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- W1489452981 abstract "A nitroreductase enzyme has been isolated from Escherichia coli B. This enzyme is an FMN-containing flavoprotein with a molecular mass of 24 kDa and requires either NADH or NADPH as a cofactor. Partial protein sequence analysis showed extensive homology with the “classical nitroreductase” of Salmonella typhimurium and a nitroreductase induced in Enterobacter cloacae. In common with the Salmonella enzyme, the E. coli B enzyme is capable of reducing nitrofurazone. The E. coli nitroreductase is also capable of reducing the anti-tumour agent CB1954 [5-(aziridin-1-yl)-2,4-dinitrobenzamide], a property shared with the mammalian enzyme DT diaphorase [NAD(P)H dehydrogenase (quinone)] as isolated species. Both enzymes also share the properties of being able to reduce quinones and are both inhibited by dicoumarol. The nitroreductase is a more active against CB1954 (kcat=360 min−) han Walker DT diaphorase (Kcat = 4 min−1) and also has a lower Km for NADH (6 vs 75 μM)." @default.
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- W1489452981 date "1992-12-01" @default.
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- W1489452981 title "The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)—I" @default.
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- W1489452981 doi "https://doi.org/10.1016/0006-2952(92)90671-5" @default.
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