Procollagen-proline dioxygenase

In enzymology, a procollagen-proline dioxygenase is an enzyme that catalyzes the chemical reaction


 * procollagen L-proline + 2-oxoglutarate + O2 $$\rightleftharpoons$$ procollagen trans-4-hydroxy-L-proline + succinate + CO2

The 3 substrates of this enzyme are procollagen L-proline, 2-oxoglutarate, and O2, whereas its 3 products are procollagen trans-4-hydroxy-L-proline, succinate, and CO2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating). Other names in common use include protocollagen hydroxylase, proline hydroxylase, proline,2-oxoglutarate 4-dioxygenase, collagen proline hydroxylase, hydroxylase, collagen proline, peptidyl proline hydroxylase, proline protocollagen hydroxylase, proline, 2-oxoglutarate dioxygenase, prolyl hydroxylase, prolylprotocollagen dioxygenase, prolylprotocollagen hydroxylase, protocollagen proline 4-hydroxylase, protocollagen proline dioxygenase, protocollagen proline hydroxylase, protocollagen prolyl hydroxylase, prolyl 4-hydroxylase, prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase,, 4-hydroxylating, and procollagen-proline 4-dioxygenase. This enzyme participates in arginine and proline metabolism. It has 2 cofactors: iron, and Ascorbate.

Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code.