A revised biosynthetic pathway for the cofactor F420 in prokaryotes

Ghader Bashiri (), James Antoney, Ehab N. M. Jirgis, Mihir V. Shah, Blair Ney, Janine Copp, Stephanie M. Stuteley, Sreevalsan Sreebhavan, Brian Palmer, Martin Middleditch, Nobuhiko Tokuriki, Chris Greening, Colin Scott (), Edward N. Baker and Colin J. Jackson ()
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Ghader Bashiri: The University of Auckland
James Antoney: CSIRO Land and Water
Ehab N. M. Jirgis: The University of Auckland
Mihir V. Shah: CSIRO Land and Water
Blair Ney: CSIRO Land and Water
Janine Copp: University of British Columbia
Stephanie M. Stuteley: The University of Auckland
Sreevalsan Sreebhavan: The University of Auckland
Brian Palmer: The University of Auckland
Martin Middleditch: The University of Auckland
Nobuhiko Tokuriki: University of British Columbia
Chris Greening: CSIRO Land and Water
Colin Scott: CSIRO Land and Water
Edward N. Baker: The University of Auckland
Colin J. Jackson: CSIRO Land and Water

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Cofactor F420 plays critical roles in primary and secondary metabolism in a range of bacteria and archaea as a low-potential hydride transfer agent. It mediates a variety of important redox transformations involved in bacterial persistence, antibiotic biosynthesis, pro-drug activation and methanogenesis. However, the biosynthetic pathway for F420 has not been fully elucidated: neither the enzyme that generates the putative intermediate 2-phospho-l-lactate, nor the function of the FMN-binding C-terminal domain of the γ-glutamyl ligase (FbiB) in bacteria are known. Here we present the structure of the guanylyltransferase FbiD and show that, along with its archaeal homolog CofC, it accepts phosphoenolpyruvate, rather than 2-phospho-l-lactate, as the substrate, leading to the formation of the previously uncharacterized intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the γ-glutamyl ligase activity of the N-terminal domain. These new insights have allowed the heterologous production of F420 from a recombinant F420 biosynthetic pathway in Escherichia coli.

Date: 2019
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DOI: 10.1038/s41467-019-09534-x

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