The Enzyme Database

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EC 1.14.11.3     
Accepted name: pyrimidine-deoxynucleoside 2′-dioxygenase
Reaction: 2′-deoxyuridine + 2-oxoglutarate + O2 = uridine + succinate + CO2
Other name(s): deoxyuridine 2′-dioxygenase; deoxyuridine 2′-hydroxylase; pyrimidine deoxyribonucleoside 2′-hydroxylase; thymidine 2′-dioxygenase; thymidine 2′-hydroxylase; thymidine 2-oxoglutarate dioxygenase; thymidine dioxygenase
Systematic name: 2′-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2′-hydroxylating)
Comments: Requires Fe(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1′-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-89-5
References:
1.  Bankel, L., Lindstedt, G. and Lindstedt, S. Thymidine 2′-hydroxylation in Neurospora crassa. J. Biol. Chem. 247 (1972) 6128–6134. [PMID: 4265566]
2.  Stubbe, J. Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. J. Biol. Chem. 260 (1985) 9972–9975. [PMID: 4040518]
3.  Warn-Cramer, B.J., Macrander, L.A. and Abbott, M.T. Markedly different ascorbate dependencies of the sequential α-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis. J. Biol. Chem. 258 (1983) 10551–10557. [PMID: 6684117]
[EC 1.14.11.3 created 1972, modified 1976, modified 1989, modified 2002]
 
 


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