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Escherichia Coli Dihydropyrimidine Dehydrogenase is a Novel NAD-dependent Heterotetramer Essential for the Production of 5,6-dihydrouracil

Overview
Journal J Bacteriol
Specialty Microbiology
Date 2010 Dec 21
PMID 21169495
Citations 16
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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.

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