Pyrimidine-deoxynucleoside 1'-dioxygenase

Pyrimidine-deoxynucleoside 1'-dioxygenase
Identifiers
EC no.1.14.11.10
CAS no.98865-52-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

Pyrimidine-deoxynucleoside 1'-dioxygenase from Rhodotorula glutinis (EC 1.14.11.10) is an enzyme that catalyzes the chemical reaction

 
O2
CO2
 
 
 
2-deoxyribonolactone
+
 

The three substrates of this enzyme are deoxyuridine, 2-oxoglutaric acid, and oxygen. Its products are 2-deoxyribonolactone, uracil, succinic acid, and carbon dioxide.[1][2]

This enzyme is an alpha-ketoglutarate-dependent hydroxylase with systematic name 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating). It is also called deoxyuridine-uridine 1'-dioxygenase. It has 2 cofactors: iron, and ascorbic acid.

Pyrimidine-deoxynucleoside 2'-dioxygenase is a related enzyme which converts deoxyuridine to uridine instead of cleaving the uracil portion.[2]

References

  1. ^ Enzyme 1.14.11.10 at KEGG Pathway Database.
  2. ^ a b Stubbe, J. (1985). "Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation". Journal of Biological Chemistry. 260 (18): 9972–9975. doi:10.1016/S0021-9258(17)39197-4. PMID 4040518.