Escherichia coli Dihydropyrimidine Dehydrogenase Is a Novel NAD-Dependent Heterotetramer Essential for the Production of 5,6-Dihydrouracil
Escherichia coli Dihydropyrimidine Dehydrogenase Is a Novel NAD-Dependent Heterotetramer Essential for the Production of 5,6-Dihydrouracil
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DOI：
10.1128/jb.01178-10
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发表时间：
2011-02-01
影响因子：
3.2
通讯作者：
Esaki, Nobuyoshi
中科院分区：
文献类型：
--
作者：
Hidese, Ryota;Mihara, Hisaaki;Esaki, Nobuyoshi
还原嘧啶分解代谢途径在大肠杆菌中不存在。然而，该细菌含有与哺乳动物二氢嘧啶脱氢酶同源的酶。在这里，我们表明，E。大肠杆菌二氢嘧啶脱氢酶是铁硫黄素酶的一个新的NADH依赖性亚类的第一个成员，催化尿嘧啶在体内转化为5，6-二氢尿嘧啶。
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.