Procollagen-proline dioxygenase

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In enzymology, a procollagen-proline dioxygenase (EC 1.14.11.2) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1TJC.

[edit] References

IUBMB entry for 1.14.11.2
BRENDA references for 1.14.11.2 (Recommended.)
PubMed references for 1.14.11.2
PubMed Central references for 1.14.11.2
Google Scholar references for 1.14.11.2
Berg RA, Prockop DJ (1973). "Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme". J. Biol. Chem. 248: 1175–82. PMID 4346946.
Hutton JJ, Jr, Tappel AL and Udenfriend S (1967). "Cofactor and substrate requirements of collagen proline hydroxylase". Arch. Biochem. Biophys. 118: 231–240. doi:10.1016/0003-9861(67)90302-5.
Kivirikko KI, Kishida Y, Sakakibara S, Prockop DJ (1972). "Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase Effect of chain length, helical conformation and amino acid sequence in the substrate". Biochim. Biophys. Acta. 271: 347–56. PMID 5046811.
Kivirikko KI and Prockop DJ (1967). "Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollogen". Arch. Biochem. Biophys. 118: 611–618. doi:10.1016/0003-9861(67)90396-7.