Procollagen-proline dioxygenase
| 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 | ||||||||
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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. 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.