Proline 3-hydroxylase
| Proline 3-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.28 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a proline 3-hydroxylase (EC 1.14.11.28) is an enzyme that catalyzes the chemical reaction
- L-proline + 2-oxoglutarate + O2 cis-3-hydroxy-L-proline + succinate + CO2
The 3 substrates of this enzyme are L-proline, 2-oxoglutarate, and O2, whereas its 3 products are cis-3-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 L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called P-3-H.
References
[edit]- Mori H, Shibasaki T, Uozaki Y, Ochiai K, Ozaki A (1996). "Detection of Novel Proline 3-Hydroxylase Activities in Streptomyces and Bacillus spp. by Regio- and Stereospecific Hydroxylation of l-Proline". Appl. Environ. Microbiol. 62 (6): 1903–1907. PMC 1388867. PMID 16535329.
- Mori H, Shibasaki T, Yano K, Ozaki A (1997). "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 (18): 5677–83. PMC 179453. PMID 9294421.
- Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ (2001). "Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases". Eur. J. Biochem. 268 (24): 6625–36. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.
