Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.3
Description:Pyrimidine-deoxynucleoside 2'-dioxygenase.
Alternative Name: Thymidine dioxygenase.
Thymidine 2-oxoglutarate dioxygenase.
Thymidine 2'-hydroxylase.
Thymidine 2'-dioxygenase.
Pyrimidine-deoxynucleoside,2-oxoglutarate 2'-dioxygenase.
Pyrimidine deoxyribonucleoside 2'-hydroxylase.
Deoxyuridine 2'-hydroxylase.
Deoxyuridine 2'-dioxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.3
BRENDA Enzyme Link: BRENDA 1.14.11.3
KEGG Enzyme Link: KEGG1.14.11.3
BioCyc Enzyme Link: BioCyc 1.14.11.3
ExPASy Enzyme Link: ExPASy1.14.11.3
EC2PDB Enzyme Link: EC2PDB 1.14.11.3
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.3
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.3
IntEnz Enzyme Link: IntEnz 1.14.11.3
MEDLINE Enzyme Link: MEDLINE 1.14.11.3
MSA:

1.14.11.3;

Phylogenetic Tree:

1.14.11.3;

Uniprot:
M-CSA:
RHEA:21076 2'-deoxyuridine + 2-oxoglutarate + O2 = CO2 + succinate + uridine
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis.Warn-Cramer BJ, Macrander LA, Abbott MT1983 Sep 106684117
Thymidine 2'-hydroxylation in Neurospora crassa.Bankel L, Lindstedt G, Lindstedt S1972 Oct 104265566
Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation.Stubbe J1985 Aug 254040518