Biosynthesis of F0, Precursor of the F420 Cofactor, Requires a Unique Two Radical-SAM Domain Enzyme and Tyrosine as Substrate

• DOI: 10.1021/ja307762b
• Publication Date: 2012-10-16T15:12:07Z
• Authors: Laure Decamps; Benjamin Philmus; Alhosna Benjdia; Robert White; Tadhg P. Begley; Olivier Berteau
• Keywords: [SDV.SA]Life Sciences [q-bio]/Agricultural sciences; 0301 basic medicine; S-Adenosylmethionine; 572; IDENTIFICATION; SULFATASE-MATURATING ENZYMES; Methanococcus; Riboflavin; SUPERFAMILY; COENZYME F-420; RIBOFLAVIN; NO; Protein Structure, Tertiary; Riboflavin Synthase; 03 medical and health sciences; 8-DIDEMETHYL-8-HYDROXY-5-DEAZARIBOFLAVIN; ESCHERICHIA-COLI; Actinomycetales; Tyrosine; MYCOBACTERIUM-TUBERCULOSIS; Nostoc; MOAA

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, unique manner, involves enzyme, F(0)-synthase. This enzyme is large monomer actinobacteria, while it constituted two subunits cyanobacteria. We report here purification both types F(0)-synthase their vitro activities. Our study allows us establish that F(0)-synthase, from types, uses 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione tyrosine as substrates but not 4-hydroxylphenylpyruvate previously suggested. Furthermore, our data support fact generates 5'-deoxyadenosyl radicals catalysis which unprecedented reaction catalyzed by radical SAM enzymes.