RRC ID 35427
Author Hidese R, Mihara H, Kurihara T, Esaki N.
Title Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.
Journal J Bacteriol
Abstract The reductive pyrimidine catabolic pathway is absent in Escherichia coli. However, the bacterium contains an enzyme homologous to mammalian dihydropyrimidine dehydrogenase. Here, we show that E. coli dihydropyrimidine dehydrogenase is the first member of a novel NADH-dependent subclass of iron-sulfur flavoenzymes catalyzing the conversion of uracil to 5,6-dihydrouracil in vivo.
Volume 193(4)
Pages 989-93
Published 2011-2-1
DOI 10.1128/JB.01178-10
PII JB.01178-10
PMID 21169495
PMC PMC3028684
MeSH Dihydrouracil Dehydrogenase (NADP) / chemistry Dihydrouracil Dehydrogenase (NADP) / genetics Dihydrouracil Dehydrogenase (NADP) / metabolism* Dimerization Escherichia coli / chemistry Escherichia coli / classification Escherichia coli / enzymology Escherichia coli / metabolism Escherichia coli Proteins / chemistry Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Kinetics Molecular Sequence Data NAD / metabolism* Phylogeny Uracil / analogs & derivatives* Uracil / metabolism
IF 3.006
Times Cited 17
Prokaryotes E. coli ME7985(W3110) JW2133(Keio)(ASKA)?