KEGG   ENZYME: 1.14.11.3
Entry
EC 1.14.11.3                Enzyme                                 
Name
pyrimidine-deoxynucleoside 2'-dioxygenase;
deoxyuridine 2'-dioxygenase;
deoxyuridine 2'-hydroxylase;
pyrimidine deoxyribonucleoside 2'-hydroxylase;
thymidine 2'-dioxygenase;
thymidine 2'-hydroxylase;
thymidine 2-oxoglutarate dioxygenase;
thymidine dioxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Sysname
2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2'-hydroxylating)
Reaction(IUBMB)
2'-deoxyuridine + 2-oxoglutarate + O2 = uridine + succinate + CO2 [RN:R01879]
Reaction(KEGG)
R01879
Substrate
2'-deoxyuridine [CPD:C00526];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
uridine [CPD:C00299];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires iron(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1'-dioxygenase.
History
EC 1.14.11.3 created 1972, modified 1976, modified 1989, modified 2002
Reference
1  [PMID:4265566]
  Authors
Bankel L, Lindstedt G, Lindstedt S.
  Title
Thymidine 2'-hydroxylation in Neurospora crassa.
  Journal
J Biol Chem 247:6128-34 (1972)
Reference
2  [PMID:4040518]
  Authors
Stubbe J.
  Title
Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation.
  Journal
J Biol Chem 260:9972-5 (1985)
Reference
3  [PMID:6684117]
  Authors
Warn-Cramer BJ, Macrander LA, Abbott MT.
  Title
Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis.
  Journal
J Biol Chem 258:10551-7 (1983)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.3
IUBMB Enzyme Nomenclature: 1.14.11.3
ExPASy - ENZYME nomenclature database: 1.14.11.3
BRENDA, the Enzyme Database: 1.14.11.3
CAS: 9076-89-5
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