+ 2-oxoglutaric
acid
Pyrimidine-deoxynucleoside 1'-dioxygenase
| Pyrimidine-deoxynucleoside 1'-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.10 | ||||||||
| CAS no. | 98865-52-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Pyrimidine-deoxynucleoside 1'-dioxygenase from Rhodotorula glutinis (EC 1.14.11.10) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are deoxyuridine, 2-oxoglutaric acid, and oxygen. Its products are 2-deoxyribonolactone, uracil, succinic acid, and carbon dioxide.[1][2]
This enzyme is an alpha-ketoglutarate-dependent hydroxylase with systematic name 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating). It is also called deoxyuridine-uridine 1'-dioxygenase. It has 2 cofactors: iron, and ascorbic acid.
Pyrimidine-deoxynucleoside 2'-dioxygenase is a related enzyme which converts deoxyuridine to uridine instead of cleaving the uracil portion.[2]
References
- ↑ Enzyme 1.14.11.10 at KEGG Pathway Database.
- 1 2 Stubbe, J. (1985). "Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation". Journal of Biological Chemistry. 260 (18): 9972–9975. doi:10.1016/S0021-9258(17)39197-4. PMID 4040518.