期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-09534-x
关键词
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资金
- NHMRC New Investigator Grant [1142699]
- ARC DECRA Fellowship [DE170100310]
- Health Research Council of New Zealand
- Australian Research Council
- National Health and Medical Research Council
- New Zealand Synchrotron Group Ltd.
- Sir Charles Hercus Fellowship
- AGRTP Scholarship
- Australian Research Council [DE170100310] Funding Source: Australian Research Council
- National Health and Medical Research Council of Australia [1142699] Funding Source: NHMRC
Cofactor F-420 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 F-420 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 gamma-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-F-420 -0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F-420-0, which produces mature F-420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. These new insights have allowed the heterologous production of F-420 from a recombinant F-420 biosynthetic pathway in Escherichia coli.
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