| EC |
1.14.11.28 |
| Accepted name: |
proline 3-hydroxylase |
| Reaction: |
L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2 |
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For diagram of reaction, click here |
| Other name(s): |
P-3-H |
| Systematic name: |
L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
| Comments: |
Requires iron(II) for activity. Unlike the proline hydroxylases involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)], this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme [2]. The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 162995-24-6 |
| References: |
| 1. |
Mori, H., Shibasaki, T., Uozaki, Y., Ochiai, K. and Ozaki, A. Detection of novel proline 3-hydroxylase activities in Streptomyces and Bacillus spp. by regio- and stereospecific hydroxylation of L-proline. Appl. Environ. Microbiol. 62 (1996) 1903–1907. [PMID: 16535329] |
| 2. |
Mori, H., Shibasaki, T., Yano, K. and Ozaki, A. Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline. J. Bacteriol. 179 (1997) 5677–5683. [DOI] [PMID: 9294421] |
| 3. |
Clifton, I.J., Hsueh, L.C., Baldwin, J.E., Harlos, K. and Schofield, C.J. Structure of proline 3-hydroxylase. Evolution of the family of
2-oxoglutarate dependent oxygenases. Eur. J. Biochem. 268 (2001) 6625–6636. [DOI] [PMID: 11737217] |
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| [EC 1.14.11.28 created 2006] |
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