Thymine dioxygenase
| thymine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.6 | ||||||||
| CAS no. | 37256-67-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction
- thymine + 2-oxoglutarate + O2 5-hydroxymethyluracil + succinate + CO2
The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, 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 thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase. It has 2 cofactors: iron, and Ascorbate.
References
- Bankel L, Holme E, Lindstedt G, Lindstedt S (1972). "Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa". FEBS Lett. 21 (2): 135–138. doi:10.1016/0014-5793(72)80121-2. PMID 11946494.
- Liu CK, Hsu CA, Abbott MT (1973). "Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase". Arch. Biochem. Biophys. 159 (1): 180–7. doi:10.1016/0003-9861(73)90443-8. PMID 4274083.
- Warn-Cramer BJ, Macrander LA, Abbott MT (1983). "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. PMID 6684117.
