Procollagen-proline dioxygenase
（重定向自Prolyl hydroxylase）
![](/Images/godic/202502/04/Project_image_12547.png")
![A closer view of the substrate binding domain of prolyl hydroxylase. Tyrosine residues, which form the binding groove, are displayed in yellow.](/Images/godic/202502/04/Project_image_22547.png")
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as 2-oxoglutarate-dependent dioxygenases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires 2-oxoglutarate, Fe, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.