Biology:Procollagen-proline 3-dioxygenase
| procollagen-proline 3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.7 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a procollagen-proline 3-dioxygenase (EC 1.14.11.7) is an enzyme that catalyzes the chemical reaction
- procollagen L-proline + 2-oxoglutarate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] procollagen trans-3-hydroxy-L-proline + succinate + CO2
The enzyme is a member of the alpha-ketoglutarate-dependent hydroxylases superfamily. The 3 substrates of this enzyme are procollagen L-proline, 2-oxoglutarate, and O2, whereas its 3 products are procollagen trans-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 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, prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen, and oxidoreductase, 3-hydroxylating. It has 2 cofactors: iron, and Ascorbate.
References
- "Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex". Eur. J. Biochem. 73 (2): 485–92. 1977. doi:10.1111/j.1432-1033.1977.tb11341.x. PMID 191255.
- "A rapid assay for prolyl 3-hydroxylase activity". Anal. Biochem. 84 (2): 423–31. 1978. doi:10.1016/0003-2697(78)90060-X. PMID 204218.
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