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Unlocking a Bacterial Enzyme’s Hidden Potential
A research team led by Professor Toshiki Furuya from Tokyo University of Science has successfully characterized the previously uncharacterized cytochrome P450 enzyme CYP107J1 from Bacillus subtilis strain 168.
By introducing two targeted amino acid mutations, the team converted CYP107J1 into a peroxygenase. This engineered form uses hydrogen peroxide directly, eliminating the need for redox partner proteins entirely.
This approach provides a template for characterizing other orphan P450 enzymes without identifying their natural redox partners.
The results are striking. The engineered enzyme showed 28-fold higher catalytic activity toward 4-hexylbenzoic acid compared to the wild-type enzyme with substitute redox partners.
In a separate application, the modified enzyme also converted indole into indigo with high efficiency, broadening its potential industrial usefulness.
Why this matters: These findings offer a practical template for studying other orphan P450 enzymes, which often remain uncharacterized precisely because their natural redox partners are unknown.