Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate.
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.
Institut National de la Recherche Agronomique, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
Laure
L
Decamps
Benjamin
B
Philmus
Alhosna
A
Benjdia
Robert
R
White
Tadhg P
TP
Begley
Olivier
O
Berteau
D000192:Actinomycetales / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D017017:Methanococcus / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D046937:Nostoc / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D012258:Riboflavin Synthase / Q000737:chemistry / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism*
D014443:Tyrosine; C015084:coenzyme F420; D012436:S-Adenosylmethionine; D012258:Riboflavin Synthase; D012256:Riboflavin