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• W2318521608 startingPage "18173" @default.
• W2318521608 abstract "Cofactors play key roles in metabolic pathways. Among them F(420) has proved to be a very attractive target for the selective inhibition of archaea and actinobacteria. Its biosynthesis, in a unique manner, involves a key enzyme, F(0)-synthase. This enzyme is a large monomer in actinobacteria, while it is constituted of two subunits in archaea and cyanobacteria. We report here the purification of both types of F(0)-synthase and their in vitro activities. Our study allows us to establish that F(0)-synthase, from both types, uses 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and tyrosine as substrates but not 4-hydroxylphenylpyruvate as previously suggested. Furthermore, our data support the fact that F(0)-synthase generates two 5'-deoxyadenosyl radicals for catalysis which is unprecedented in reaction catalyzed by radical SAM enzymes." @default.
• W2318521608 created "2016-06-24" @default.
• W2318521608 creator A5046873300 @default.
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• W2318521608 date "2012-10-24" @default.
• W2318521608 modified "2023-10-18" @default.
• W2318521608 title "Biosynthesis of F₀, Precursor of the F₄₂₀ Cofactor, Requires a Unique Two Radical-SAM Domain Enzyme and Tyrosine as Substrate" @default.
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• W2318521608 doi "https://doi.org/10.1021/ja307762b" @default.
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• W2318521608 hasPublicationYear "2012" @default.
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