| Procollagen-proline dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Alpha subunits of procollagen-proline dioxygenase. Image shows substrate binding region (orange) and the binding groove of tyrosine residues (yellow) | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.11.2 | ||||||||
| CAS no. | 9028-06-2 | ||||||||
| 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 dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe2+, and ascorbate.[1][2] This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.[3]
- ^ Smith TG, Talbot NP (April 2010). "Prolyl hydroxylases and therapeutics". Antioxidants & Redox Signaling. 12 (4): 431–3. doi:10.1089/ars.2009.2901. PMID 19761407.
- ^ Hutton JJ, Trappel AL, Udenfriend S (July 1966). "Requirements for alpha-ketoglutarate, ferrous ion and ascorbate by collagen proline hydroxylase". Biochemical and Biophysical Research Communications. 24 (2): 179–84. doi:10.1016/0006-291x(66)90716-9. PMID 5965224.
- ^ Gorres KL, Raines RT (April 2010). "Prolyl 4-hydroxylase". Critical Reviews in Biochemistry and Molecular Biology. 45 (2): 106–24. doi:10.3109/10409231003627991. PMC 2841224. PMID 20199358.