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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
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
Substances
-
Escherichia coli Proteins
-
dihydrouracil
-
NAD
-
Uracil
-
Dihydrouracil Dehydrogenase (NADP)