Biology:Pyrimidine-deoxynucleoside 2'-dioxygenase
| pyrimidine-deoxynucleoside 2'-dioxygenase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.14.11.3 | ||||||||
| CAS number | 9076-89-5 | ||||||||
| 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 pyrimidine-deoxynucleoside 2'-dioxygenase (EC 1.14.11.3) is an enzyme that catalyzes the chemical reaction
- 2'-deoxyuridine + 2-oxoglutarate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] uridine + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxyuridine, 2-oxoglutarate, and O2, whereas its 3 products are uridine, 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 (2'-hydroxylating). Other names in common use include deoxyuridine 2'-dioxygenase, deoxyuridine 2'-hydroxylase, pyrimidine deoxyribonucleoside 2'-hydroxylase, thymidine 2'-dioxygenase, thymidine 2'-hydroxylase, thymidine 2-oxoglutarate dioxygenase, and thymidine dioxygenase. It has 2 cofactors: iron, and Ascorbate.
References
- "Thymidine 2'-hydroxylation in Neurospora crassa". J. Biol. Chem. 247 (19): 6128–34. 1972. PMID 4265566.
- Stubbe J (1985). "Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation". J. Biol. Chem. 260 (18): 9972–5. PMID 4040518.
- "Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis". J. Biol. Chem. 258 (17): 10551–7. 1983. PMID 6684117.
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