Journal
CHEMBIOCHEM
Volume 21, Issue 13, Pages 1856-1860Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000051
Keywords
Escherichia coli; fluoride channels; fluorinases; halogenations; SAM transporters
Funding
- Industrial Biotechnology Innovation Centre (IBioIC)
- GlaxoSmithKline
- EU Horizon 2020 (Sinfonia consortia)
Ask authors/readers for more resources
Selectively fluorinated compounds are found frequently in pharmaceutical and agrochemical products where currently 25-30 % of optimised compounds emerge from development containing at least one fluorine atom. There are many methods for the site-specific introduction of fluorine, but all are chemical and they often use environmentally challenging reagents. Biochemical processes for C-F bond formation are attractive, but they are extremely rare. In this work, the fluorinase enzyme, originally identified from the actinomycete bacterium Streptomyces cattleya, is engineered into Escherichia coli in such a manner that the organism is able to produce 5 '-fluorodeoxyadenosine (5 '-FDA) from S-adenosyl-l-methionine (SAM) and fluoride in live E. coli cells. Success required the introduction of a SAM transporter and deletion of the endogenous fluoride efflux capacity in order to generate an E. coli host that has the potential for future engineering of more elaborate fluorometabolites.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available