Communications of the ACM
Computer Redesigns Enzyme
University of Groningen biotechnologists used a computational method to redesign aspartase and convert it to a catalyst for asymmetric hydroamination reactions.
Credit: Hein Wijma/University of Groningen
Using a computational method, biotechnologists at the University of Groningen in the Netherlands redesigned aspartase and converted it to a catalyst for asymmetric hydroamination reactions.
Fellow researchers at the Chinese Academy of Sciences scaled up the enzyme's production and created kilograms of pure building blocks for pharmaceuticals and other bioactive compounds.
Modifying enzymes is labor-intensive and can require testing thousands of enzyme variants in multiple rounds. A more efficient approach would be to make a rational design of the required changes based on information on the enzyme's structure and properties, but even this leads to a huge matrix of protein structures, explains University of Groningen's Hein Wijma.
To speed up this process, the researchers used an extremely fast Monte Carlo search algorithm that seeks trends in the enzyme's reactivity. Performing the search took a couple of days in a dedicated computer cluster at the university.
The method achieved substrate conversions of 99% with a 99% enantioselectivity in quantities up to one kilogram, proving that the method works for producing useful enzymes.
From University of Groningen
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