Procollagen-proline 3-dioxygenase
| Procollagen-proline 3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.7 | ||||||||
| CAS no. | 63551-75-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Procollagen-proline 3-dioxygenase (EC 1.14.11.7) is an enzyme that catalyzes the chemical reaction
The enzyme is a member of the alpha-ketoglutarate-dependent hydroxylase superfamily. It converts L-proline amino acids incorporated in a peptide, typically collagen, to trans-3-hydroxyproline equivalents.[1][2][3]
The enzyme is an oxidase with the systematic name procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include proline,2-oxoglutarate 3-dioxygenase, prolyl 3-hydroxylase, protocollagen proline 3-hydroxylase, and oxidoreductase, 3-hydroxylating.[1] It uses molecular oxygen as oxidant, with incorporation of one of its atoms. The enzyme is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4]
The mechanism 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. Ascorbic acid is also required to enhance the turnover number of the enzyme and its lack can cause scurvy because collagen biosynthesis is not complete.[5]
See also
- Procollagen-proline dioxygenase which acts in a similar way but gives 4-hydroxyproline as product
References
- ^ a b Enzyme 1.14.11.7 at KEGG Pathway Database.
- ^ Risteli J, Tryggvason K, Kivirikko KI (1977). "Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex". Eur. J. Biochem. 73 (2): 485–92. doi:10.1111/j.1432-1033.1977.tb11341.x. PMID 191255.
- ^ Risteli J, Tryggvason K, Kivirikko KI (1978). "A rapid assay for prolyl 3-hydroxylase activity". Anal. Biochem. 84 (2): 423–31. doi:10.1016/0003-2697(78)90060-X. PMID 204218.
- ^ 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.