EC 1.14.11.3 - Pyrimidine-deoxynucleoside 2'-dioxygenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.14.11.3

Names

Accepted name:
pyrimidine-deoxynucleoside 2'-dioxygenase
Other names:
deoxyuridine 2'-dioxygenase
deoxyuridine 2'-hydroxylase
pyrimidine deoxyribonucleoside 2'-hydroxylase
thymidine 2'-dioxygenase
thymidine 2'-hydroxylase
thymidine 2-oxoglutarate dioxygenase
thymidine dioxygenase
pyrimidine-deoxynucleoside,2-oxoglutarate 2'-dioxygenase
Systematic name:
2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2'-hydroxylating)

Reaction

Cofactors

Comments:

Requires Fe(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1'-dioxygenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047080
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: 6128-6134 (1972). [PMID: 4265566]
  2. Stubbe, J.
    Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation.
    J. Biol. Chem. 260: 9972-9975 (1985). [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: 10551-10557 (1983). [PMID: 6684117]

[EC 1.14.11.3 created 1972, modified 1976, modified 1989, modified 2002]