KEGG   ENZYME: 1.14.11.49Help
Entry
EC 1.14.11.49               Enzyme                                 

Name
uridine-5'-phosphate dioxygenase;
lipL (gene name)
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
BRITE hierarchy
Sysname
UMP,2-oxoglutarate:oxygen oxidoreductase
Reaction(IUBMB)
UMP + 2-oxoglutarate + O2 = 5'-dehydrouridine + succinate + CO2 + phosphate [RN:R11053]
Reaction(KEGG)
Substrate
UMP [CPD:C00105];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
5'-dehydrouridine [CPD:C21079];
succinate [CPD:C00042];
CO2 [CPD:C00011];
phosphate [CPD:C00009]
Comment
The enzyme catalyses a net dephosphorylation and oxidation of UMP to generate 5'-dehydrouridine, the first intermediate in the biosynthesis of the unusual aminoribosyl moiety found in several C7-furanosyl nucleosides such as A-90289s, caprazamycins, liposidomycins, muraymycins and FR-900453. Requires Fe2+.
History
EC 1.14.11.49 created 2015
Reference
1  [PMID:21216959]
  Authors
Yang Z, Chi X, Funabashi M, Baba S, Nonaka K, Pahari P, Unrine J, Jacobsen JM, Elliott GI, Rohr J, Van Lanen SG
  Title
Characterization of LipL as a non-heme, Fe(II)-dependent alpha-ketoglutarate:UMP  dioxygenase that generates uridine-5'-aldehyde during A-90289 biosynthesis.
  Journal
J Biol Chem 286:7885-92 (2011)
DOI:10.1074/jbc.M110.203562
Reference
2  [PMID:23034228]
  Authors
Yang Z, Unrine J, Nonaka K, Van Lanen SG
  Title
Fe(II)-dependent, uridine-5'-monophosphate alpha-ketoglutarate dioxygenases in the synthesis of 5'-modified nucleosides.
  Journal
Methods Enzymol 516:153-68 (2012)
DOI:10.1016/B978-0-12-394291-3.00031-9
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.49
IUBMB Enzyme Nomenclature: 1.14.11.49
ExPASy - ENZYME nomenclature database: 1.14.11.49
BRENDA, the Enzyme Database: 1.14.11.49

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