What does prolyl hydroxylase do to collagen?

What does prolyl hydroxylase do to collagen?

Collagen prolyl 4-hydroxylase (P4H) is an α2β2 tetrameric α-ketoglutarate (α-KG)-dependent dioxygenase that catalyzes 4-hydroxylation of proline to promote formation of the collagen triple helix, releasing succinate as a product3.

What is the significance of hydroxyproline residue in collagen proteins?

Hydroxyproline is a major component of the protein collagen, comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. They permit the sharp twisting of the collagen helix.

What is the difference between Proline and hydroxyproline?

Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom.

What does lysyl oxidase do?

Lysyl oxidase (LO) is a copper-dependent amine oxidase that plays a critical role in the biogenesis of connective tissue matrices by crosslinking the extracellular matrix proteins, collagen and elastin.

What is proline hydroxylation?

Proline hydroxylation is a common but still poorly understood protein modification (Gorres and Raines, 2010). The proline hydroxylation reaction is catalyzed by the 2-oxoglutarate- and oxygen-dependent dioxygenases PHD1, PHD2, and PHD3 (Semenza, 2001).

What is the substrate of prolyl hydroxylase?

HIF-α prolyl hydroxylase. The hydroxylation of proline residues is an enzymatic reaction using 2-oxoglutarate as a substrate in addition to HIF-1α or HIF-2α subunits and molecular oxygen. Three types of prolyl hydroxylase domains are known in humans, but in most cells, PHD2 is mainly involved.

What is the function of the hydroxylation acceptor proline in CMGC?

Mutation of the hydroxylation acceptor proline precludes tyrosine autophosphorylation and folding of DYRK1, resulting in a kinase unable to preserve VHL function and lacking glioma suppression activity. The consensus proline sequence is shared by most CMGC kinases, and prolyl hydroxylation is essential for catalytic activation.

Which enzyme hydroxylates the proline residues of the HIF-α subunit?

In particular, the enzyme that hydroxylates the proline residues of the HIF-α subunit is a dioxygenase or hydroxlase whose substrates are the HIF-α subunit, α-ketoglutarate (2-oxoglutarate: 2-OG), and molecular oxygen (O2); its cofactors are divalent iron (Fe2+) and ascorbic acid.