydroxyproline. At the same time alpha-ketoglutarate is oxidized to succinate and carbon dioxide. Ascorbate does not participate in the hydroxylation reaction, but is specifically required to keep enzyme-bound iron in the reduced form.
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