In enzymology, a pyrimidine-deoxynucleoside 1'-dioxygenase (EC 1.14.11.10) is an enzyme that catalyzes the chemical reaction
pyrimidine-deoxynucleoside 1'-dioxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.11.10 | ||||||||
CAS no. | 98865-52-2 | ||||||||
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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- 2'-deoxyuridine + 2-oxoglutarate + O2 uracil + 2-deoxyribonolactone + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxyuridine, 2-oxoglutarate, and O2, whereas its 4 products are uracil, 2-deoxyribonolactone, 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 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating). This enzyme is also called deoxyuridine-uridine 1'-dioxygenase. It has 2 cofactors: iron, and Ascorbate.
References
edit- Stubbe J (August 1985). "Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation". The Journal of Biological Chemistry. 260 (18): 9972–5. PMID 4040518.