Pyrimidine-deoxynucleoside 2'-dioxygenase
| Pyrimidine-deoxynucleoside 2'-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.3 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
Pyrimidine-deoxynucleoside 2'-dioxygenase (EC 1.14.11.3) is an enzyme that catalyzes the chemical reaction
The enzyme converts deoxyuridine to uridine by oxidation using molecular oxygen.[1][2]
This enzyme is an oxidoreductase with systematic name 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.[3] It is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4]
The mechanism used by these 2-oxoglutarate-dependent oxygenases requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed. Ascorbic acid enhances the turnover number of the enzyme by reducing any iron converted to Fe(III) back to the required Fe(II).[5][6]
References
- ^ Bankel L, Lindstedt G, Lindstedt S (1972). "Thymidine 2'-hydroxylation in Neurospora crassa". J. Biol. Chem. 247 (19): 6128–34. doi:10.1016/S0021-9258(19)44773-X. 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. doi:10.1016/S0021-9258(17)39197-4. PMID 4040518.
- ^ Enzyme 1.14.11.3 at KEGG Pathway Database.
- ^ Mbenza, Naasson M.; Vadakkedath, Praveen G.; McGillivray, Duncan J.; Leung, Ivanhoe K.H. (2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". Journal of Inorganic Biochemistry. 177: 384–394. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ^ 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. doi:10.1016/S0021-9258(17)44491-7. PMID 6684117.
- ^ Clifton, Ian J.; Hsueh, Li-Ching; Baldwin, Jack E.; Harlos, Karl; Schofield, Christopher J. (2001). "Structure of proline 3-hydroxylase". European Journal of Biochemistry. 268 (24): 6625–6636. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.