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Protein engineering

This tag is associated with 4 posts

“Research Highlight” in Nature Chemistry

Our recently published article in JACS on engineering enantioselectivity in DFPase is now a “Research Highlight” in Nature Chemistry. The article is publicly available but a nature account is required.

Reversed Enantioselectivity of DFPase by Rational Design

Based on structural and mechanistic knowledge, mutants of the phosphotriesterase enzmye DFPase were created that reverse the enantioselectivity of the enzyme from the less toxic to the more toxic stereoisomer of G-type nerve agents. The mutants not only feature a reversed enantioselectivity but also increased enzymatic activity compared to the wildtype. The results are described in a new paper published in the Journal of the American Chemical Society (JACS).