Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution

Our VP Technology Development and Commercialisation, Tom Moody, recently contributed to a published article in Nature Communications entitled, “Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution.”
The article suggests, “Engineering artificial enzymes with high activity and catalytic mechanism different from naturally occurring enzymes is a challenge in protein design. For example, many attempts have been made to obtain active hydrolases by introducing a Ser→Cys exchange at the respective catalytic triads, but this generally induced a breakdown of activity. We now report that this long-standing dogma no longer pertains, provided additional mutations are introduced by directed evolution.”