Hydroxyproline
Hydroxyproline is an amino acid that plays key roles in collagen stability, protein folding, and cellular homeostasis. It is a non-essential amino acid, meaning it can be synthesized by the body.
Biochemistry[edit | edit source]
Hydroxyproline is produced from proline by the enzyme prolyl hydroxylase following protein synthesis. The hydroxylation reaction consumes oxygen and alpha-ketoglutarate and produces carbon dioxide and succinate as byproducts. This reaction is vitamin C-dependent, and lack of this vitamin can lead to reduced hydroxyproline levels and the disease scurvy.
Function[edit | edit source]
In collagen, hydroxyproline stabilizes the triple-helix structure by forming hydrogen bonds. It is critical for collagen stability and is overrepresented in collagen compared to other proteins. Hydroxyproline is also involved in cell-signaling pathways related to cellular homeostasis and stress response.
Clinical significance[edit | edit source]
Abnormal hydroxyproline metabolism can lead to a variety of diseases. For example, overproduction of hydroxyproline has been associated with fibrosis, while underproduction is associated with scurvy and Ehlers-Danlos syndrome. Measurement of hydroxyproline levels can be used as a marker for bone turnover and collagen degradation.
See also[edit | edit source]
Hydroxyproline Resources | ||
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