New Nature Comms Paper

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The deazaflavin cofactor F420 is involved in a range of important redox reactions in bacteria and archaea. However, there are aspects of the F420 biosynthetic pathway that remain unclear. This work presents a revised biosynthetic pathway for F420, showing that phosphoenolpyruvate, rather than 2-phospho-L-lactate, is the key intermediate during the biosynthesis of F420. A range of techniques, including Mass Spec and X-ray crystallography were used to gain a better understanding of the enzymes and intermediates in this pathway.

Importantly, this information allowed us to heterologously express a functional F420 biosynthetic pathway in E. coli at levels comparable to native F420-producing organisms.

This collaborative piece of work was published in Nature Communications. Well done to James, Ghader and all those involved!

See it here. 

 

 

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