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"We examined how these #flavonoids are #oxidized by human #P450 family 1 and 2A #enzymes. Naringenin was principally oxidized at the 3′-position to form eriodictyol by CYP1 enzymes more efficiently than by CYP2A enzymes, and the resulting eriodictyol was further oxidized to two penta-hydroxylated products. In contrast to plant P450 enzymes, these human P450s did not mediate the desaturation of naringenin and eriodictyol to give apigenin and luteolin, respectively."

https://pubs.acs.org/doi/10.1021/acs.chemrestox.3c00229

Optimizing cytochrome P450 network for high-level production of quillaic acid

Researchers from the Shenzhen Institute of Advanced Technology of the Chinese Academy of Sciences have developed a combinatorial optimization approach to construct and spatially control a cytochrome P450-cytochrome P450 reductase (CYP-CPR) network in an engineered Saccharomyces cerevisiae strain to boost quillaic acid production.

Phys.org
Study identifies new levers for controlling plant biochemistry

Plant biochemists at the U.S. Department of Energy's Brookhaven National Laboratory have discovered a new level of regulation in the biochemical "machinery" that plants use to convert organic carbon derived from photosynthesis into a range of ring-shaped aromatic molecules. The research, just published in the journal Science Advances, suggests new strategies for controlling plant biochemistry for agricultural and industrial applications.