Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 44, Pages 18173-18176Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja307762b
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Funding
- INRA, AlimH department
- Robert A. Welch Foundation [A-0034]
- National Science Foundation [MCB0722787]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1120346] Funding Source: National Science Foundation
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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.
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