Reprogramming the Rossmann fold signature motif creates orthogonal redox biocatalysts
Oct, 13, 2026
Congratulations to Minh Anh and the entire team on their new publication, “Reprogramming the Rossmann fold signature motif creates orthogonal redox biocatalysts,” published in Nature Communications!
The study presents a strategy for engineering enzymes to use NMN(H), an alternative redox cofactor. By redesigning the conserved Rossmann-fold motif, the team created orthogonal enzymes that minimize interference with natural cofactors. The engineered phosphite dehydrogenases achieved approximately 240-fold greater productivity than previous catalysts, and the approach was successfully demonstrated across 12 diverse enzymes.
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Ping Y, Kim JY, Dinh ML, Luu E, Worakaensai S, Zhang S, Black WB, Monge E, Ng HJC, Perea S, Zhang Y, Cui Y, King E, Siegel JB, and Li H. Reprogramming the Rossmann fold signature motif creates orthogonal redox biocatalysts. Nature Communications, 2026. https://doi.org/10.1038/s41467-026-77633-7