| EC |
1.14.11.7 |
| Accepted name: |
procollagen-proline 3-dioxygenase |
| Reaction: |
[procollagen]-L-proline + 2-oxoglutarate + O2 = [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2 |
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For diagram of reaction, click here |
| Other name(s): |
proline,2-oxoglutarate 3-dioxygenase; prolyl 3-hydroxylase; protocollagen proline 3-hydroxylase; prolyl-4-hydroxyprolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase, 3-hydroxylating |
| Systematic name: |
[procollagen]-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
| Comments: |
Requires Fe2+ and ascorbate. The enzyme forms a complex with protein disulfide isomerase, and is located in the endoplasmic reticulum. It modifies proline residues within the procollagen peptide of certain collagen types. The modification is essential for proper collagen triple helix formation. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 63551-75-7 |
| References: |
| 1. |
Risteli, J., Tryggvason, K. and Kivirikko, K.I. Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex. Eur. J. Biochem. 73 (1977) 485–492. [DOI] [PMID: 191255] |
| 2. |
Risteli, J., Tryggvason, K. and Kivirikko, K.I. A rapid assay for prolyl 3-hydroxylase activity. Anal. Biochem. 84 (1978) 423–431. [DOI] [PMID: 204218] |
| 3. |
Vranka, J.A., Sakai, L.Y. and Bachinger, H.P. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 279 (2004) 23615–23621. [DOI] [PMID: 15044469] |
| 4. |
Tiainen, P., Pasanen, A., Sormunen, R. and Myllyharju, J. Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV. J. Biol. Chem. 283 (2008) 19432–19439. [DOI] [PMID: 18487197] |
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| [EC 1.14.11.7 created 1981, modified 1983, modified 2017] |
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