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Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Procollagen-proline dioxygenase catalyzes the following reaction: L-proline + alpha-ketoglutaric acid + O 2 → (2S, 4R)-4-hydroxyproline + succinate + CO 2. The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: [3] In the first, a highly reactive Fe(IV)=O species is produced.
Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate".
In enzymology, a 4-hydroxyproline epimerase (EC 5.1.1.8) is an enzyme that catalyzes the chemical reaction trans -4-hydroxy-L-proline ⇌ {\displaystyle \rightleftharpoons } cis -4-hydroxy-D-proline Hence, this enzyme has one substrate , trans-4-hydroxy-L-proline , and one product , cis-4-hydroxy-D-proline .
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
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