| Entry |
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| Name |
procollagen-proline 4-dioxygenase;
P4HA (gene name);
P4HB (gene name);
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;
procollagen-proline 4-dioxygenase (ambiguous)
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| Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
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| Sysname |
procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
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| Reaction(IUBMB) |
procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN: R03219]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
procollagen trans-4-hydroxy-L-proline [CPD: C04398];
succinate [CPD: C00042];
CO2 [CPD: C00011]
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| Comment |
Requires Fe2+ and ascorbate.The enzyme, which is located within the lumen of the endoplasmic reticulum, catalyses the 4-hydroxylation of prolines in -X-Pro-Gly- sequences. The 4-hydroxyproline residues are essential for the formation of the collagen triple helix. The enzyme forms a complex with protein disulfide isomerase and acts not only on procollagen but also on more than 15 other proteins that have collagen-like domains.
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| History |
EC 1.14.11.2 created 1972, modified 1981, modified 1983, modified 2017
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| Pathway |
| ec00330 | Arginine and proline metabolism |
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| Orthology |
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| Genes |
» show all
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| Reference |
1 |
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| Authors |
Hutton, J.J., Jr., Tappel, A.L. and Udenfriend, S. |
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| Title |
Cofactor and substrate requirements of collagen proline hydroxylase. |
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| Journal |
Arch. Biochem. Biophys. 118 (1967) 231-240. |
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| Reference |
2 |
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| Authors |
Kivirikko, K.I. and Prockop, D.J. |
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| Title |
Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollogen. |
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| Journal |
Arch. Biochem. Biophys. 118 (1967) 611-618. |
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| Reference |
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| Authors |
Kivirikko KI, Kishida Y, Sakakibara S, Prockop DJ. |
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| Title |
Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase. Effect of chain length, helical conformation and amino acid sequence in the substrate. |
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| Journal |
Biochim. Biophys. Acta. 271 (1972) 347-56. |
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| Reference |
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| Authors |
Berg RA, Prockop DJ. |
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| Title |
Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme. |
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| Journal |
J. Biol. Chem. 248 (1973) 1175-82. |
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| Reference |
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| Authors |
John DC, Bulleid NJ |
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| Title |
Prolyl 4-hydroxylase: defective assembly of alpha-subunit mutants indicates that assembled alpha-subunits are intramolecularly disulfide bonded. |
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| Journal |
Biochemistry. 33 (1994) 14018-25. |
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| Reference |
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| Authors |
Lamberg A, Pihlajaniemi T, Kivirikko KI |
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| Title |
Site-directed mutagenesis of the alpha subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity. |
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| Journal |
J. Biol. Chem. 270 (1995) 9926-31. |
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| Reference |
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| Authors |
Myllyharju J, Kivirikko KI |
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| Title |
Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. |
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| Journal |
EMBO. J. 16 (1997) 1173-80. |
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| Reference |
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| Authors |
Kivirikko KI, Myllyharju J |
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| Title |
Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. |
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| Journal |
Matrix. Biol. 16 (1998) 357-68. |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 1.14.11.2 |
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