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 | ||||||||
| |||||||||
Proline 3-hydroxylase (EC 1.14.11.28) is an enzyme that catalyzes the chemical reaction:[1][2]
The systematic name of this enzyme class is L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called P-3-H.[3] It is an oxidase which uses molecular oxygen as oxidant, with incorporation of one of its atoms. These enzymes are non-heme iron proteins with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4]
The mechanism used by these 2-oxoglutarate-dependent oxygenases requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed.[5]
References
- ^ 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. Bibcode:1996ApEnM..62.1903M. doi:10.1128/aem.62.6.1903-1907.1996. 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. doi:10.1128/jb.179.18.5677-5683.1997. PMC 179453. PMID 9294421.
- ^ Enzyme 1.14.11.28 at KEGG Pathway Database.
- ^ Mbenza NM, Vadakkedath PG, McGillivray DJ, Leung IK (December 2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". J. Inorg. Biochem. 177: 384–394. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ^ 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.