Hydroxyproline
From Wikipedia, the free encyclopedia
| Hydroxyproline | |
|---|---|
| Common name | hydroxyproline |
| Systematic name | 4-hydroxypyrrolidine- 2-carboxylic acid |
| Chemical formula | C5H9NO3 |
4-Hydroxyproline, or hydroxyproline (C5H9O3N), is an uncommon amino acid, abbreviated as HYP, e.g., in Protein Data Bank. Its IUPAC name is 4-hydroxypyrrolidine-2-carboxylic acid. Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the C (gamma) atom. Other hydroxyprolines also exist in nature, notably 2,3-cis 3,4-trans-dihydroxyproline, which occurs in diatom cell walls, and is postulated to have a role in silica deposition.
Hydroxyproline is produced by hydroxylation of the amino acid proline. It is not directly coded for by DNA, however, and is hydroxylated after protein synthesis.
Hydroxyproline is a major component of the protein collagen. It helps provide stability to the triple-helical structure of collagen by forming hydrogen bonds. Hydroxyproline is found in few proteins other than collagen.
Proline hydroxylation requires ascorbic acid. The most obvious, first effects (gum and hair problems) of absence of ascorbic acid in humans come from the resulting defect in hydroxylation of proline residues of collagen, with reduced stability of the collagen molecule causing scurvy.
