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Expression of a soluble flavone synthase allows the biosynthesis of phytoestrogen derivatives in Escherichia coli

  • Applied Genetics and Molecular Biotechnology
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Abstract

Flavones are plant secondary metabolites with potent pharmacological properties. We report the functional expression of FSI, a flavonoid 2-oxoglutarate-dependent dioxygenase-encoding flavone synthase from parsley in Escherichia coli. This expression allows the biosynthesis of various flavones from phenylpropanoid acids in recombinant E. coli strains simultaneously expressing five plant-specific flavone biosynthetic genes. The gene ensemble consists of 4CL-2 (4-coumarate:CoA ligase) and FSI (flavone synthase I) from parsley, chsA (chalcone synthase) and chiA (chalcone isomerase) from Petunia hybrida, and OMT1A (7-O-methyltransferase) from peppermint. After a 24-h cultivation, the recombinant E. coli produces significant amounts of apigenin (415 μg/l), luteolin (10 μg/l), and genkwanin (208 μg/l). The majority of the flavone products are excreted in the culture media; however, 25% is contained within the cells. The metabolic engineering strategy presented demonstrates that plant-specific flavones are successfully produced in E. coli for the first time by incorporating a soluble flavone synthase confined only in Apiaceae.

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Acknowledgements

This work was supported by a research grant from the US National Science Foundation (BES-0331404) to M.A.G. Koffas.

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Correspondence to Mattheos A. G. Koffas.

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Leonard, E., Chemler, J., Lim, K.H. et al. Expression of a soluble flavone synthase allows the biosynthesis of phytoestrogen derivatives in Escherichia coli . Appl Microbiol Biotechnol 70, 85–91 (2006). https://doi.org/10.1007/s00253-005-0059-x

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  • DOI: https://doi.org/10.1007/s00253-005-0059-x

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