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

L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)

L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2 [RN:R09572]

R09572

L-proline [CPD:C00148];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]

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].

EC 1.14.11.28 created 2006

1  [PMID:16535329]

Mori H, Shibasaki T, Uozaki Y, Ochiai K, 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.

2  [PMID:9294421]

Mori H, Shibasaki T, Yano K, 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) 5677-83.

[ag:BAA22406]

3  [PMID:11737217]

Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ.

Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.

Eur. J. Biochem. 268 (2001) 6625-36.